BRENDA - Enzyme Database
show all sequences of 1.1.1.34

Determination of 3-hydroxy-3-methylglutaryl CoA reductase activity in plants

Campos, N.; Arro, M.; Ferrer, A.; Boronat, A.; Methods Mol. Biol. 1153, 21-40 (2014) View publication on PubMed

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
DTT
-
Vigna radiata var. radiata
DTT
-
Hordeum vulgare
DTT
-
Spinacia oleracea
DTT
-
Pisum sativum
DTT
-
Zea mays
DTT
-
Solanum tuberosum
DTT
-
Nicotiana tabacum
DTT
-
Glycine max
DTT
-
Lithospermum erythrorhizon
DTT
-
Arabidopsis thaliana
DTT
-
Picea abies
DTT
-
Brassica napus
DTT
-
Arachis hypogaea
DTT
-
Medicago sativa
DTT
-
Daucus carota
DTT
-
Solanum lycopersicum
DTT
-
Helianthus tuberosus
DTT
-
Raphanus sativus
DTT
-
Gossypium hirsutum
DTT
-
Ochromonas malhamensis
DTT
-
Hevea brasiliensis
DTT
-
Persea americana
DTT
-
Cucumis melo
DTT
-
Cannabis sativa
DTT
-
Sinapis alba
DTT
-
Ipomoea batatas
DTT
-
Malus domestica
DTT
-
Dunaliella salina
DTT
-
Euphorbia lathyris
DTT
-
Nepeta cataria
DTT
-
Pimpinella anisum
DTT
-
Parthenium argentatum
DTT
-
Gossypium barbadense
DTT
-
Artemisia annua
DTT
-
Nicotiana benthamiana
DTT
-
Stevia rebaudiana
DTT
-
Salvia miltiorrhiza
DTT
-
Taraxacum brevicorniculatum
DTT
-
Solanum virginianum
DTT
-
Bixa orellana
EDTA
increases the apparent HMGR activity in sweet potato extracts
Ipomoea batatas
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
inhibits the subsequent reactions of the mevalonate pathway in Hevea latex
Hevea brasiliensis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
-
Vigna radiata var. radiata
5789
-
endoplasmic reticulum membrane
-
Hordeum vulgare
5789
-
endoplasmic reticulum membrane
-
Spinacia oleracea
5789
-
endoplasmic reticulum membrane
-
Pisum sativum
5789
-
endoplasmic reticulum membrane
-
Zea mays
5789
-
endoplasmic reticulum membrane
-
Solanum tuberosum
5789
-
endoplasmic reticulum membrane
-
Nicotiana tabacum
5789
-
endoplasmic reticulum membrane
-
Glycine max
5789
-
endoplasmic reticulum membrane
-
Lithospermum erythrorhizon
5789
-
endoplasmic reticulum membrane
-
Picea abies
5789
-
endoplasmic reticulum membrane
-
Brassica napus
5789
-
endoplasmic reticulum membrane
-
Arachis hypogaea
5789
-
endoplasmic reticulum membrane
-
Medicago sativa
5789
-
endoplasmic reticulum membrane
-
Daucus carota
5789
-
endoplasmic reticulum membrane
-
Solanum lycopersicum
5789
-
endoplasmic reticulum membrane
-
Helianthus tuberosus
5789
-
endoplasmic reticulum membrane
-
Raphanus sativus
5789
-
endoplasmic reticulum membrane
-
Gossypium hirsutum
5789
-
endoplasmic reticulum membrane
-
Ochromonas malhamensis
5789
-
endoplasmic reticulum membrane
-
Hevea brasiliensis
5789
-
endoplasmic reticulum membrane
-
Persea americana
5789
-
endoplasmic reticulum membrane
-
Cucumis melo
5789
-
endoplasmic reticulum membrane
-
Cannabis sativa
5789
-
endoplasmic reticulum membrane
-
Sinapis alba
5789
-
endoplasmic reticulum membrane
-
Ipomoea batatas
5789
-
endoplasmic reticulum membrane
-
Malus domestica
5789
-
endoplasmic reticulum membrane
-
Dunaliella salina
5789
-
endoplasmic reticulum membrane
-
Euphorbia lathyris
5789
-
endoplasmic reticulum membrane
-
Nepeta cataria
5789
-
endoplasmic reticulum membrane
-
Pimpinella anisum
5789
-
endoplasmic reticulum membrane
-
Parthenium argentatum
5789
-
endoplasmic reticulum membrane
-
Gossypium barbadense
5789
-
endoplasmic reticulum membrane
-
Artemisia annua
5789
-
endoplasmic reticulum membrane
-
Nicotiana benthamiana
5789
-
endoplasmic reticulum membrane
-
Stevia rebaudiana
5789
-
endoplasmic reticulum membrane
-
Salvia miltiorrhiza
5789
-
endoplasmic reticulum membrane
-
Taraxacum brevicorniculatum
5789
-
endoplasmic reticulum membrane
-
Solanum virginianum
5789
-
endoplasmic reticulum membrane
-
Bixa orellana
5789
-
endoplasmic reticulum membrane
the enzyme spans the endoplasmic reticulum membrane twice. Both the N-terminal region and the highly conserved catalytic domain are in the cytosol, whereas only a short stretch of the protein is in the endoplasmic reticulum lumen. Insertion in the endoplasmic reticulum membrane is mediated by the signal recognition particle (SRP) that recognizes the two hydrophobic sequences which will become membrane spanning segments
Arabidopsis thaliana
5789
-
microsome
the HMGR activity is detected in the final microsomal pellet after ultracentrifugation
Arabidopsis thaliana
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Vigna radiata var. radiata
Ca2+
activates
Hordeum vulgare
Ca2+
activates
Spinacia oleracea
Ca2+
activates
Pisum sativum
Ca2+
activates
Zea mays
Ca2+
activates
Solanum tuberosum
Ca2+
activates
Nicotiana tabacum
Ca2+
activates
Glycine max
Ca2+
activates
Lithospermum erythrorhizon
Ca2+
activates
Arabidopsis thaliana
Ca2+
activates
Picea abies
Ca2+
activates
Brassica napus
Ca2+
activates
Arachis hypogaea
Ca2+
activates
Medicago sativa
Ca2+
activates
Daucus carota
Ca2+
activates
Solanum lycopersicum
Ca2+
activates
Helianthus tuberosus
Ca2+
activates
Raphanus sativus
Ca2+
activates
Gossypium hirsutum
Ca2+
activates
Ochromonas malhamensis
Ca2+
activates
Hevea brasiliensis
Ca2+
activates
Persea americana
Ca2+
activates
Cucumis melo
Ca2+
activates
Cannabis sativa
Ca2+
activates
Sinapis alba
Ca2+
activates
Ipomoea batatas
Ca2+
activates
Malus domestica
Ca2+
activates
Dunaliella salina
Ca2+
activates
Euphorbia lathyris
Ca2+
activates
Nepeta cataria
Ca2+
activates
Pimpinella anisum
Ca2+
activates
Parthenium argentatum
Ca2+
activates
Gossypium barbadense
Ca2+
activates
Artemisia annua
Ca2+
activates
Nicotiana benthamiana
Ca2+
activates
Stevia rebaudiana
Ca2+
activates
Salvia miltiorrhiza
Ca2+
activates
Taraxacum brevicorniculatum
Ca2+
activates
Solanum virginianum
Ca2+
activates
Bixa orellana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(R)-mevalonate + CoA + 2 NADP+
Vigna radiata var. radiata
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Hordeum vulgare
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Spinacia oleracea
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Pisum sativum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Zea mays
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Solanum tuberosum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Nicotiana tabacum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Glycine max
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Lithospermum erythrorhizon
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Arabidopsis thaliana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Picea abies
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Brassica napus
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Arachis hypogaea
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Medicago sativa
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Daucus carota
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Solanum lycopersicum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Helianthus tuberosus
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Raphanus sativus
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Gossypium hirsutum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Ochromonas malhamensis
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Hevea brasiliensis
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Persea americana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Cucumis melo
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Cannabis sativa
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Sinapis alba
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Ipomoea batatas
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Malus domestica
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Dunaliella salina
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Euphorbia lathyris
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Nepeta cataria
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Pimpinella anisum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Parthenium argentatum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Gossypium barbadense
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Artemisia annua
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Nicotiana benthamiana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Stevia rebaudiana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Salvia miltiorrhiza
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Taraxacum brevicorniculatum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Solanum virginianum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Bixa orellana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Vigna radiata var. radiata
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Hordeum vulgare
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Spinacia oleracea
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Pisum sativum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Zea mays
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Solanum tuberosum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Nicotiana tabacum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Glycine max
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Lithospermum erythrorhizon
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Arabidopsis thaliana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Picea abies
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Brassica napus
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Arachis hypogaea
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Medicago sativa
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Daucus carota
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Solanum lycopersicum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Helianthus tuberosus
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Raphanus sativus
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Gossypium hirsutum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ochromonas malhamensis
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Hevea brasiliensis
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Persea americana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Cucumis melo
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Cannabis sativa
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Sinapis alba
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ipomoea batatas
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Malus domestica
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Dunaliella salina
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Euphorbia lathyris
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Nepeta cataria
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Pimpinella anisum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Parthenium argentatum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Gossypium barbadense
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Artemisia annua
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Nicotiana benthamiana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Stevia rebaudiana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Salvia miltiorrhiza
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Taraxacum brevicorniculatum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Solanum virginianum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Bixa orellana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Arabidopsis thaliana
-
-
-
Arachis hypogaea
-
-
-
Artemisia annua
-
-
-
Bixa orellana
-
-
-
Brassica napus
-
-
-
Cannabis sativa
-
-
-
Cucumis melo
-
-
-
Daucus carota
-
-
-
Dunaliella salina
-
-
-
Euphorbia lathyris
-
-
-
Glycine max
-
-
-
Gossypium barbadense
-
-
-
Gossypium hirsutum
-
-
-
Helianthus tuberosus
-
-
-
Hevea brasiliensis
-
-
-
Hordeum vulgare
-
-
-
Ipomoea batatas
-
-
-
Lithospermum erythrorhizon
-
-
-
Malus domestica
-
-
-
Medicago sativa
-
-
-
Nepeta cataria
-
-
-
Nicotiana benthamiana
-
-
-
Nicotiana tabacum
-
-
-
Ochromonas malhamensis
-
-
-
Parthenium argentatum
-
-
-
Persea americana
-
-
-
Picea abies
-
-
-
Pimpinella anisum
-
-
-
Pisum sativum
-
-
-
Raphanus sativus
-
-
-
Salvia miltiorrhiza
-
-
-
Sinapis alba
-
-
-
Solanum lycopersicum
-
-
-
Solanum tuberosum
-
-
-
Solanum virginianum
-
-
-
Spinacia oleracea
-
-
-
Stevia rebaudiana
-
-
-
Taraxacum brevicorniculatum
-
-
-
Vigna radiata var. radiata
-
-
-
Zea mays
-
-
-
Oxidation Stability
Oxidation Stability
Organism
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Vigna radiata var. radiata
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Hordeum vulgare
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Spinacia oleracea
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Pisum sativum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Zea mays
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Solanum tuberosum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Nicotiana tabacum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Glycine max
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Lithospermum erythrorhizon
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Arabidopsis thaliana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Picea abies
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Brassica napus
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Arachis hypogaea
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Medicago sativa
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Daucus carota
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Solanum lycopersicum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Helianthus tuberosus
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Raphanus sativus
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Gossypium hirsutum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Ochromonas malhamensis
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Hevea brasiliensis
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Persea americana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Cucumis melo
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Cannabis sativa
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Sinapis alba
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Ipomoea batatas
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Malus domestica
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Dunaliella salina
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Euphorbia lathyris
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Nepeta cataria
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Pimpinella anisum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Parthenium argentatum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Gossypium barbadense
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Artemisia annua
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Nicotiana benthamiana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Stevia rebaudiana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Salvia miltiorrhiza
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Taraxacum brevicorniculatum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Solanum virginianum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Bixa orellana
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Vigna radiata var. radiata
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Hordeum vulgare
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Spinacia oleracea
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Pisum sativum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Zea mays
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Solanum tuberosum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Nicotiana tabacum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Glycine max
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Lithospermum erythrorhizon
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Arabidopsis thaliana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Picea abies
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Brassica napus
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Arachis hypogaea
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Medicago sativa
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Daucus carota
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Solanum lycopersicum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Helianthus tuberosus
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Raphanus sativus
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Gossypium hirsutum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Ochromonas malhamensis
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Hevea brasiliensis
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Persea americana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Cucumis melo
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Cannabis sativa
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Sinapis alba
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Ipomoea batatas
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Malus domestica
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Dunaliella salina
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Euphorbia lathyris
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Nepeta cataria
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Pimpinella anisum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Parthenium argentatum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Gossypium barbadense
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Artemisia annua
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Nicotiana benthamiana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Stevia rebaudiana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Salvia miltiorrhiza
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Taraxacum brevicorniculatum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Solanum virginianum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Bixa orellana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Vigna radiata var. radiata
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Hordeum vulgare
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Spinacia oleracea
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Pisum sativum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Zea mays
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Solanum tuberosum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Nicotiana tabacum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Glycine max
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Lithospermum erythrorhizon
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Arabidopsis thaliana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Picea abies
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Brassica napus
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Arachis hypogaea
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Medicago sativa
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Daucus carota
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Solanum lycopersicum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Helianthus tuberosus
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Raphanus sativus
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Gossypium hirsutum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Ochromonas malhamensis
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Hevea brasiliensis
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Persea americana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Cucumis melo
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Cannabis sativa
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Sinapis alba
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Ipomoea batatas
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Malus domestica
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Dunaliella salina
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Euphorbia lathyris
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Nepeta cataria
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Pimpinella anisum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Parthenium argentatum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Gossypium barbadense
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Artemisia annua
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Nicotiana benthamiana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Stevia rebaudiana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Salvia miltiorrhiza
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Taraxacum brevicorniculatum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Solanum virginianum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Bixa orellana
Purification (Commentary)
Purification (Commentary)
Organism
native enzyme by ultracentrifugation
Arabidopsis thaliana
Source Tissue
Source Tissue
Commentary
Organism
Textmining
bark
-
Parthenium argentatum
-
BY-2 cell
-
Nicotiana tabacum
-
callus
-
Nicotiana tabacum
-
callus
-
Picea abies
-
callus
-
Nepeta cataria
-
callus
-
Bixa orellana
-
cell culture
-
Nicotiana tabacum
-
cell culture
-
Glycine max
-
cell culture
-
Lithospermum erythrorhizon
-
cell culture
-
Picea abies
-
cell culture
-
Daucus carota
-
cell culture
-
Ochromonas malhamensis
-
cell culture
-
Dunaliella salina
-
cell culture
-
Pimpinella anisum
-
cell suspension culture
-
Solanum virginianum
-
cotyledon
-
Glycine max
-
exocarp
-
Malus domestica
-
fruit
-
Solanum lycopersicum
-
fruit
-
Cucumis melo
-
hairy root
-
Lithospermum erythrorhizon
-
hairy root
-
Medicago sativa
-
hairy root
-
Salvia miltiorrhiza
-
hypocotyl
-
Glycine max
-
KY-14 cell
-
Nicotiana tabacum
-
latex
-
Hevea brasiliensis
-
latex
-
Euphorbia lathyris
-
latex
-
Taraxacum brevicorniculatum
-
leaf
-
Vigna radiata var. radiata
-
leaf
-
Spinacia oleracea
-
leaf
-
Picea abies
-
leaf
-
Solanum lycopersicum
-
leaf
-
Cannabis sativa
-
leaf
-
Euphorbia lathyris
-
leaf
-
Nepeta cataria
-
leaf
-
Artemisia annua
-
leaf
-
Nicotiana benthamiana
-
leaf
-
Stevia rebaudiana
-
leaf
-
Bixa orellana
-
leaf
expanded
Nicotiana tabacum
-
leaf
fully expanded
Parthenium argentatum
-
leaf
rosette leaves and fully expanded leaves
Arabidopsis thaliana
-
mesocarp
-
Persea americana
-
pericarp
-
Cucumis melo
-
root
-
Glycine max
-
root
-
Ipomoea batatas
-
seed
-
Arabidopsis thaliana
-
seed
-
Persea americana
-
seed
developing
Nicotiana tabacum
-
seed
developing
Brassica napus
-
seedling
-
Hordeum vulgare
-
seedling
-
Picea abies
-
seedling
-
Raphanus sativus
-
seedling
etiolated
Zea mays
-
seedling
green
Arachis hypogaea
-
seedling
green
Sinapis alba
-
seedling
aerial part and full seedling
Nicotiana tabacum
-
seedling
apical part
Glycine max
-
seedling
etiolated and green seedlings
Pisum sativum
-
seedling
green seedling, aerial part and root
Arabidopsis thaliana
-
stele
-
Gossypium hirsutum
-
stele
-
Gossypium barbadense
-
stem
-
Euphorbia lathyris
-
stem
lower
Parthenium argentatum
-
tuber
-
Solanum tuberosum
-
tuber
explants
Helianthus tuberosus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(R)-mevalonate + CoA + 2 NADP+
-
740956
Vigna radiata var. radiata
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Hordeum vulgare
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Spinacia oleracea
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Pisum sativum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Zea mays
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Solanum tuberosum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Nicotiana tabacum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Glycine max
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Lithospermum erythrorhizon
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Arabidopsis thaliana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Picea abies
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Brassica napus
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Arachis hypogaea
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Medicago sativa
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Daucus carota
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Solanum lycopersicum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Helianthus tuberosus
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Raphanus sativus
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Gossypium hirsutum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Ochromonas malhamensis
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Hevea brasiliensis
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Persea americana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Cucumis melo
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Cannabis sativa
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Sinapis alba
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Ipomoea batatas
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Malus domestica
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Dunaliella salina
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Euphorbia lathyris
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Nepeta cataria
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Pimpinella anisum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Parthenium argentatum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Gossypium barbadense
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Artemisia annua
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Nicotiana benthamiana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Stevia rebaudiana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Salvia miltiorrhiza
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Taraxacum brevicorniculatum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Solanum virginianum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Bixa orellana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Vigna radiata var. radiata
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Hordeum vulgare
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Spinacia oleracea
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Pisum sativum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Zea mays
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Solanum tuberosum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Nicotiana tabacum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Glycine max
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Lithospermum erythrorhizon
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Arabidopsis thaliana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Picea abies
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Brassica napus
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Arachis hypogaea
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Medicago sativa
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Daucus carota
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Solanum lycopersicum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Helianthus tuberosus
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Raphanus sativus
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Gossypium hirsutum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Ochromonas malhamensis
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Hevea brasiliensis
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Persea americana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Cucumis melo
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Cannabis sativa
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Sinapis alba
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Ipomoea batatas
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Malus domestica
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Dunaliella salina
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Euphorbia lathyris
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Nepeta cataria
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Pimpinella anisum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Parthenium argentatum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Gossypium barbadense
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Artemisia annua
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Nicotiana benthamiana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Stevia rebaudiana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Salvia miltiorrhiza
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Taraxacum brevicorniculatum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Solanum virginianum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Bixa orellana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Vigna radiata var. radiata
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Hordeum vulgare
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Spinacia oleracea
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Pisum sativum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Zea mays
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Solanum tuberosum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Nicotiana tabacum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Glycine max
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Lithospermum erythrorhizon
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Arabidopsis thaliana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Picea abies
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Brassica napus
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Arachis hypogaea
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Medicago sativa
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Daucus carota
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Solanum lycopersicum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Helianthus tuberosus
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Raphanus sativus
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Gossypium hirsutum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Ochromonas malhamensis
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Hevea brasiliensis
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Persea americana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Cucumis melo
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Cannabis sativa
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Sinapis alba
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Ipomoea batatas
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Malus domestica
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Dunaliella salina
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Euphorbia lathyris
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Nepeta cataria
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Pimpinella anisum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Parthenium argentatum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Gossypium barbadense
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Artemisia annua
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Nicotiana benthamiana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Stevia rebaudiana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Salvia miltiorrhiza
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Taraxacum brevicorniculatum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Solanum virginianum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Bixa orellana
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 63000-70000
Vigna radiata var. radiata
?
x * 63000-70000
Hordeum vulgare
?
x * 63000-70000
Spinacia oleracea
?
x * 63000-70000
Pisum sativum
?
x * 63000-70000
Zea mays
?
x * 63000-70000
Solanum tuberosum
?
x * 63000-70000
Nicotiana tabacum
?
x * 63000-70000
Glycine max
?
x * 63000-70000
Lithospermum erythrorhizon
?
x * 63000-70000
Arabidopsis thaliana
?
x * 63000-70000
Picea abies
?
x * 63000-70000
Brassica napus
?
x * 63000-70000
Arachis hypogaea
?
x * 63000-70000
Medicago sativa
?
x * 63000-70000
Daucus carota
?
x * 63000-70000
Solanum lycopersicum
?
x * 63000-70000
Helianthus tuberosus
?
x * 63000-70000
Raphanus sativus
?
x * 63000-70000
Gossypium hirsutum
?
x * 63000-70000
Ochromonas malhamensis
?
x * 63000-70000
Hevea brasiliensis
?
x * 63000-70000
Persea americana
?
x * 63000-70000
Cucumis melo
?
x * 63000-70000
Cannabis sativa
?
x * 63000-70000
Sinapis alba
?
x * 63000-70000
Ipomoea batatas
?
x * 63000-70000
Malus domestica
?
x * 63000-70000
Dunaliella salina
?
x * 63000-70000
Euphorbia lathyris
?
x * 63000-70000
Nepeta cataria
?
x * 63000-70000
Pimpinella anisum
?
x * 63000-70000
Parthenium argentatum
?
x * 63000-70000
Gossypium barbadense
?
x * 63000-70000
Artemisia annua
?
x * 63000-70000
Nicotiana benthamiana
?
x * 63000-70000
Stevia rebaudiana
?
x * 63000-70000
Salvia miltiorrhiza
?
x * 63000-70000
Taraxacum brevicorniculatum
?
x * 63000-70000
Solanum virginianum
?
x * 63000-70000
Bixa orellana
Synonyms
Synonyms
Commentary
Organism
3-hydroxy-3-methylglutaryl CoA reductase
-
Vigna radiata var. radiata
3-hydroxy-3-methylglutaryl CoA reductase
-
Hordeum vulgare
3-hydroxy-3-methylglutaryl CoA reductase
-
Spinacia oleracea
3-hydroxy-3-methylglutaryl CoA reductase
-
Pisum sativum
3-hydroxy-3-methylglutaryl CoA reductase
-
Zea mays
3-hydroxy-3-methylglutaryl CoA reductase
-
Solanum tuberosum
3-hydroxy-3-methylglutaryl CoA reductase
-
Nicotiana tabacum
3-hydroxy-3-methylglutaryl CoA reductase
-
Glycine max
3-hydroxy-3-methylglutaryl CoA reductase
-
Lithospermum erythrorhizon
3-hydroxy-3-methylglutaryl CoA reductase
-
Arabidopsis thaliana
3-hydroxy-3-methylglutaryl CoA reductase
-
Picea abies
3-hydroxy-3-methylglutaryl CoA reductase
-
Brassica napus
3-hydroxy-3-methylglutaryl CoA reductase
-
Arachis hypogaea
3-hydroxy-3-methylglutaryl CoA reductase
-
Medicago sativa
3-hydroxy-3-methylglutaryl CoA reductase
-
Daucus carota
3-hydroxy-3-methylglutaryl CoA reductase
-
Solanum lycopersicum
3-hydroxy-3-methylglutaryl CoA reductase
-
Helianthus tuberosus
3-hydroxy-3-methylglutaryl CoA reductase
-
Raphanus sativus
3-hydroxy-3-methylglutaryl CoA reductase
-
Gossypium hirsutum
3-hydroxy-3-methylglutaryl CoA reductase
-
Ochromonas malhamensis
3-hydroxy-3-methylglutaryl CoA reductase
-
Hevea brasiliensis
3-hydroxy-3-methylglutaryl CoA reductase
-
Persea americana
3-hydroxy-3-methylglutaryl CoA reductase
-
Cucumis melo
3-hydroxy-3-methylglutaryl CoA reductase
-
Cannabis sativa
3-hydroxy-3-methylglutaryl CoA reductase
-
Sinapis alba
3-hydroxy-3-methylglutaryl CoA reductase
-
Ipomoea batatas
3-hydroxy-3-methylglutaryl CoA reductase
-
Malus domestica
3-hydroxy-3-methylglutaryl CoA reductase
-
Dunaliella salina
3-hydroxy-3-methylglutaryl CoA reductase
-
Euphorbia lathyris
3-hydroxy-3-methylglutaryl CoA reductase
-
Nepeta cataria
3-hydroxy-3-methylglutaryl CoA reductase
-
Pimpinella anisum
3-hydroxy-3-methylglutaryl CoA reductase
-
Parthenium argentatum
3-hydroxy-3-methylglutaryl CoA reductase
-
Gossypium barbadense
3-hydroxy-3-methylglutaryl CoA reductase
-
Artemisia annua
3-hydroxy-3-methylglutaryl CoA reductase
-
Nicotiana benthamiana
3-hydroxy-3-methylglutaryl CoA reductase
-
Stevia rebaudiana
3-hydroxy-3-methylglutaryl CoA reductase
-
Salvia miltiorrhiza
3-hydroxy-3-methylglutaryl CoA reductase
-
Taraxacum brevicorniculatum
3-hydroxy-3-methylglutaryl CoA reductase
-
Solanum virginianum
3-hydroxy-3-methylglutaryl CoA reductase
-
Bixa orellana
HMGR
-
Vigna radiata var. radiata
HMGR
-
Hordeum vulgare
HMGR
-
Spinacia oleracea
HMGR
-
Pisum sativum
HMGR
-
Zea mays
HMGR
-
Solanum tuberosum
HMGR
-
Nicotiana tabacum
HMGR
-
Glycine max
HMGR
-
Lithospermum erythrorhizon
HMGR
-
Arabidopsis thaliana
HMGR
-
Picea abies
HMGR
-
Brassica napus
HMGR
-
Arachis hypogaea
HMGR
-
Medicago sativa
HMGR
-
Daucus carota
HMGR
-
Solanum lycopersicum
HMGR
-
Helianthus tuberosus
HMGR
-
Raphanus sativus
HMGR
-
Gossypium hirsutum
HMGR
-
Ochromonas malhamensis
HMGR
-
Hevea brasiliensis
HMGR
-
Persea americana
HMGR
-
Cucumis melo
HMGR
-
Cannabis sativa
HMGR
-
Sinapis alba
HMGR
-
Ipomoea batatas
HMGR
-
Malus domestica
HMGR
-
Dunaliella salina
HMGR
-
Euphorbia lathyris
HMGR
-
Nepeta cataria
HMGR
-
Pimpinella anisum
HMGR
-
Parthenium argentatum
HMGR
-
Gossypium barbadense
HMGR
-
Artemisia annua
HMGR
-
Nicotiana benthamiana
HMGR
-
Stevia rebaudiana
HMGR
-
Salvia miltiorrhiza
HMGR
-
Taraxacum brevicorniculatum
HMGR
-
Solanum virginianum
HMGR
-
Bixa orellana
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Vigna radiata var. radiata
37
-
assay at
Hordeum vulgare
37
-
assay at
Spinacia oleracea
37
-
assay at
Pisum sativum
37
-
assay at
Zea mays
37
-
assay at
Solanum tuberosum
37
-
assay at
Nicotiana tabacum
37
-
assay at
Glycine max
37
-
assay at
Lithospermum erythrorhizon
37
-
assay at
Arabidopsis thaliana
37
-
assay at
Picea abies
37
-
assay at
Brassica napus
37
-
assay at
Arachis hypogaea
37
-
assay at
Medicago sativa
37
-
assay at
Daucus carota
37
-
assay at
Solanum lycopersicum
37
-
assay at
Helianthus tuberosus
37
-
assay at
Raphanus sativus
37
-
assay at
Gossypium hirsutum
37
-
assay at
Ochromonas malhamensis
37
-
assay at
Hevea brasiliensis
37
-
assay at
Persea americana
37
-
assay at
Cucumis melo
37
-
assay at
Cannabis sativa
37
-
assay at
Sinapis alba
37
-
assay at
Ipomoea batatas
37
-
assay at
Malus domestica
37
-
assay at
Dunaliella salina
37
-
assay at
Euphorbia lathyris
37
-
assay at
Nepeta cataria
37
-
assay at
Pimpinella anisum
37
-
assay at
Parthenium argentatum
37
-
assay at
Gossypium barbadense
37
-
assay at
Artemisia annua
37
-
assay at
Nicotiana benthamiana
37
-
assay at
Stevia rebaudiana
37
-
assay at
Salvia miltiorrhiza
37
-
assay at
Taraxacum brevicorniculatum
37
-
assay at
Solanum virginianum
37
-
assay at
Bixa orellana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
two pH optima are found, corresponding to HMGR from the heavy or the light fractions: pH 7.0 and pH 75, respectively
Parthenium argentatum
additional information
-
two pH optima are found, corresponding to HMGR from the heavy or the light fractions: pH 7.9 and pH 6.9, respectively
Pisum sativum
6.8
-
-
Hevea brasiliensis
6.9
-
-
Pisum sativum
7
-
-
Parthenium argentatum
7.2
-
assay at
Vigna radiata var. radiata
7.2
-
assay at
Hordeum vulgare
7.2
-
assay at
Spinacia oleracea
7.2
-
assay at
Zea mays
7.2
-
assay at
Solanum tuberosum
7.2
-
assay at
Nicotiana tabacum
7.2
-
assay at
Glycine max
7.2
-
assay at
Lithospermum erythrorhizon
7.2
-
assay at
Arabidopsis thaliana
7.2
-
assay at
Picea abies
7.2
-
assay at
Brassica napus
7.2
-
assay at
Arachis hypogaea
7.2
-
assay at
Medicago sativa
7.2
-
assay at
Daucus carota
7.2
-
assay at
Solanum lycopersicum
7.2
-
assay at
Helianthus tuberosus
7.2
-
assay at
Gossypium hirsutum
7.2
-
assay at
Ochromonas malhamensis
7.2
-
assay at
Persea americana
7.2
-
assay at
Cucumis melo
7.2
-
assay at
Cannabis sativa
7.2
-
assay at
Sinapis alba
7.2
-
assay at
Ipomoea batatas
7.2
-
assay at
Malus domestica
7.2
-
assay at
Dunaliella salina
7.2
-
assay at
Euphorbia lathyris
7.2
-
assay at
Nepeta cataria
7.2
-
assay at
Pimpinella anisum
7.2
-
assay at
Gossypium barbadense
7.2
-
assay at
Artemisia annua
7.2
-
assay at
Nicotiana benthamiana
7.2
-
assay at
Stevia rebaudiana
7.2
-
assay at
Salvia miltiorrhiza
7.2
-
assay at
Taraxacum brevicorniculatum
7.2
-
assay at
Solanum virginianum
7.2
-
assay at
Bixa orellana
7.3
7.5
-
Raphanus sativus
7.5
-
-
Parthenium argentatum
7.9
-
-
Pisum sativum
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Vigna radiata var. radiata
NADP+
-
Hordeum vulgare
NADP+
-
Spinacia oleracea
NADP+
-
Pisum sativum
NADP+
-
Zea mays
NADP+
-
Solanum tuberosum
NADP+
-
Nicotiana tabacum
NADP+
-
Glycine max
NADP+
-
Lithospermum erythrorhizon
NADP+
-
Arabidopsis thaliana
NADP+
-
Picea abies
NADP+
-
Brassica napus
NADP+
-
Arachis hypogaea
NADP+
-
Medicago sativa
NADP+
-
Daucus carota
NADP+
-
Solanum lycopersicum
NADP+
-
Helianthus tuberosus
NADP+
-
Raphanus sativus
NADP+
-
Gossypium hirsutum
NADP+
-
Ochromonas malhamensis
NADP+
-
Hevea brasiliensis
NADP+
-
Persea americana
NADP+
-
Cucumis melo
NADP+
-
Cannabis sativa
NADP+
-
Sinapis alba
NADP+
-
Ipomoea batatas
NADP+
-
Malus domestica
NADP+
-
Dunaliella salina
NADP+
-
Euphorbia lathyris
NADP+
-
Nepeta cataria
NADP+
-
Pimpinella anisum
NADP+
-
Parthenium argentatum
NADP+
-
Gossypium barbadense
NADP+
-
Artemisia annua
NADP+
-
Nicotiana benthamiana
NADP+
-
Stevia rebaudiana
NADP+
-
Salvia miltiorrhiza
NADP+
-
Taraxacum brevicorniculatum
NADP+
-
Solanum virginianum
NADP+
-
Bixa orellana
NADPH
-
Vigna radiata var. radiata
NADPH
-
Hordeum vulgare
NADPH
-
Spinacia oleracea
NADPH
-
Pisum sativum
NADPH
-
Zea mays
NADPH
-
Solanum tuberosum
NADPH
-
Nicotiana tabacum
NADPH
-
Glycine max
NADPH
-
Lithospermum erythrorhizon
NADPH
-
Arabidopsis thaliana
NADPH
-
Picea abies
NADPH
-
Brassica napus
NADPH
-
Arachis hypogaea
NADPH
-
Medicago sativa
NADPH
-
Daucus carota
NADPH
-
Solanum lycopersicum
NADPH
-
Helianthus tuberosus
NADPH
-
Raphanus sativus
NADPH
-
Gossypium hirsutum
NADPH
-
Ochromonas malhamensis
NADPH
-
Hevea brasiliensis
NADPH
-
Persea americana
NADPH
-
Cucumis melo
NADPH
-
Cannabis sativa
NADPH
-
Sinapis alba
NADPH
-
Ipomoea batatas
NADPH
-
Malus domestica
NADPH
-
Dunaliella salina
NADPH
-
Euphorbia lathyris
NADPH
-
Nepeta cataria
NADPH
-
Pimpinella anisum
NADPH
-
Parthenium argentatum
NADPH
-
Gossypium barbadense
NADPH
-
Artemisia annua
NADPH
-
Nicotiana benthamiana
NADPH
-
Stevia rebaudiana
NADPH
-
Salvia miltiorrhiza
NADPH
-
Taraxacum brevicorniculatum
NADPH
-
Solanum virginianum
NADPH
-
Bixa orellana
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
DTT
-
Vigna radiata var. radiata
DTT
-
Hordeum vulgare
DTT
-
Spinacia oleracea
DTT
-
Pisum sativum
DTT
-
Zea mays
DTT
-
Solanum tuberosum
DTT
-
Nicotiana tabacum
DTT
-
Glycine max
DTT
-
Lithospermum erythrorhizon
DTT
-
Arabidopsis thaliana
DTT
-
Picea abies
DTT
-
Brassica napus
DTT
-
Arachis hypogaea
DTT
-
Medicago sativa
DTT
-
Daucus carota
DTT
-
Solanum lycopersicum
DTT
-
Helianthus tuberosus
DTT
-
Raphanus sativus
DTT
-
Gossypium hirsutum
DTT
-
Ochromonas malhamensis
DTT
-
Hevea brasiliensis
DTT
-
Persea americana
DTT
-
Cucumis melo
DTT
-
Cannabis sativa
DTT
-
Sinapis alba
DTT
-
Ipomoea batatas
DTT
-
Malus domestica
DTT
-
Dunaliella salina
DTT
-
Euphorbia lathyris
DTT
-
Nepeta cataria
DTT
-
Pimpinella anisum
DTT
-
Parthenium argentatum
DTT
-
Gossypium barbadense
DTT
-
Artemisia annua
DTT
-
Nicotiana benthamiana
DTT
-
Stevia rebaudiana
DTT
-
Salvia miltiorrhiza
DTT
-
Taraxacum brevicorniculatum
DTT
-
Solanum virginianum
DTT
-
Bixa orellana
EDTA
increases the apparent HMGR activity in sweet potato extracts
Ipomoea batatas
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Vigna radiata var. radiata
NADP+
-
Hordeum vulgare
NADP+
-
Spinacia oleracea
NADP+
-
Pisum sativum
NADP+
-
Zea mays
NADP+
-
Solanum tuberosum
NADP+
-
Nicotiana tabacum
NADP+
-
Glycine max
NADP+
-
Lithospermum erythrorhizon
NADP+
-
Arabidopsis thaliana
NADP+
-
Picea abies
NADP+
-
Brassica napus
NADP+
-
Arachis hypogaea
NADP+
-
Medicago sativa
NADP+
-
Daucus carota
NADP+
-
Solanum lycopersicum
NADP+
-
Helianthus tuberosus
NADP+
-
Raphanus sativus
NADP+
-
Gossypium hirsutum
NADP+
-
Ochromonas malhamensis
NADP+
-
Hevea brasiliensis
NADP+
-
Persea americana
NADP+
-
Cucumis melo
NADP+
-
Cannabis sativa
NADP+
-
Sinapis alba
NADP+
-
Ipomoea batatas
NADP+
-
Malus domestica
NADP+
-
Dunaliella salina
NADP+
-
Euphorbia lathyris
NADP+
-
Nepeta cataria
NADP+
-
Pimpinella anisum
NADP+
-
Parthenium argentatum
NADP+
-
Gossypium barbadense
NADP+
-
Artemisia annua
NADP+
-
Nicotiana benthamiana
NADP+
-
Stevia rebaudiana
NADP+
-
Salvia miltiorrhiza
NADP+
-
Taraxacum brevicorniculatum
NADP+
-
Solanum virginianum
NADP+
-
Bixa orellana
NADPH
-
Vigna radiata var. radiata
NADPH
-
Hordeum vulgare
NADPH
-
Spinacia oleracea
NADPH
-
Pisum sativum
NADPH
-
Zea mays
NADPH
-
Solanum tuberosum
NADPH
-
Nicotiana tabacum
NADPH
-
Glycine max
NADPH
-
Lithospermum erythrorhizon
NADPH
-
Arabidopsis thaliana
NADPH
-
Picea abies
NADPH
-
Brassica napus
NADPH
-
Arachis hypogaea
NADPH
-
Medicago sativa
NADPH
-
Daucus carota
NADPH
-
Solanum lycopersicum
NADPH
-
Helianthus tuberosus
NADPH
-
Raphanus sativus
NADPH
-
Gossypium hirsutum
NADPH
-
Ochromonas malhamensis
NADPH
-
Hevea brasiliensis
NADPH
-
Persea americana
NADPH
-
Cucumis melo
NADPH
-
Cannabis sativa
NADPH
-
Sinapis alba
NADPH
-
Ipomoea batatas
NADPH
-
Malus domestica
NADPH
-
Dunaliella salina
NADPH
-
Euphorbia lathyris
NADPH
-
Nepeta cataria
NADPH
-
Pimpinella anisum
NADPH
-
Parthenium argentatum
NADPH
-
Gossypium barbadense
NADPH
-
Artemisia annua
NADPH
-
Nicotiana benthamiana
NADPH
-
Stevia rebaudiana
NADPH
-
Salvia miltiorrhiza
NADPH
-
Taraxacum brevicorniculatum
NADPH
-
Solanum virginianum
NADPH
-
Bixa orellana
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
inhibits the subsequent reactions of the mevalonate pathway in Hevea latex
Hevea brasiliensis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
-
Vigna radiata var. radiata
5789
-
endoplasmic reticulum membrane
-
Hordeum vulgare
5789
-
endoplasmic reticulum membrane
-
Spinacia oleracea
5789
-
endoplasmic reticulum membrane
-
Pisum sativum
5789
-
endoplasmic reticulum membrane
-
Zea mays
5789
-
endoplasmic reticulum membrane
-
Solanum tuberosum
5789
-
endoplasmic reticulum membrane
-
Nicotiana tabacum
5789
-
endoplasmic reticulum membrane
-
Glycine max
5789
-
endoplasmic reticulum membrane
-
Lithospermum erythrorhizon
5789
-
endoplasmic reticulum membrane
-
Picea abies
5789
-
endoplasmic reticulum membrane
-
Brassica napus
5789
-
endoplasmic reticulum membrane
-
Arachis hypogaea
5789
-
endoplasmic reticulum membrane
-
Medicago sativa
5789
-
endoplasmic reticulum membrane
-
Daucus carota
5789
-
endoplasmic reticulum membrane
-
Solanum lycopersicum
5789
-
endoplasmic reticulum membrane
-
Helianthus tuberosus
5789
-
endoplasmic reticulum membrane
-
Raphanus sativus
5789
-
endoplasmic reticulum membrane
-
Gossypium hirsutum
5789
-
endoplasmic reticulum membrane
-
Ochromonas malhamensis
5789
-
endoplasmic reticulum membrane
-
Hevea brasiliensis
5789
-
endoplasmic reticulum membrane
-
Persea americana
5789
-
endoplasmic reticulum membrane
-
Cucumis melo
5789
-
endoplasmic reticulum membrane
-
Cannabis sativa
5789
-
endoplasmic reticulum membrane
-
Sinapis alba
5789
-
endoplasmic reticulum membrane
-
Ipomoea batatas
5789
-
endoplasmic reticulum membrane
-
Malus domestica
5789
-
endoplasmic reticulum membrane
-
Dunaliella salina
5789
-
endoplasmic reticulum membrane
-
Euphorbia lathyris
5789
-
endoplasmic reticulum membrane
-
Nepeta cataria
5789
-
endoplasmic reticulum membrane
-
Pimpinella anisum
5789
-
endoplasmic reticulum membrane
-
Parthenium argentatum
5789
-
endoplasmic reticulum membrane
-
Gossypium barbadense
5789
-
endoplasmic reticulum membrane
-
Artemisia annua
5789
-
endoplasmic reticulum membrane
-
Nicotiana benthamiana
5789
-
endoplasmic reticulum membrane
-
Stevia rebaudiana
5789
-
endoplasmic reticulum membrane
-
Salvia miltiorrhiza
5789
-
endoplasmic reticulum membrane
-
Taraxacum brevicorniculatum
5789
-
endoplasmic reticulum membrane
-
Solanum virginianum
5789
-
endoplasmic reticulum membrane
-
Bixa orellana
5789
-
endoplasmic reticulum membrane
the enzyme spans the endoplasmic reticulum membrane twice. Both the N-terminal region and the highly conserved catalytic domain are in the cytosol, whereas only a short stretch of the protein is in the endoplasmic reticulum lumen. Insertion in the endoplasmic reticulum membrane is mediated by the signal recognition particle (SRP) that recognizes the two hydrophobic sequences which will become membrane spanning segments
Arabidopsis thaliana
5789
-
microsome
the HMGR activity is detected in the final microsomal pellet after ultracentrifugation
Arabidopsis thaliana
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates
Vigna radiata var. radiata
Ca2+
activates
Hordeum vulgare
Ca2+
activates
Spinacia oleracea
Ca2+
activates
Pisum sativum
Ca2+
activates
Zea mays
Ca2+
activates
Solanum tuberosum
Ca2+
activates
Nicotiana tabacum
Ca2+
activates
Glycine max
Ca2+
activates
Lithospermum erythrorhizon
Ca2+
activates
Arabidopsis thaliana
Ca2+
activates
Picea abies
Ca2+
activates
Brassica napus
Ca2+
activates
Arachis hypogaea
Ca2+
activates
Medicago sativa
Ca2+
activates
Daucus carota
Ca2+
activates
Solanum lycopersicum
Ca2+
activates
Helianthus tuberosus
Ca2+
activates
Raphanus sativus
Ca2+
activates
Gossypium hirsutum
Ca2+
activates
Ochromonas malhamensis
Ca2+
activates
Hevea brasiliensis
Ca2+
activates
Persea americana
Ca2+
activates
Cucumis melo
Ca2+
activates
Cannabis sativa
Ca2+
activates
Sinapis alba
Ca2+
activates
Ipomoea batatas
Ca2+
activates
Malus domestica
Ca2+
activates
Dunaliella salina
Ca2+
activates
Euphorbia lathyris
Ca2+
activates
Nepeta cataria
Ca2+
activates
Pimpinella anisum
Ca2+
activates
Parthenium argentatum
Ca2+
activates
Gossypium barbadense
Ca2+
activates
Artemisia annua
Ca2+
activates
Nicotiana benthamiana
Ca2+
activates
Stevia rebaudiana
Ca2+
activates
Salvia miltiorrhiza
Ca2+
activates
Taraxacum brevicorniculatum
Ca2+
activates
Solanum virginianum
Ca2+
activates
Bixa orellana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(R)-mevalonate + CoA + 2 NADP+
Vigna radiata var. radiata
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Hordeum vulgare
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Spinacia oleracea
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Pisum sativum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Zea mays
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Solanum tuberosum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Nicotiana tabacum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Glycine max
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Lithospermum erythrorhizon
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Arabidopsis thaliana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Picea abies
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Brassica napus
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Arachis hypogaea
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Medicago sativa
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Daucus carota
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Solanum lycopersicum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Helianthus tuberosus
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Raphanus sativus
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Gossypium hirsutum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Ochromonas malhamensis
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Hevea brasiliensis
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Persea americana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Cucumis melo
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Cannabis sativa
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Sinapis alba
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Ipomoea batatas
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Malus domestica
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Dunaliella salina
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Euphorbia lathyris
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Nepeta cataria
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Pimpinella anisum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Parthenium argentatum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Gossypium barbadense
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Artemisia annua
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Nicotiana benthamiana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Stevia rebaudiana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Salvia miltiorrhiza
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Taraxacum brevicorniculatum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Solanum virginianum
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(R)-mevalonate + CoA + 2 NADP+
Bixa orellana
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Vigna radiata var. radiata
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Hordeum vulgare
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Spinacia oleracea
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Pisum sativum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Zea mays
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Solanum tuberosum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Nicotiana tabacum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Glycine max
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Lithospermum erythrorhizon
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Arabidopsis thaliana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Picea abies
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Brassica napus
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Arachis hypogaea
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Medicago sativa
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Daucus carota
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Solanum lycopersicum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Helianthus tuberosus
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Raphanus sativus
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Gossypium hirsutum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ochromonas malhamensis
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Hevea brasiliensis
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Persea americana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Cucumis melo
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Cannabis sativa
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Sinapis alba
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ipomoea batatas
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Malus domestica
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Dunaliella salina
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Euphorbia lathyris
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Nepeta cataria
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Pimpinella anisum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Parthenium argentatum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Gossypium barbadense
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Artemisia annua
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Nicotiana benthamiana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Stevia rebaudiana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Salvia miltiorrhiza
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Taraxacum brevicorniculatum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Solanum virginianum
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Bixa orellana
-
(R)-mevalonate + CoA + 2 NADP+
-
-
r
Oxidation Stability (protein specific)
Oxidation Stability
Organism
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Vigna radiata var. radiata
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Hordeum vulgare
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Spinacia oleracea
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Pisum sativum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Zea mays
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Solanum tuberosum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Nicotiana tabacum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Glycine max
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Lithospermum erythrorhizon
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Arabidopsis thaliana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Picea abies
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Brassica napus
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Arachis hypogaea
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Medicago sativa
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Daucus carota
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Solanum lycopersicum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Helianthus tuberosus
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Raphanus sativus
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Gossypium hirsutum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Ochromonas malhamensis
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Hevea brasiliensis
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Persea americana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Cucumis melo
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Cannabis sativa
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Sinapis alba
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Ipomoea batatas
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Malus domestica
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Dunaliella salina
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Euphorbia lathyris
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Nepeta cataria
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Pimpinella anisum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Parthenium argentatum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Gossypium barbadense
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Artemisia annua
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Nicotiana benthamiana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Stevia rebaudiana
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Salvia miltiorrhiza
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Taraxacum brevicorniculatum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Solanum virginianum
the catalytic activity of plant HMGR depends on free thiol groups and a reducing agent is used to protect their reduced state. DTT is better than 2-mercaptoethanol or glutathione for this purpose
Bixa orellana
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Vigna radiata var. radiata
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Hordeum vulgare
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Spinacia oleracea
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Pisum sativum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Zea mays
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Solanum tuberosum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Nicotiana tabacum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Glycine max
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Lithospermum erythrorhizon
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Arabidopsis thaliana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Picea abies
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Brassica napus
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Arachis hypogaea
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Medicago sativa
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Daucus carota
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Solanum lycopersicum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Helianthus tuberosus
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Raphanus sativus
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Gossypium hirsutum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Ochromonas malhamensis
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Hevea brasiliensis
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Persea americana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Cucumis melo
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Cannabis sativa
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Sinapis alba
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Ipomoea batatas
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Malus domestica
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Dunaliella salina
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Euphorbia lathyris
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Nepeta cataria
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Pimpinella anisum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Parthenium argentatum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Gossypium barbadense
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Artemisia annua
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Nicotiana benthamiana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Stevia rebaudiana
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Salvia miltiorrhiza
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Taraxacum brevicorniculatum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Solanum virginianum
additional information
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
Bixa orellana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Vigna radiata var. radiata
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Hordeum vulgare
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Spinacia oleracea
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Pisum sativum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Zea mays
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Solanum tuberosum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Nicotiana tabacum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Glycine max
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Lithospermum erythrorhizon
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Arabidopsis thaliana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Picea abies
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Brassica napus
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Arachis hypogaea
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Medicago sativa
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Daucus carota
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Solanum lycopersicum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Helianthus tuberosus
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Raphanus sativus
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Gossypium hirsutum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Ochromonas malhamensis
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Hevea brasiliensis
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Persea americana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Cucumis melo
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Cannabis sativa
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Sinapis alba
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Ipomoea batatas
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Malus domestica
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Dunaliella salina
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Euphorbia lathyris
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Nepeta cataria
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Pimpinella anisum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Parthenium argentatum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Gossypium barbadense
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Artemisia annua
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Nicotiana benthamiana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Stevia rebaudiana
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Salvia miltiorrhiza
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Taraxacum brevicorniculatum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Solanum virginianum
phosphoprotein
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
Bixa orellana
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme by ultracentrifugation
Arabidopsis thaliana
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
bark
-
Parthenium argentatum
-
BY-2 cell
-
Nicotiana tabacum
-
callus
-
Nicotiana tabacum
-
callus
-
Picea abies
-
callus
-
Nepeta cataria
-
callus
-
Bixa orellana
-
cell culture
-
Nicotiana tabacum
-
cell culture
-
Glycine max
-
cell culture
-
Lithospermum erythrorhizon
-
cell culture
-
Picea abies
-
cell culture
-
Daucus carota
-
cell culture
-
Ochromonas malhamensis
-
cell culture
-
Dunaliella salina
-
cell culture
-
Pimpinella anisum
-
cell suspension culture
-
Solanum virginianum
-
cotyledon
-
Glycine max
-
exocarp
-
Malus domestica
-
fruit
-
Solanum lycopersicum
-
fruit
-
Cucumis melo
-
hairy root
-
Lithospermum erythrorhizon
-
hairy root
-
Medicago sativa
-
hairy root
-
Salvia miltiorrhiza
-
hypocotyl
-
Glycine max
-
KY-14 cell
-
Nicotiana tabacum
-
latex
-
Hevea brasiliensis
-
latex
-
Euphorbia lathyris
-
latex
-
Taraxacum brevicorniculatum
-
leaf
-
Vigna radiata var. radiata
-
leaf
-
Spinacia oleracea
-
leaf
-
Picea abies
-
leaf
-
Solanum lycopersicum
-
leaf
-
Cannabis sativa
-
leaf
-
Euphorbia lathyris
-
leaf
-
Nepeta cataria
-
leaf
-
Artemisia annua
-
leaf
-
Nicotiana benthamiana
-
leaf
-
Stevia rebaudiana
-
leaf
-
Bixa orellana
-
leaf
expanded
Nicotiana tabacum
-
leaf
fully expanded
Parthenium argentatum
-
leaf
rosette leaves and fully expanded leaves
Arabidopsis thaliana
-
mesocarp
-
Persea americana
-
pericarp
-
Cucumis melo
-
root
-
Glycine max
-
root
-
Ipomoea batatas
-
seed
-
Arabidopsis thaliana
-
seed
-
Persea americana
-
seed
developing
Nicotiana tabacum
-
seed
developing
Brassica napus
-
seedling
-
Hordeum vulgare
-
seedling
-
Picea abies
-
seedling
-
Raphanus sativus
-
seedling
etiolated
Zea mays
-
seedling
green
Arachis hypogaea
-
seedling
green
Sinapis alba
-
seedling
aerial part and full seedling
Nicotiana tabacum
-
seedling
apical part
Glycine max
-
seedling
etiolated and green seedlings
Pisum sativum
-
seedling
green seedling, aerial part and root
Arabidopsis thaliana
-
stele
-
Gossypium hirsutum
-
stele
-
Gossypium barbadense
-
stem
-
Euphorbia lathyris
-
stem
lower
Parthenium argentatum
-
tuber
-
Solanum tuberosum
-
tuber
explants
Helianthus tuberosus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(R)-mevalonate + CoA + 2 NADP+
-
740956
Vigna radiata var. radiata
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Hordeum vulgare
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Spinacia oleracea
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Pisum sativum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Zea mays
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Solanum tuberosum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Nicotiana tabacum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Glycine max
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Lithospermum erythrorhizon
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Arabidopsis thaliana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Picea abies
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Brassica napus
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Arachis hypogaea
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Medicago sativa
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Daucus carota
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Solanum lycopersicum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Helianthus tuberosus
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Raphanus sativus
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Gossypium hirsutum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Ochromonas malhamensis
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Hevea brasiliensis
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Persea americana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Cucumis melo
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Cannabis sativa
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Sinapis alba
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Ipomoea batatas
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Malus domestica
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Dunaliella salina
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Euphorbia lathyris
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Nepeta cataria
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Pimpinella anisum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Parthenium argentatum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Gossypium barbadense
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Artemisia annua
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Nicotiana benthamiana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Stevia rebaudiana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Salvia miltiorrhiza
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Taraxacum brevicorniculatum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Solanum virginianum
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
-
740956
Bixa orellana
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Vigna radiata var. radiata
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Hordeum vulgare
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Spinacia oleracea
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Pisum sativum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Zea mays
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Solanum tuberosum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Nicotiana tabacum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Glycine max
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Lithospermum erythrorhizon
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Arabidopsis thaliana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Picea abies
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Brassica napus
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Arachis hypogaea
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Medicago sativa
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Daucus carota
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Solanum lycopersicum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Helianthus tuberosus
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Raphanus sativus
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Gossypium hirsutum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Ochromonas malhamensis
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Hevea brasiliensis
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Persea americana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Cucumis melo
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Cannabis sativa
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Sinapis alba
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Ipomoea batatas
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Malus domestica
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Dunaliella salina
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Euphorbia lathyris
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Nepeta cataria
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Pimpinella anisum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Parthenium argentatum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Gossypium barbadense
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Artemisia annua
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Nicotiana benthamiana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Stevia rebaudiana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Salvia miltiorrhiza
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Taraxacum brevicorniculatum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Solanum virginianum
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
740956
Bixa orellana
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Vigna radiata var. radiata
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Hordeum vulgare
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Spinacia oleracea
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Pisum sativum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Zea mays
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Solanum tuberosum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Nicotiana tabacum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Glycine max
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Lithospermum erythrorhizon
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Arabidopsis thaliana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Picea abies
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Brassica napus
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Arachis hypogaea
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Medicago sativa
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Daucus carota
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Solanum lycopersicum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Helianthus tuberosus
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Raphanus sativus
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Gossypium hirsutum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Ochromonas malhamensis
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Hevea brasiliensis
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Persea americana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Cucumis melo
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Cannabis sativa
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Sinapis alba
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Ipomoea batatas
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Malus domestica
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Dunaliella salina
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Euphorbia lathyris
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Nepeta cataria
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Pimpinella anisum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Parthenium argentatum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Gossypium barbadense
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Artemisia annua
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Nicotiana benthamiana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Stevia rebaudiana
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Salvia miltiorrhiza
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Taraxacum brevicorniculatum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Solanum virginianum
?
-
-
-
?
additional information
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
740956
Bixa orellana
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 63000-70000
Vigna radiata var. radiata
?
x * 63000-70000
Hordeum vulgare
?
x * 63000-70000
Spinacia oleracea
?
x * 63000-70000
Pisum sativum
?
x * 63000-70000
Zea mays
?
x * 63000-70000
Solanum tuberosum
?
x * 63000-70000
Nicotiana tabacum
?
x * 63000-70000
Glycine max
?
x * 63000-70000
Lithospermum erythrorhizon
?
x * 63000-70000
Arabidopsis thaliana
?
x * 63000-70000
Picea abies
?
x * 63000-70000
Brassica napus
?
x * 63000-70000
Arachis hypogaea
?
x * 63000-70000
Medicago sativa
?
x * 63000-70000
Daucus carota
?
x * 63000-70000
Solanum lycopersicum
?
x * 63000-70000
Helianthus tuberosus
?
x * 63000-70000
Raphanus sativus
?
x * 63000-70000
Gossypium hirsutum
?
x * 63000-70000
Ochromonas malhamensis
?
x * 63000-70000
Hevea brasiliensis
?
x * 63000-70000
Persea americana
?
x * 63000-70000
Cucumis melo
?
x * 63000-70000
Cannabis sativa
?
x * 63000-70000
Sinapis alba
?
x * 63000-70000
Ipomoea batatas
?
x * 63000-70000
Malus domestica
?
x * 63000-70000
Dunaliella salina
?
x * 63000-70000
Euphorbia lathyris
?
x * 63000-70000
Nepeta cataria
?
x * 63000-70000
Pimpinella anisum
?
x * 63000-70000
Parthenium argentatum
?
x * 63000-70000
Gossypium barbadense
?
x * 63000-70000
Artemisia annua
?
x * 63000-70000
Nicotiana benthamiana
?
x * 63000-70000
Stevia rebaudiana
?
x * 63000-70000
Salvia miltiorrhiza
?
x * 63000-70000
Taraxacum brevicorniculatum
?
x * 63000-70000
Solanum virginianum
?
x * 63000-70000
Bixa orellana
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Vigna radiata var. radiata
37
-
assay at
Hordeum vulgare
37
-
assay at
Spinacia oleracea
37
-
assay at
Pisum sativum
37
-
assay at
Zea mays
37
-
assay at
Solanum tuberosum
37
-
assay at
Nicotiana tabacum
37
-
assay at
Glycine max
37
-
assay at
Lithospermum erythrorhizon
37
-
assay at
Arabidopsis thaliana
37
-
assay at
Picea abies
37
-
assay at
Brassica napus
37
-
assay at
Arachis hypogaea
37
-
assay at
Medicago sativa
37
-
assay at
Daucus carota
37
-
assay at
Solanum lycopersicum
37
-
assay at
Helianthus tuberosus
37
-
assay at
Raphanus sativus
37
-
assay at
Gossypium hirsutum
37
-
assay at
Ochromonas malhamensis
37
-
assay at
Hevea brasiliensis
37
-
assay at
Persea americana
37
-
assay at
Cucumis melo
37
-
assay at
Cannabis sativa
37
-
assay at
Sinapis alba
37
-
assay at
Ipomoea batatas
37
-
assay at
Malus domestica
37
-
assay at
Dunaliella salina
37
-
assay at
Euphorbia lathyris
37
-
assay at
Nepeta cataria
37
-
assay at
Pimpinella anisum
37
-
assay at
Parthenium argentatum
37
-
assay at
Gossypium barbadense
37
-
assay at
Artemisia annua
37
-
assay at
Nicotiana benthamiana
37
-
assay at
Stevia rebaudiana
37
-
assay at
Salvia miltiorrhiza
37
-
assay at
Taraxacum brevicorniculatum
37
-
assay at
Solanum virginianum
37
-
assay at
Bixa orellana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
two pH optima are found, corresponding to HMGR from the heavy or the light fractions: pH 7.0 and pH 75, respectively
Parthenium argentatum
additional information
-
two pH optima are found, corresponding to HMGR from the heavy or the light fractions: pH 7.9 and pH 6.9, respectively
Pisum sativum
6.8
-
-
Hevea brasiliensis
6.9
-
-
Pisum sativum
7
-
-
Parthenium argentatum
7.2
-
assay at
Vigna radiata var. radiata
7.2
-
assay at
Hordeum vulgare
7.2
-
assay at
Spinacia oleracea
7.2
-
assay at
Zea mays
7.2
-
assay at
Solanum tuberosum
7.2
-
assay at
Nicotiana tabacum
7.2
-
assay at
Glycine max
7.2
-
assay at
Lithospermum erythrorhizon
7.2
-
assay at
Arabidopsis thaliana
7.2
-
assay at
Picea abies
7.2
-
assay at
Brassica napus
7.2
-
assay at
Arachis hypogaea
7.2
-
assay at
Medicago sativa
7.2
-
assay at
Daucus carota
7.2
-
assay at
Solanum lycopersicum
7.2
-
assay at
Helianthus tuberosus
7.2
-
assay at
Gossypium hirsutum
7.2
-
assay at
Ochromonas malhamensis
7.2
-
assay at
Persea americana
7.2
-
assay at
Cucumis melo
7.2
-
assay at
Cannabis sativa
7.2
-
assay at
Sinapis alba
7.2
-
assay at
Ipomoea batatas
7.2
-
assay at
Malus domestica
7.2
-
assay at
Dunaliella salina
7.2
-
assay at
Euphorbia lathyris
7.2
-
assay at
Nepeta cataria
7.2
-
assay at
Pimpinella anisum
7.2
-
assay at
Gossypium barbadense
7.2
-
assay at
Artemisia annua
7.2
-
assay at
Nicotiana benthamiana
7.2
-
assay at
Stevia rebaudiana
7.2
-
assay at
Salvia miltiorrhiza
7.2
-
assay at
Taraxacum brevicorniculatum
7.2
-
assay at
Solanum virginianum
7.2
-
assay at
Bixa orellana
7.3
7.5
-
Raphanus sativus
7.5
-
-
Parthenium argentatum
7.9
-
-
Pisum sativum
General Information
General Information
Commentary
Organism
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Vigna radiata var. radiata
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Hordeum vulgare
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Spinacia oleracea
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Pisum sativum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Zea mays
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Solanum tuberosum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Nicotiana tabacum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Glycine max
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Lithospermum erythrorhizon
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Arabidopsis thaliana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Picea abies
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Brassica napus
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Arachis hypogaea
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Medicago sativa
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Daucus carota
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Solanum lycopersicum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Helianthus tuberosus
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Raphanus sativus
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Gossypium hirsutum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Ochromonas malhamensis
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Hevea brasiliensis
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Persea americana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Cucumis melo
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Cannabis sativa
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Sinapis alba
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Ipomoea batatas
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Malus domestica
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Dunaliella salina
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Euphorbia lathyris
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Nepeta cataria
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Pimpinella anisum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Parthenium argentatum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Gossypium barbadense
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Artemisia annua
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Nicotiana benthamiana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Stevia rebaudiana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Salvia miltiorrhiza
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Taraxacum brevicorniculatum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Solanum virginianum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Bixa orellana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Vigna radiata var. radiata
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Hordeum vulgare
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Spinacia oleracea
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Pisum sativum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Zea mays
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Solanum tuberosum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Nicotiana tabacum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Glycine max
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Lithospermum erythrorhizon
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Arabidopsis thaliana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Picea abies
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Brassica napus
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Arachis hypogaea
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Medicago sativa
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Daucus carota
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Solanum lycopersicum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Helianthus tuberosus
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Raphanus sativus
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Gossypium hirsutum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Ochromonas malhamensis
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Hevea brasiliensis
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Persea americana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Cucumis melo
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Cannabis sativa
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Sinapis alba
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Ipomoea batatas
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Malus domestica
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Dunaliella salina
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Euphorbia lathyris
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Nepeta cataria
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Pimpinella anisum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Parthenium argentatum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Gossypium barbadense
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Artemisia annua
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Nicotiana benthamiana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Stevia rebaudiana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Salvia miltiorrhiza
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Taraxacum brevicorniculatum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Solanum virginianum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Bixa orellana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Vigna radiata var. radiata
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Hordeum vulgare
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Spinacia oleracea
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Pisum sativum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Zea mays
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Solanum tuberosum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Nicotiana tabacum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Glycine max
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Lithospermum erythrorhizon
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Picea abies
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Brassica napus
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Arachis hypogaea
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Medicago sativa
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Daucus carota
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Solanum lycopersicum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Helianthus tuberosus
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Raphanus sativus
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Gossypium hirsutum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Ochromonas malhamensis
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Hevea brasiliensis
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Persea americana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Cucumis melo
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Cannabis sativa
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Sinapis alba
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Ipomoea batatas
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Malus domestica
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Dunaliella salina
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Euphorbia lathyris
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Nepeta cataria
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Pimpinella anisum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Parthenium argentatum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Gossypium barbadense
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Artemisia annua
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Nicotiana benthamiana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Stevia rebaudiana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Salvia miltiorrhiza
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Taraxacum brevicorniculatum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Solanum virginianum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Bixa orellana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated. Protein phosphatase 2A (PP2A) is both a transcriptional and a posttranslational regulator of HMGR in Arabidopsis thaliana
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Vigna radiata var. radiata
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Hordeum vulgare
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Spinacia oleracea
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Pisum sativum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Zea mays
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Solanum tuberosum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Nicotiana tabacum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Glycine max
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Lithospermum erythrorhizon
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Arabidopsis thaliana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Picea abies
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Brassica napus
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Arachis hypogaea
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Medicago sativa
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Daucus carota
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Solanum lycopersicum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Helianthus tuberosus
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Raphanus sativus
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Gossypium hirsutum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Ochromonas malhamensis
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Hevea brasiliensis
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Persea americana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Cucumis melo
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Cannabis sativa
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Sinapis alba
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Ipomoea batatas
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Malus domestica
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Dunaliella salina
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Euphorbia lathyris
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Nepeta cataria
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Pimpinella anisum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Parthenium argentatum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Gossypium barbadense
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Artemisia annua
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Nicotiana benthamiana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Stevia rebaudiana
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Salvia miltiorrhiza
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Taraxacum brevicorniculatum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Solanum virginianum
evolution
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
Bixa orellana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Vigna radiata var. radiata
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Hordeum vulgare
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Spinacia oleracea
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Pisum sativum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Zea mays
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Solanum tuberosum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Nicotiana tabacum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Glycine max
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Lithospermum erythrorhizon
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Arabidopsis thaliana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Picea abies
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Brassica napus
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Arachis hypogaea
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Medicago sativa
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Daucus carota
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Solanum lycopersicum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Helianthus tuberosus
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Raphanus sativus
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Gossypium hirsutum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Ochromonas malhamensis
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Hevea brasiliensis
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Persea americana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Cucumis melo
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Cannabis sativa
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Sinapis alba
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Ipomoea batatas
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Malus domestica
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Dunaliella salina
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Euphorbia lathyris
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Nepeta cataria
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Pimpinella anisum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Parthenium argentatum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Gossypium barbadense
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Artemisia annua
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Nicotiana benthamiana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Stevia rebaudiana
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Salvia miltiorrhiza
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Taraxacum brevicorniculatum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Solanum virginianum
metabolism
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
Bixa orellana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Vigna radiata var. radiata
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Hordeum vulgare
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Spinacia oleracea
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Pisum sativum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Zea mays
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Solanum tuberosum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Nicotiana tabacum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Glycine max
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Lithospermum erythrorhizon
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Picea abies
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Brassica napus
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Arachis hypogaea
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Medicago sativa
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Daucus carota
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Solanum lycopersicum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Helianthus tuberosus
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Raphanus sativus
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Gossypium hirsutum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Ochromonas malhamensis
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Hevea brasiliensis
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Persea americana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Cucumis melo
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Cannabis sativa
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Sinapis alba
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Ipomoea batatas
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Malus domestica
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Dunaliella salina
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Euphorbia lathyris
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Nepeta cataria
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Pimpinella anisum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Parthenium argentatum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Gossypium barbadense
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Artemisia annua
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Nicotiana benthamiana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Stevia rebaudiana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Salvia miltiorrhiza
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Taraxacum brevicorniculatum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Solanum virginianum
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
Bixa orellana
physiological function
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated. Protein phosphatase 2A (PP2A) is both a transcriptional and a posttranslational regulator of HMGR in Arabidopsis thaliana
Arabidopsis thaliana
Other publictions for EC 1.1.1.34
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Protein Variants
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
kcat/KM [mM/s]
kcat/KM [mM/s] (protein specific)
761343
Zheng
Brassinosteroid regulates 3-h ...
Vitis vinifera
J. Agric. Food Chem.
68
11987-11996
2020
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762169
Zhang
The 3-hydroxy-3-methylglutary ...
Malus domestica
Plant Physiol. Biochem.
146
269-277
2020
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761172
Wei
Characterization and function ...
Populus trichocarpa
Front. Plant Sci.
10
1476
2019
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761539
Costa
Computational study of confor ...
Homo sapiens
J. Biomol. Struct. Dyn.
37
4374-4383
2019
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761571
Andrade-Pavon
Inhibition of recombinant enz ...
[Candida] glabrata, [Candida] glabrata CBS138
J. Biotechnol.
292
64-67
2019
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761759
Ando
Side-chain oxysterols suppres ...
Homo sapiens, Mus musculus
J. Steroid Biochem. Mol. Biol.
195
105482
2019
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762318
Zhang
cDNA cloning, prokaryotic exp ...
Pogostemon cablin
Protein Expr. Purif.
163
105454
2019
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1
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11
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1
1
2
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1
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1
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1
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8
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The relationship between late ...
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Transcriptome analysis of Hev ...
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4
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Engineering of Yarrowia lipol ...
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760659
Devi
An insight into structure, fu ...
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3
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740265
Oliveira
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QM/MM study of the mechanism o ...
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2
1
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Kalita
Molecular cloning, characteriz ...
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1
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5
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1
1
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2
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741192
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Characterization and function ...
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2
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2
2
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1
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1
1
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740956
Campos
Determination of 3-hydroxy-3-m ...
Arabidopsis thaliana, Arachis hypogaea, Persea americana, Brassica napus, Cannabis sativa, Cucumis melo, Daucus carota, Dunaliella salina, Euphorbia lathyris, Glycine max, Gossypium barbadense, Gossypium hirsutum, Helianthus tuberosus, Hevea brasiliensis, Hordeum vulgare, Ipomoea batatas, Lithospermum erythrorhizon, Medicago sativa, Solanum lycopersicum, Malus domestica, Nepeta cataria, Nicotiana tabacum, Ochromonas malhamensis, Parthenium argentatum, Vigna radiata var. radiata, Picea abies, Pimpinella anisum, Pisum sativum, Raphanus sativus, Sinapis alba, Solanum tuberosum, Spinacia oleracea, Zea mays, Artemisia annua, Nicotiana benthamiana, Stevia rebaudiana, Salvia miltiorrhiza, Taraxacum brevicorniculatum, Solanum virginianum, Bixa orellana
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65
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120
40
80
40
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-
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44
-
-
80
-
-
-
41
-
-
80
-
-
-
-
1
-
-
41
40
-
80
-
40
80
1
-
65
-
-
120
40
40
-
-
-
44
-
-
-
-
120
120
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740970
Dinesh
Exploring Leishmania donovani ...
Leishmania donovani, Leishmania donovani MHOM/80/IN/Dd8
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66
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1
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4
3
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1
2
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5
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1
-
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2
-
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4
2
3
1
1
1
-
1
1
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2
-
1
2
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1
2
-
-
-
2
4
-
3
-
-
1
2
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-
1
-
2
-
-
4
2
1
1
1
-
1
1
-
1
-
1
1
-
-
-
721267
Pak
Design of a highly potent inhi ...
Homo sapiens
Amino Acids
43
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2012
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-
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23
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1
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2
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-
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1
-
3
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1
1
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22
-
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-
1
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22
24
1
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-
1
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-
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1
-
-
-
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-
-
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1
1
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-
722328
Chen
Molecular cloning, tissue expr ...
Sus scrofa
Gene
495
170-177
2012
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1
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3
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-
-
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1
1
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21
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3
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15
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1
1
2
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1
-
1
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1
1
-
3
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1
1
-
-
3
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15
-
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1
1
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-
-
-
-
-
-
1
-
2
2
-
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722329
Rui
3-Hydroxy-3-methylglutaryl coe ...
Litchi chinensis
Gene
498
28-35
2012
-
-
1
-
-
-
-
-
-
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1
-
7
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9
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1
-
3
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1
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1
1
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1
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-
-
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9
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1
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-
-
-
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2
2
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723598
Song
Overexpressing 3-hydroxy-3-met ...
Lactococcus lactis, Lactococcus lactis NZ9000
PLoS ONE
7
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2012
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1
1
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-
-
-
-
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-
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2
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14
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-
-
-
-
-
-
2
-
2
1
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-
-
1
-
-
1
-
-
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-
1
1
1
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-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
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-
-
-
1
1
-
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722189
Sashidhara
Discovery of a new class of HM ...
Mesocricetus auratus
Eur. J. Med. Chem.
46
5206-5211
2011
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-
-
-
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2
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3
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-
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-
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-
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3
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-
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2
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-
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-
-
-
-
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-
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712198
Gholamhoseinian
-
Inhibitory activity of some pl ...
Homo sapiens
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6
705-711
2010
-
-
-
-
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1
1
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1
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1
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-
1
-
1
-
-
-
-
1
-
-
2
1
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-
-
-
-
2
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
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-
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712214
Leopoldini
On the inhibitor effects of be ...
Homo sapiens
J. Agric. Food Chem.
58
10768-10773
2010
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-
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4
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1
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2
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-
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2
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2
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4
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-
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-
-
-
-
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-
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3
3
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712676
Mozzicafreddo
Rapid reverse phase-HPLC assay ...
Homo sapiens
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51
2460-2463
2010
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-
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-
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1
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1
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-
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2
-
-
2
-
2
1
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-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
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-
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2
-
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2
-
1
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-
1
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-
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695827
Ohto
Overexpression of the gene enc ...
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82
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1
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-
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3
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-
-
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1
-
2
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-
-
-
-
-
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-
-
-
1
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
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-
-
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696687
Hosoda
Application of a 3,3-diphenylp ...
Rattus norvegicus
Bioorg. Med. Chem. Lett.
19
4228-4231
2009
-
-
-
-
-
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11
-
-
-
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1
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-
-
-
-
-
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1
-
3
-
-
-
-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
11
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
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697143
Seiki
Pharmacologic inhibition of sq ...
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-
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2
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-
-
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-
-
-
-
-
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-
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-
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-
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1
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698528
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Functional expression of human ...
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3
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1
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1
1
1
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3
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3
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1
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700117
Cao
Molecular cloning, characteriz ...
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1
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3
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1
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3
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1
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1
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1
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3
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1
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700682
Nieto
Arabidopsis 3-hydroxy-3-methyl ...
Arabidopsis thaliana
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70
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2
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-
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2
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1
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7
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1
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2
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1
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1
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700852
Aquil
Overexpression of the HMG-CoA ...
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1
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1
1
1
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710786
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Molecular cloning, characteriz ...
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712189
Perchellet
Novel synthetic inhibitors of ...
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Int. J. Mol. Med.
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1
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2
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1
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2
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2
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-
2
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6
-
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1
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-
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1
-
-
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-
-
-
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-
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-
1
1
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-
685531
Pak
Binding effect and design of a ...
Rattus norvegicus
Bioorg. Med. Chem.
16
1309-1318
2008
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-
-
-
-
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15
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1
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-
1
-
3
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1
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1
-
2
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1
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15
-
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1
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-
15
16
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1
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1
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1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
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685680
Shang
Cloning and characterization o ...
Ganoderma lucidum
Biosci. Biotechnol. Biochem.
72
1333-1339
2008
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1
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1
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1
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11
-
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1
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2
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1
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1
1
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1
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1
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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687094
Burse
Implication of HMGR in homeost ...
Phaedon cochleariae
Insect Biochem. Mol. Biol.
38
76-88
2008
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-
1
-
-
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3
-
1
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2
2
-
8
-
2
1
-
-
1
-
-
3
3
1
1
1
-
-
2
-
-
1
-
1
2
-
-
1
1
-
-
-
2
3
-
-
1
-
2
2
-
-
2
1
-
1
-
-
3
3
1
1
-
-
2
-
-
1
-
-
-
-
-
-
687713
Schiefelbein
Biphasic regulation of HMG-CoA ...
Mus musculus, Mus musculus C57/BL6J
J. Biol. Chem.
283
15479-15490
2008
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-
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1
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-
-
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2
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4
-
1
1
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1
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1
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1
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1
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1
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4
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2
-
-
4
-
1
-
-
-
1
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688473
Pak
Modeling an active conformatio ...
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J. Mol. Recognit.
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2008
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3
1
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2
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1
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1
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2
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1
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1
1
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1
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3
1
1
1
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1
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1
-
-
1
-
-
-
-
1
-
-
-
-
-
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-
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695855
Subbaiah
Sphingolipids and cellular cho ...
Homo sapiens
Arch. Biochem. Biophys.
474
32-38
2008
1
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-
-
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3
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1
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1
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1
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1
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1
-
-
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-
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-
-
-
-
-
-
-
-
701255
Vaupotic
HMG-CoA reductase is regulated ...
Aspergillus amstelodami, Aureobasidium pullulans, Saccharomyces cerevisiae, Debaryomyces hansenii, Hortaea werneckii, Neophaeotheca triangularis, Trimmatostroma salinum, Wallemia ichthyophaga, Saccharomyces cerevisiae MZKI K86, Wallemia ichthyophaga EXF 994, Neophaeotheca triangularis MZKI B741, Aureobasidium pullulans MZKI B802, Hortaea werneckii MZKI B736, Aspergillus amstelodami MZKI A561, Debaryomyces hansenii CBS 767, Trimmatostroma salinum MZKI B734
Stud. Mycol.
61
61-66
2008
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1
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8
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16
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27
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16
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16
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8
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16
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-
16
-
-
-
-
-
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684808
Gueguen
Compared effect of immunosuppr ...
Homo sapiens
Basic Clin. Pharmacol. Toxicol.
100
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2007
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1
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1
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685520
Bratton
Discovery of pyrrole-based hep ...
Rattus norvegicus
Bioorg. Med. Chem.
15
5576-5589
2007
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1
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16
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1
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1
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1
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5
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1
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1
1
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1
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15
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1
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1
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15
16
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1
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1
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-
5
-
-
1
-
1
-
-
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685581
Pfefferkorn
Design and synthesis of novel, ...
Mus musculus
Bioorg. Med. Chem. Lett.
17
4531-4537
2007
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31
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33
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2
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1
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686736
Vaupotic
Osmoadaptation-dependent activ ...
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581
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1
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8
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1
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1
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2
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2
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2
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1
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2
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1
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3
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2
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1
1
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1
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2
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-
-
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689453
Munoz-Bertomeu
Up-regulation of an N-terminal ...
Arabidopsis thaliana
Plant Biotechnol. J.
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2007
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1
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2
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2
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1
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1
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1
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1
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1
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1
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-
2
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667158
Lee
Additive effects of combined b ...
Rattus norvegicus
Am. J. Physiol. Heart Circ. Physiol.
291
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1
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4
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1
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1
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-
-
-
-
-
-
-
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667236
Muzio
HMG-CoA reductase and PPARalph ...
Homo sapiens
Apoptosis
11
265-275
2006
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5
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2
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2
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668026
Jiang
Molecular cloning of a HMG-CoA ...
Eucommia ulmoides
Biosci. Rep.
26
171-181
2006
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1
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3
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1
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3
-
-
-
-
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-
-
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-
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668493
Ness
Selective compensatory inducti ...
Rattus norvegicus
Exp. Biol. Med.
231
559-565
2006
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1
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6
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668533
Bidle
HMG-CoA reductase is regulated ...
Haloferax volcanii
Extremophiles
11
49-55
2006
-
-
1
-
-
-
-
-
1
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1
3
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7
-
-
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-
-
1
1
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4
1
2
1
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-
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-
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1
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-
1
1
-
-
-
-
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1
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1
3
-
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1
1
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4
1
1
-
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669520
Datta
Regulation of 3-hydroxy-3-meth ...
Mus musculus
J. Biol. Chem.
281
807-812
2006
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1
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1
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-
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-
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669600
Pallottini
Modified HMG-CoA reductase and ...
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
J. Cell. Biochem.
98
1044-1053
2006
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1
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669695
Pallottini
Rat HMGCoA reductase activatio ...
Rattus norvegicus
J. Hepatol.
44
368-374
2006
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2
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1
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2
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1
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1
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2
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1
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669764
Lee
Mutations within membrane doma ...
Cricetulus griseus
J. Lipid Res.
48
318-327
2006
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1
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1
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3
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1
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670100
Lecian
Renal effects of HMG-CoA reduc ...
Rattus norvegicus
Kidney Blood Press. Res.
29
135-143
2006
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1
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1
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1
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1
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1
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654375
Mokashi
Supernatant protein factor sti ...
Rattus norvegicus
Arch. Biochem. Biophys.
433
474-480
2005
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1
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1
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1
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1
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1
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1
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1
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1
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1
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2
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1
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1
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667150
Shin
Effects of gender on hepatic H ...
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Am. J. Physiol. Endocrinol. Metab.
289
E993-E998
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1
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667627
Carbonell
Binding thermodynamics of stat ...
Homo sapiens
Biochemistry
44
11741-11748
2005
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2
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1
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1
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1
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1
5
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1
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5
5
2
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1
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668139
Duncan
Regulation of HMG-CoA reductas ...
Homo sapiens
Cancer Lett.
224
221-228
2005
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1
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2
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1
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1
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1
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1
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2
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670587
Leivar
Subcellular localization of Ar ...
Arabidopsis thaliana
Plant Physiol.
137
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2005
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1
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1
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1
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1
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654546
Li
The lobster mandibular organ p ...
Homarus americanus
Biochem. J.
381
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2
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3
2
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1
1
4
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1
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2
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2
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3
2
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2
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3
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2
1
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3
2
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1
1
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1
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655059
Sung
Isoflavones found in korean so ...
Mesocricetus auratus
Biosci. Biotechnol. Biochem.
68
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2004
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3
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9
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1
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655507
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Differential translational eff ...
Homo sapiens
Exp. Biol. Med.
229
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2004
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656216
Shearer
Structural control of endoplas ...
Saccharomyces cerevisiae
J. Biol. Chem.
279
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2004
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657007
Suzuki
Loss of function of 3-hydroxy- ...
Arabidopsis thaliana
Plant J.
37
750-761
2004
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654559
Holdgate
Molecular mechanism for inhibi ...
Homo sapiens
Biochem. Soc. Trans.
31
528-531
2003
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1
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6
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2
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3
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655032
Kondo
Induction mechanism of 3-hydro ...
Ipomoea batatas, Solanum tuberosum, Solanum x edinense
Biosci. Biotechnol. Biochem.
67
1007-1017
2003
2
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3
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8
2
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3
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3
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3
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656131
Tabernero
Crystal structure of a statin ...
Pseudomonas mevalonii
J. Biol. Chem.
278
19933-19938
2003
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4
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657004
Holmberg
Co-expression of N-terminal tr ...
Hevea brasiliensis
Plant J.
36
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2003
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1
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1
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487702
Hedl
Enterococcus faecalis acetoace ...
Enterococcus faecalis
J. Bacteriol.
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2116-2122
2002
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1
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1
1
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5
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1
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4
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1
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10
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5
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1
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4
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655549
Hurtado-Guerrrero
Kinetic properties and inhibit ...
Trypanosoma cruzi
FEBS Lett.
510
141-144
2002
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1
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2
6
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1
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1
2
1
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2
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1
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1
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2
1
6
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1
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2
1
1
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2
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286583
Montalvetti
Characterization and regulatio ...
Leishmania major
Biochem. J.
349
27-34
2000
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1
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2
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2
1
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6
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1
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1
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1
1
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286586
Kim
Engineering of Sulfolobus solf ...
Saccharolobus solfataricus
Biochemistry
39
2269-2275
2000
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1
-
2
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18
-
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1
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12
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1
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2
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5
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2
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1
2
-
2
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18
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1
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2
-
5
-
-
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286587
Wilding
Essentiality, expression, and ...
Staphylococcus aureus
J. Bacteriol.
182
5147-5152
2000
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1
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7
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1
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1
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1
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286581
Takahashi
Purification, characterization ...
Streptomyces sp.
J. Bacteriol.
181
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1999
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1
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2
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4
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1
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1
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1
1
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1
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1
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1
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1
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2
1
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1
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1
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1
1
1
1
-
-
1
-
-
-
-
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-
-
-
-
286582
Polo
3-Hydroxy-3-methylglutaryl coe ...
Mus musculus
Comp. Biochem. Physiol. B
122
433-437
1999
-
-
-
-
-
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5
1
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1
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15
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5
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1
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1
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1
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5
1
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1
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5
-
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1
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-
-
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-
-
-
-
-
-
-
-
-
286585
Kim
Expression and characterizatio ...
Saccharolobus solfataricus
Protein Expr. Purif.
17
435-442
1999
-
-
2
-
1
-
1
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-
-
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1
-
9
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1
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1
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2
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2
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1
1
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2
1
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1
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1
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1
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1
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1
-
2
-
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-
-
2
-
-
-
-
-
-
-
-
-
286580
Concepcion
3-Hydroxy-3-methylglutaryl-CoA ...
Trypanosoma cruzi
Arch. Biochem. Biophys.
352
114-120
1998
-
-
-
-
-
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1
2
2
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1
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5
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1
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1
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1
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1
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2
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1
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1
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1
-
1
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
286579
Friesen
Identification of elements cri ...
Pseudomonas mevalonii
Biochemistry
36
1157-1162
1997
-
-
1
-
1
-
-
-
-
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1
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6
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1
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1
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1
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1
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-
-
-
-
-
-
-
-
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286584
Bochar
3-Hydroxy-3-methylglutaryl coe ...
Saccharolobus solfataricus, Saccharolobus solfataricus P2
J. Bacteriol.
179
3632-3638
1997
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1
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30
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2
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-
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2
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6
-
-
1
-
2
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
4
-
-
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2
-
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-
2
-
-
2
-
6
-
1
-
2
-
1
-
-
-
-
-
-
-
-
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728768
Bischoff
3-Hydroxy-3-methylglutaryl-coe ...
Haloferax volcanii, Haloferax volcanii DSM 3757
Protein Sci.
6
156-161
1997
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-
-
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2
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18
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-
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6
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1
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-
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4
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2
1
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1
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-
-
-
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-
-
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-
-
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2
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-
-
18
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1
-
-
-
-
4
-
1
-
-
-
1
-
-
-
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286578
Bischoff
3-Hydroxy-3-methylglutaryl-coe ...
Haloferax volcanii
J. Bacteriol.
178
19-23
1996
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1
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2
7
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1
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14
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1
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1
-
4
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
7
-
-
-
1
-
-
-
1
-
-
1
-
4
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
286577
Ball
Biochemical characterization o ...
Brassica oleracea
Eur. J. Biochem.
219
743-750
1994
-
-
-
-
-
-
-
-
-
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1
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5
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1
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-
-
-
-
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1
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-
-
-
-
-
-
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-
1
-
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-
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1
-
-
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1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286575
Chen
Purification and characterizat ...
Schistosoma mansoni
Exp. Parasitol.
73
82-92
1991
-
-
-
-
-
-
1
2
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1
1
-
4
-
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1
-
-
-
1
2
1
1
-
-
-
-
-
-
-
-
1
-
-
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-
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-
1
-
-
-
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1
-
2
-
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1
1
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-
-
1
-
-
1
2
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286576
Hupperich
Substrate and inhibitor specif ...
Homo sapiens
Biol. Chem. Hoppe-Seyler
372
857-863
1991
-
-
-
-
-
-
5
-
-
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1
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3
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
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-
-
-
1
-
-
-
-
5
-
-
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-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286574
Gibson
-
Hydroxymethylglutaryl-coenzyme ...
Rattus norvegicus
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )
18
179-215
1987
-
-
-
-
-
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2
-
2
-
1
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
2
-
1
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
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286573
Feingold
The effect of substrates and c ...
Rattus norvegicus
Arch. Biochem. Biophys.
249
46-51
1986
-
-
-
-
-
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3
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1
-
1
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1
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-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
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-
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-
-
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286572
Ness
Activation of rat liver micros ...
Rattus norvegicus
J. Biol. Chem.
260
12391-12393
1985
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-
-
-
-
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1
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2
1
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4
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-
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2
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-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
2
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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286569
Van Heusden
Hydroxymethylglutaryl CoA redu ...
Rattus norvegicus
J. Lipid Res.
25
27-32
1984
-
-
-
-
-
-
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2
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1
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6
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1
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-
2
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1
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-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
2
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
286570
Arebalo
-
Cellular distribution of 3-hyd ...
Nepeta cataria
Phytochemistry
23
13-18
1984
-
-
-
-
-
-
-
-
2
-
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1
-
1
-
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1
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1
1
-
1
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-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
286571
Harwood
Regulation of human leukocyte ...
Homo sapiens
Biochim. Biophys. Acta
805
245-251
1984
-
-
-
-
-
-
-
-
1
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1
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6
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1
1
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5
-
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1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
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-
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1
-
-
1
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-
1
1
-
5
-
-
1
-
-
-
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-
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286567
Young
Recovery and activation from h ...
Rattus norvegicus
J. Lipid Res.
23
257-265
1982
-
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1
-
-
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1
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4
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1
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3
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2
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-
-
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1
-
-
-
-
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1
-
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1
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-
1
-
-
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1
-
3
-
-
2
-
-
-
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-
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-
-
-
286568
Sipat
-
Hydroxymethylglutaryl CoA redu ...
Hevea brasiliensis, Pisum sativum, Rattus norvegicus
Phytochemistry
21
2613-2618
1982
2
-
-
-
-
3
7
1
3
-
-
3
-
3
-
-
-
-
-
1
-
-
3
-
-
1
-
-
-
3
-
-
4
-
-
-
2
-
-
4
-
-
3
-
7
-
1
3
-
-
3
-
-
-
-
-
1
-
-
3
-
1
-
-
-
3
-
-
-
-
-
-
-
-
-
286565
Ingebritsen
Regulation of liver hydroxymet ...
Rattus norvegicus
J. Biol. Chem.
256
1138-1144
1981
-
-
-
-
-
-
-
-
1
-
-
2
-
1
-
1
1
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
1
1
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286566
Gilbert
Inactivation of hydroxymethylg ...
Saccharomyces cerevisiae
J. Biol. Chem.
256
1782-1785
1981
-
-
-
-
-
-
5
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
5
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286564
Preiss
Hydroxymethylglutaryl coenzyme ...
Cricetinae
Biochem. Biophys. Res. Commun.
88
1140-1146
1979
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286563
Madhosingh
Hydroxymethylglutaryl coenzyme ...
Fusarium oxysporum
Biochim. Biophys. Acta
523
283-296
1978
-
-
-
-
-
-
-
1
1
-
1
1
-
9
-
-
1
-
-
-
1
1
1
1
-
1
1
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
1
1
-
1
1
-
-
-
1
-
-
1
1
1
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
286562
Madhosingh
-
Hydroxymethylglutaryl coenzyme ...
Fusarium oxysporum
Agric. Biol. Chem.
41
1519-1521
1977
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286561
Heller
Prevention of cold inactivatio ...
Rattus norvegicus
Biochim. Biophys. Acta
388
254-259
1975
-
-
-
-
-
-
-
-
1
-
-
1
-
4
-
-
-
-
-
1
1
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
286560
Madhosingh
Inhibition of yeast hydroxymet ...
Saccharomyces cerevisiae, Rattus norvegicus
FEBS Lett.
46
20-22
1974
-
-
-
-
-
-
-
-
3
-
-
2
-
2
-
-
2
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
3
-
-
2
-
-
-
2
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286559
Kawachi
Solubilization and purificatio ...
Rattus norvegicus
Biochemistry
9
1700-1705
1970
-
-
-
-
-
-
10
2
1
-
1
1
-
3
-
-
1
-
-
2
1
1
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
10
-
2
1
-
1
1
-
-
-
1
-
2
1
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286557
Bucher
beta-Hydroxy-beta-methylglutar ...
Rattus norvegicus
Biochim. Biophys. Acta
40
491-501
1960
-
-
-
-
-
1
1
-
2
-
-
1
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
1
-
-
2
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286558
Durr
The reduction of beta-hydroxy- ...
Saccharomyces cerevisiae
J. Biol. Chem.
235
2572-2578
1960
-
-
-
-
-
-
2
-
-
-
-
1
-
1
-
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
1
-
-
1
-
1
-
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-
-
-
-
-
-
-
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-
-