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Information on EC 1.1.1.34 - hydroxymethylglutaryl-CoA reductase (NADPH) and Organism(s) Arabidopsis thaliana

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EC Tree
IUBMB Comments
The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
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This record set is specific for:
Arabidopsis thaliana
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
hmg-coa reductase, hmgcr, 3-hydroxy-3-methylglutaryl coenzyme a reductase, hmgr, hmg coa reductase, 3-hydroxy-3-methylglutaryl-coa reductase, 3-hydroxy-3-methylglutaryl-coenzyme a reductase, hmgcoa reductase, 3-hydroxy-3-methylglutaryl coa reductase, hmg-coar, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxy-3-methylglutaryl Ccoenzyme A reductase 1
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3-hydroxy-3-methylglutaryl CoA reductase
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3-hydroxy-3-methylglutaryl-CoA reductase
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3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)
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3-hydroxy-3-methylglutaryl-CoA reductase 1
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beta-hydroxy-beta-methylglutaryl coenzyme A reductase
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-
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beta-hydroxy-beta-methylglutaryl-Co A reductase
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HMG-CoA reductase
HMG2.2
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-
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HMG3.3
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-
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HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating CoA)
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-
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HMGR1
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-
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HMGR1S
HMGR2
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hydroxymethylglutaryl CoA reductase (NADPH)
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hydroxymethylglutaryl-coenzyme A reductase (reduced nicotinamide adenine dinucleotide phosphate)
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mevalonate:NADP+ oxidoreductase (acetylating CoA)
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NADPH-hydroxymethylglutaryl-CoA reductase
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S-3-hydroxy-3-methylglutaryl-CoA reductase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
(R)-mevalonate:NADP+ oxidoreductase (CoA-acylating)
The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-35-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
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-
-
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r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
show the reaction diagram
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
show the reaction diagram
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up- and down-regulation of HMGR activity in response to changes in the flux of the mevalonate pathway occur via post-translational control
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-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
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-
-
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r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
show the reaction diagram
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
show the reaction diagram
-
up- and down-regulation of HMGR activity in response to changes in the flux of the mevalonate pathway occur via post-translational control
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
show the reaction diagram
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key enzyme of the mevalonic acid pathway catalysing the first committed step with NADPH as cofactor, overview
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-
?
additional information
?
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phytosterol biosynthetic pathway, overview
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activates
Mg2+
1 mM used in assay conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lovastatin
myriocin
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concomitant reduction of both HMGR activity and the sterol content by depletion of the sphingolipid pathway. At 0.01 mM myriocin decrease to ca. 55% of the HMGR activity in control plants. Myriocin-induced down-regulation of HMGR activity is exerted at the post-translational level, like the regulatory response of HMGR to enhancement or depletion of the flux through the sterol pathway
squalestatin
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mutant plants, not wild-type plants, become sterile
additional information
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whether plants are grown with mevalonate from the beginning or only during the last 9 days, HMGR activity is drastically reduced to 25% of the activity in plants grown in the absence of mevalonate. Plants grown without mevalonate during the last 9 days show a severe, though less pronounced, reduction in HMGR activity, which decreases to 60% of the activity in control plants. Significant reduction of HMGR activity does not correlate with changes in both the expression of HMG1 and HMG2 genes and the amount of HMGR protein
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
squalestatin
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leads to a significant concentration-dependent activation of HMGR of ca. 3fold the activity in untreated plants. Maximal HMGR activation at 0.06 mM squalestatin. No relevant changes in the level of expression of the HMG genes or in the amount of HMGR protein
terbinafine
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leads to a significant concentration-dependent activation of HMGR of ca. 3fold the activity in untreated plants. Maximal HMGR activation at 0.75 mM terbinafine. No relevant changes in the level of expression of the HMG genes or in the amount of HMGR protein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01333
mutant enzyme S577A from transgenic line 2, at 30°C, pH not specified in the publication
0.01644
mutant enzyme S577A from transgenic line 1, at 30°C, pH not specified in the publication
0.01949
wild type enzyme from transgenic line 1, at 30°C, pH not specified in the publication
0.03568
wild type enzyme from transgenic line 2, at 30°C, not pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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green seedling, aerial part and root
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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localized predominantly within spherical vesicular structures that range from 0.0002-0.0006 mm in diameter, located in the cytoplasm and within the central vacuole in differentiated cotyledon cells. The N-terminal region, including the transmembrane domain of HMGR, is found to be necessary and sufficient for directing HMGR to the endoplasmic reticulum and the spherical structures
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
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the HMGR activity is detected in the final microsomal pellet after ultracentrifugation
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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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
metabolism
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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
physiological function
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HMDH2_ARATH
562
2
60715
Swiss-Prot
other Location (Reliability: 2)
HMDH1_ARATH
592
3
63598
Swiss-Prot
Chloroplast (Reliability: 4)
A0A178W3L3_ARATH
592
3
63598
TrEMBL
Chloroplast (Reliability: 4)
A0A178VRN5_ARATH
562
2
60715
TrEMBL
other Location (Reliability: 2)
A0A654ER34_ARATH
642
3
69280
TrEMBL
Chloroplast (Reliability: 4)
C0Z3D4_ARATH
91
1
9124
TrEMBL
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63000
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immunoblot analysis, isoform HMGR1S
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 63000-70000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
additional information
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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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S577A
the mutant shows reduced activity compared to the wild type enzyme
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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740956
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-FLAG-tag magnetic bead chromatography
native enzyme by ultracentrifugation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suzuki, M.; Kamide, Y.; Nagata, N.; Seki, H.; Ohyama, K.; Kato, H.; Masuda, K.; Sato, S.; Kato, T.; Tabata, S.; Yoshida, S.; Muranaka, T.
Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility, and reduced sterol levels
Plant J.
37
750-761
2004
Arabidopsis thaliana
Manually annotated by BRENDA team
Leivar, P.; Gonzalez, V.M.; Castel, S.; Trelease, R.N.; Lopez-Iglesias, C.; Arro, M.; Boronat, A.; Campos, N.; Ferrer, A.; Fernandez-Busquets, X.
Subcellular localization of Arabidopsis 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Plant Physiol.
137
57-69
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Munoz-Bertomeu, J.; Sales, E.; Ros, R.; Arrillaga, I.; Segura, J.
Up-regulation of an N-terminal truncated 3-hydroxy-3-methylglutaryl CoA reductase enhances production of essential oils and sterols in transgenic Lavandula latifolia
Plant Biotechnol. J.
5
746-758
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Nieto, B.; Fores, O.; Arro, M.; Ferrer, A.
Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the post-translational level in response to alterations of the sphingolipid and the sterol biosynthetic pathways
Phytochemistry
70
53-59
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Campos, N.; Arro, M.; Ferrer, A.; Boronat, A.
Determination of 3-hydroxy-3-methylglutaryl CoA reductase activity in plants
Methods Mol. Biol.
1153
21-40
2014
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
Manually annotated by BRENDA team
Robertlee, J.; Kobayashi, K.; Tang, J.; Suzuki, M.; Muranaka, T.
Evidence that the Arabidopsis thaliana 3-hydroxy-3-methylglutaryl-CoA reductase 1 is phosphorylated at Ser577 in planta
Plant Biotechnol.
35
1-7
2018
Arabidopsis thaliana (P14891), Arabidopsis thaliana
Manually annotated by BRENDA team