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Information on EC 1.14.12.10 - benzoate 1,2-dioxygenase
for references in articles please use BRENDA:EC1.14.12.10
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor
1.14.12.10 benzoate 1,2-dioxygenase
IUBMB Comments
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), and an iron-sulfur oxygenase. Requires Fe2+.
The enzyme appears in viruses and cellular organisms
- 1.14.12.10
- catechol
- calcoaceticus
- toluate
- 2-chlorobenzoate
- chlorocatechols
-
rieske
-
cis-diols
-
rieske-type
-
beta-ketoadipate
-
benzoate-grown
- radioresistens
- 3-methylbenzoate
-
benzoate-induced
-
3,4-dioxygenase
-
cis-dihydrodiols
- 4-chlorocatechol
-
ring-hydroxylating
- arvilla
- synthesis
Reaction Schemes
showSynonyms
benzoate dioxygenase, benzoate 1,2-dioxygenase, benabc, benzoate 1,2-dioxygenase system, benzoate hydroxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BDO
BenA
benABC
benzoate 1,2-dioxygenase
benzoate 1,2-dioxygenase oxygenase
benzoate 1,2-dioxygenase system
benzoate dioxygenase
benzoate hydroxylase
-
-
-
-
benzoic hydroxylase
-
-
-
-
BZDO
BZDO enzyme
EC 1.13.99.2
-
-
formerly
-
oxygenase, benzoate 1,2-di-
-
-
-
-
benABC
-
genes are organized in a single cluster and are under benzoate induced regulation. The benABC genes jointly encode benzoate 1,2-dioxygenase, which catalyzes the dihydroxylation of benzoate to produce 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid
benABC
-
genes are organized in a single cluster and are under benzoate induced regulation. The benABC genes jointly encode benzoate 1,2-dioxygenase, which catalyzes the dihydroxylation of benzoate to produce 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid
-
benzoate 1,2-dioxygenase oxygenase
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
-
-
benzoate dioxygenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzoate + NADH + H+ + O2 = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
proposed catalytic cycle
-
benzoate + NADH + H+ + O2 = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
the enzyme consists of two proteins, a NADH-cytochrome c reductase and an oxygenase
-
benzoate + NADH + H+ + O2 = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
proposed catalytic cycle
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
-
benzoate + NADH + H+ + O2 = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
the enzyme consists of two proteins, a NADH-cytochrome c reductase and an oxygenase
-
-
benzoate + NADH + H+ + O2 = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
benzoate degradation I (aerobic)
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SYSTEMATIC NAME
IUBMB Comments
benzoate,NADH:oxygen oxidoreductase (1,2-hydroxylating)
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), and an iron-sulfur oxygenase. Requires Fe2+.
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CAS REGISTRY NUMBER
COMMENTARY
9059-18-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzene + O2 + NADH
(R,S)-1,2-dihydro-1,2-dihydroxycatechol + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH-cytochrome c reductase component + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+-cytochrome c reductase component
-
Substrates: -
Products: -
Products: -
r
2-methylbenzoate + O2 + NADH
cis-1,2-dihydro-1,2-dihydroxy-2-methyl-benzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-methylbenzoate + O2 + NADH
cis-1,2-dihydro-1,2-dihydroxy-2-methyl-benzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
Substrates: activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
Products: -
Products: -
?
3-aminobenzoate + O2 + NADH
3-amino-2-hydro-1,2-dihydroxybenzoate
-
Substrates: activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
Products: -
Products: -
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzoate + O2 + NADH + H+
3-chloro-2-hydro-1,2-dihydroxybenzoate + NAD+
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: benzoate analogues with substituents in meta position are oxygenated more rapidly than those with ortho- or para substitution
Products: -
Products: -
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: benzoate analogues with substituents in meta position are oxygenated more rapidly than those with ortho- or para substitution
Products: -
Products: -
?
3-fluorobenzoate + O2 + NADH + H+
3-fluoro-2-hydro-1,2-dihydroxybenzoate + NAD+
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
Substrates: -
Products: -
Products: -
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
Substrates: -
Products: -
Products: -
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
Products: -
Products: -
?
3-methylbenzoate + O2 + NADH + H+
3-methyl-2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
Products: -
Products: -
?
4-fluorobenzoate + O2 + NADH
4-fluoro-2-hydro-1,2-dihydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
4-fluorobenzoate + O2 + NADH
4-fluoro-2-hydro-1,2-dihydroxybenzoate
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: catabolism of aromatic compounds
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: catabolism of aromatic compounds
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
Products: -
Products: -
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: activity in E. coli expressing a presumed dioxygenase component from Rhodococcus
Products: -
Products: -
?
ethyl benzene + NADH + H+ + O2
?
-
Substrates: highest activity
Products: -
Products: -
?
ethyl benzene + NADH + H+ + O2
?
-
Substrates: highest activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: benzoate induces the expression of benzoate 1,2-dioxygenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: benzoate 1,2 dioxygenase oxygenase component (BZDO) prepared in a form with the Rieske cluster oxidized and the mononuclear iron in the Fe(III) state can utilize H2O2 as a source of reduced oxygen to form the correct cis-dihydrodiol product from benzoate
Products: -
Products: -
?
additional information
?
-
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
Substrates: benzoate 1,2 dioxygenase oxygenase component (BZDO) prepared in a form with the Rieske cluster oxidized and the mononuclear iron in the Fe(III) state can utilize H2O2 as a source of reduced oxygen to form the correct cis-dihydrodiol product from benzoate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: benzoate induces the expression of benzoate 1,2-dioxygenase
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
?
benzoate + NADH + H+ + O2
cis-1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylate + NAD+
-
Substrates: -
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
Products: Recombinant strain with overexpression of benABC gene and benD knockout. Highest biotransformation is found with cells grown on 2.88 g/l Na-benzoate, yielding approximately 2.3 g/l 1,2-dihydroxy-cyclohexa-3,5-diene-1-carboxylic acid with a yield of 73%. The biotransformation yield decreases along with the increase in substrate benzoate concentration. The benD knockout mutant harboring BZDO genes produced concentration of cis-diol product in fermentation (17 g/l, 61% yield).
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: catabolism of aromatic compounds
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: catabolism of aromatic compounds
Products: -
Products: -
?
benzoate + O2 + NADH
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
benzoate + O2 + NADH + H+
2-hydro-1,2-dihydroxybenzoate + NAD+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iron-sulfur center
-
each alpha-subunit contains a Rieske [2Fe-2S] cluster and a mononuclear iron site
FAD
-
requirement, benzoate 1,2-dioxygenase system consists of 2 proteins: a 37500 Da NADH-cytochrome c reductase containing 1 FAD and 1 iron-sulfur cluster [2Fe-2S] and an oxygenase which may contain 4 [2Fe-2S] clusters
NADH
-
requirement, benzoate 1,2-dioxygenase system consists of 2 proteins: a 37500 Da NADH-cytochrome c reductase containing 1 FAD and 1 iron-sulfur cluster [2Fe-2S] and an oxygenase which may contain 4 [2Fe-2S] clusters
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
-
reductase component contains a plant type [2Fe-2S] cluster and a presumed mononuclear iron, the terminal dioxygenase contains a Rieske-type [2Fe-2S] cluster
Iron
-
oxygenase component: 2.7 mol/mol of alphabeta subunit, each alpha subunit contains a Rieske [2Fe-2S] cluster and a mononuclear iron site, reductase component: 2.02 mol/monomer
Iron
-
iron sulfur protein with [2Fe-2S]clusters and additional iron atoms
Iron
-
each alpha-subunit contains a Rieske [2Fe-2S] cluster and a mononuclear iron site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
367
benzoate
-
in the presence of saturating amounts of NADH-cytochrome c reductase
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
The recombinant bacteria shows a BZDO activity of 1.2 mmol benzoate per gram cell dry weight, while Pseudomonas putida KTSY01 shows a BZDO activity of only 0.09 mmol.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (1824 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
-
alpha3,beta3, 3 * 19000 + 3 * 49000, oxygenase component, SDS-PAGE
195000
20000
-
alpha3,beta3, 3 * 20000 + 3 * 50000, oxygenase component of the enzyme system, SDS-PAGE
38000
49000
-
alpha3,beta3, 3 * 19000 + 3 * 49000, oxygenase component, SDS-PAGE
50000
-
alpha3,beta3, 3 * 20000 + 3 * 50000, oxygenase component of the enzyme system, SDS-PAGE
52300
-
calculated from the deduced amino acid sequence, alpha subunit
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
monomer
trimer
hexamer
-
alpha3,beta3, 3 * 20000 + 3 * 50000, oxygenase component of the enzyme system, SDS-PAGE
hexamer
-
alpha3,beta3, 3 * 19000 + 3 * 49000, oxygenase component, SDS-PAGE
hexamer
-
alpha3,beta3, 3 * 20000 + 3 * 50000, oxygenase component of the enzyme system, SDS-PAGE
-
hexamer
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
alpha3,beta3, 3 * 19000 + 3 * 49000, oxygenase component, SDS-PAGE
-
monomer
-
1 * 38000, reductase component, sedimentation analysis, SDS-PAGE
monomer
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
1 * 38000, reductase component, sedimentation analysis, SDS-PAGE
-
trimer
-
2 * alpha + 1 * beta subunit, alpha subunits are hydroxylase components, beta subunit is the electron transfer component
trimer