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Information on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase
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3.7.1.8 2,6-dioxo-6-phenylhexa-3-enoate hydrolaseIUBMB Comments
Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase, by ring-fission at a -CO-C bond. Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp.
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Word Map
- 3.7.1.8
- biphenyls
- hydrolases
- dioxygenase
- hopdas
- benzoate
-
1,2-dioxygenase
- 2-hydroxypenta-2,4-dienoate
- sphingomonas
-
oxyanion
-
polychlorinated
- 2,3-dihydroxybiphenyl
- cumene
- molecular biology
- rhodococcus
- dibenzofuran
-
ser-his-asp
- xenovorans
- acyl-enzyme
- 4-chlorobiphenyl
-
ring-hydroxylating
- wittichii
-
isopropylbenzene
-
carbanion
- 2-hydroxy-6-oxohepta-2,4-dienoate
-
2-hydroxymuconic
-
extradiol
- degradation
- environmental protection
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2, 4-dienoate hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dieonic acid hydrolase, 6-phenyl HODA hydrolase, BphD, BphD enzyme, BphDP6, CarC, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid hydrolase
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase
2-hydroxy-6-oxo-6-phenylhexa-2,4-dieonic acid hydrolase
6-phenyl HODA hydrolase
BphD
BphD enzyme
BphDP6
CarC
HOPDA hydrolase
HPDA hydrolase
HsaD
MCP hydrolase
meta-cleavage product hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
mechanism may involve an Asp-Ser-His catalytic triad
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
formation of a catalytic intermediate carbanion during hydrolysis, the carbanion abstracts a proton from Ser112, thereby completing tautomerization and generating a serinate for nucleophilic attack on the C6-carbonyl, catalytic mechanism, overview. BphD is a half-site reactive enzyme with versatility of the Ser-His-Asp triad, role of the catalytic His in acylation and deacylation
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
general base and nucleophilic catalytic reaction mechanisms, overview
-
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
although MCP hydrolases have a catalytic serine in the active site, the mechanism proceeds via a geminal diol, rather than an acyl-enzyme intermediate, reaction mechanism of the hydrolysis reaction, overview. MCP hydrolases accept alternative nucleophiles in addition to water, and accepts hydroxylamine in the C-C cleavage reaction. The Ser-His-Asp triad containing enzyme BphD most likely shows the formation of a covalent acyl enzyme intermediate, reaction mechanism, overview
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
although MCP hydrolases have a catalytic serine in the active site, the mechanism proceeds via a geminal diol, rather than an acyl-enzyme intermediate, reaction mechanism of the hydrolysis reaction, overview. MCP hydrolases accept alternative nucleophiles in addition to water, and accepts hydroxylamine in the C-C cleavage reaction. The Ser-His-Asp triad containing enzyme BphD most likely shows the formation of a covalent acyl enzyme intermediate, reaction mechanism, overview
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
catalytic mechanism involving enol-to-keto tautomerization that consists of two elementary reactions, the calculated Boltzmann weighted average barriers favor a substrate-assisted acylation mechanism, and the most feasible acylation pathway involves a catalytic triad, Ser-His-Asp. The product (2-hydroxypenta-2,4-dienoic acid) of the acylation process is replaced by three water molecules, and one of which is involved in the deacylation process, quantum mechanics/molecular mechanics study, overview
-
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
although MCP hydrolases have a catalytic serine in the active site, the mechanism proceeds via a geminal diol, rather than an acyl-enzyme intermediate, reaction mechanism of the hydrolysis reaction, overview. MCP hydrolases accept alternative nucleophiles in addition to water, and accepts hydroxylamine in the C-C cleavage reaction. The Ser-His-Asp triad containing enzyme BphD most likely shows the formation of a covalent acyl enzyme intermediate, reaction mechanism, overview
-
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2,6-dioxo-6-phenylhexa-3-enoate benzoylhydrolase
Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase, by ring-fission at a -CO-C bond. Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp.
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CAS REGISTRY NUMBER
COMMENTARY
102925-38-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid + H2O
4-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
2-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,4-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,5-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2,4-dihydroxypenta-2,4-dienoic acid
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-4-chloro-2-hydroxypenta-2,4-dienoic acid
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E,4Z)-5-chloro-2-hydroxypenta-2,4-dienoic acid
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2Z)-3-chloro-2-hydroxypenta-2,4-dienoic acid
2,6-dihydroxy-6-phenylhexa-2,4-dienoate
benzaldehyde + (2E)-2-hydroxypenta-2,4-dienoic acid
2-hydroxy-6-oxo-6-(2,3-dihydroxyphenyl)-hexa-2,4-dienoate + H2O
2,3-dihydroxybenzoate + 2-oxopent-4-enoate + H+
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid + H2O
2-aminobenzoic acid + 2-hydroxypenta-2,4-dienoic acid
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-hydroxypenta-2,4-dienoate + benzoate
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
?
-
i.e. HOPDA
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + 2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
4,11-dicarboxy-8-hydroxy-9-methoxy-2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate + H2O
5-carboxyvanillate + 4-carboxy-2-hydroxypenta-2,4-dienoate
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
3-[(7aR)-7a-hydroxy-1,5-dioxooctahydro-1H-inden-4-yl]propanoic acid + (2Z,4Z)-5-hydroxyhexa-2,4-dienoic acid
4-nitrophenyl benzoate + H2O
4-nitrophenol + benzoate
-
the serine nucleophile is activated by the His-Asp dyad
-
-
?
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate + H2O
benzoate + ethyl 2-(acetyloxy)penta-2,4-dienoate
-
-
-
-
?
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate + H2O
benzoate + ethyl-2-(acetyloxy)penta-2,4-dienoate
-
-
-
-
?
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid + H2O
4-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid + H2O
4-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid + H2O
4-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid + H2O
4-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
2-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
2-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
2-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
2-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,4-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,4-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,5-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,5-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2,4-dihydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2,4-dihydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2,4-dihydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-4-chloro-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-4-chloro-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E,4Z)-5-chloro-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E,4Z)-5-chloro-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2Z)-3-chloro-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2Z)-3-chloro-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
2,6-dihydroxy-6-phenylhexa-2,4-dienoate
benzaldehyde + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
2,6-dihydroxy-6-phenylhexa-2,4-dienoate
benzaldehyde + (2E)-2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
enzyme BphD catalyses the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, and many substrate analogues
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
enzyme BphD catalyses the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, and many substrate analogues
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
enzyme BphD catalyses the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, and many substrate analogues
-
-
?
2-hydroxy-6-oxo-6-(2,3-dihydroxyphenyl)-hexa-2,4-dienoate + H2O
2,3-dihydroxybenzoate + 2-oxopent-4-enoate + H+
-
-
enzyme is involved in metabolism of 2,2'-dihydroxybiphenyl
-
?
2-hydroxy-6-oxo-6-(2,3-dihydroxyphenyl)-hexa-2,4-dienoate + H2O
2,3-dihydroxybenzoate + 2-oxopent-4-enoate + H+
-
-
enzyme is involved in metabolism of 2,2'-dihydroxybiphenyl
-
?
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid + H2O
2-aminobenzoic acid + 2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid + H2O
2-aminobenzoic acid + 2-hydroxypenta-2,4-dienoic acid
-
-
-
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-hydroxypenta-2,4-dienoate + benzoate
-
-
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-hydroxypenta-2,4-dienoate + benzoate
the enzyme is involved in the biodegradation of biphenyl
-
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-hydroxypenta-2,4-dienoate + benzoate
the enzyme (BphD) utilizes a water-assisted nucleophilic mechanism, which contains acylation and deacylation stages. In acylation reaction, an active site water molecule assists the proton transfer from Ser112 to the carbanion intermediate (substrate) by forming hydrogen bonds with Ser112 and His265, and this proton transfer is in concert with the nucleophilic attack of deprotonated Ser112 on the C6-carbonyl of substrate to form the acylated intermediate. In deacylation, the Asp237-His265 dyad acts as a general base to activate the hydrolytic water, whose nucleophilic attack leads to the collapses of acyl-enzyme intermediate. The acylation and deacylation process correspond to the highest energy barriers of 21.0 and 23.9 kcal/mol, respectively. During the catalytic reaction, the active site water and Asp237-His265 dyad play an important role for each elementary steps
-
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
-
-
enzyme is involved in metabolism of 2,2'-dihydroxybiphenyl
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
-
-
enzyme is involved in metabolism of 2,2'-dihydroxybiphenyl
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate
-
-
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-hydroxypenta-2,4-dienoate
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-hydroxypenta-2,4-dienoate
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-hydroxypenta-2,4-dienoate
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-hydroxypenta-2,4-dienoate
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
i.e. HOPDA, a biphenyl meta-cleavage product
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
i.e. HOPDA, a biphenyl meta-cleavage product
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
i.e. HOPDA
-
-
?
4,11-dicarboxy-8-hydroxy-9-methoxy-2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate + H2O
5-carboxyvanillate + 4-carboxy-2-hydroxypenta-2,4-dienoate
the enzyme is involved in the catabolism of 2,2'-dihydroxy-3,3'-dimethoxy-5,5'-dicarboxybiphenyl, a lignin-derived biphenyl
-
-
?
4,11-dicarboxy-8-hydroxy-9-methoxy-2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate + H2O
5-carboxyvanillate + 4-carboxy-2-hydroxypenta-2,4-dienoate
mechanism in which the metallocenter primarily catalyzes substrate tautomerization and the water required for the hydrolytic half-reaction is activated in a substrate-assisted manner
-
-
?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
3-[(7aR)-7a-hydroxy-1,5-dioxooctahydro-1H-inden-4-yl]propanoic acid + (2Z,4Z)-5-hydroxyhexa-2,4-dienoic acid
i.e. DSHA, a cholesterol meta-cleavage product
-
-
?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
3-[(7aR)-7a-hydroxy-1,5-dioxooctahydro-1H-inden-4-yl]propanoic acid + (2Z,4Z)-5-hydroxyhexa-2,4-dienoic acid
i.e. DSHA, a cholesterol meta-cleavage product
-
-
?
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
i.e. HOPODA, a HOPDA synthetic analogue
-
-
?
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
i.e. HOPODA, a HOPDA synthetic analogue
-
-
?
meta-ring fission intermediate + H2O
?
-
catalysis of the hydrolytic C-C cleavage on phenylpropionic acid pathway
-
-
?
meta-ring fission intermediate + H2O
?
-
catalysis of the hydrolytic C-C cleavage on biphenyl degradation pathway
-
-
?
additional information
?
-
-
faint activity towards 2-hydroxy-6-oxohepta-2,4-dienoate and 2-hydroxymuconic semialdehyde
-
-
?
additional information
?
-
-
faint activity towards 2-hydroxy-6-oxohepta-2,4-dienoate and 2-hydroxymuconic semialdehyde
-
-
?
additional information
?
-
key role of non-active-site residue Met148 on the catalytic efficiency of meta-cleavage product hydrolase BphD
-
-
?
additional information
?
-
key role of non-active-site residue Met148 on the catalytic efficiency of meta-cleavage product hydrolase BphD
-
-
?
additional information
?
-
MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon
-
-
?
additional information
?
-
enzyme BphD accepts small alcohols such as methanol, ethanol, n-propanol and 2-propanol as nucleophiles in C-C bond cleavage of 2,6-dioxo-6-phenylhexa-3-enoate, thereby directly forming benzoate esters.Iin addition to the hydrolysis of C-C bonds, BphD also hydrolyses the ester bond in para-substituted nitrophenyl benzoates
-
-
?
additional information
?
-
-
enzyme is involved in the degradation of biphenyl
-
-
?
additional information
?
-
-
enzyme is involved in the degradation of biphenyl
-
-
?
additional information
?
-
-
6-acryl-2-hydroxy-6-ketohexa-2,4-dienoic acids synthesized as substrates for C-C hydrolase BphD
-
-
?
additional information
?
-
-
first total synthesis of meta ring fission intermediates, 6-acryl-2-hydroxy-6-ketohexa-2,4-dienoic acids synthesized as substrates for C-C hydrolase BphD
-
-
?
additional information
?
-
-
first total synthesis of meta ring fission intermediates, 6-acryl-2-hydroxy-6-ketohexa-2,4-dienoic acids synthesized as substrates for C-C hydrolase BphD
-
-
?
additional information
?
-
-
6-acryl-2-hydroxy-6-ketohexa-2,4-dienoic acids synthesized as substrates for C-C hydrolase BphD
-
-
?
additional information
?
-
MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon
-
-
?
additional information
?
-
enzyme BphD accepts small alcohols such as methanol, ethanol, n-propanol and 2-propanol as nucleophiles in C-C bond cleavage of 2,6-dioxo-6-phenylhexa-3-enoate, thereby directly forming benzoate esters.Iin addition to the hydrolysis of C-C bonds, BphD also hydrolyses the ester bond in para-substituted nitrophenyl benzoates
-
-
?
additional information
?
-
MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon
-
-
?
additional information
?
-
enzyme BphD accepts small alcohols such as methanol, ethanol, n-propanol and 2-propanol as nucleophiles in C-C bond cleavage of 2,6-dioxo-6-phenylhexa-3-enoate, thereby directly forming benzoate esters.Iin addition to the hydrolysis of C-C bonds, BphD also hydrolyses the ester bond in para-substituted nitrophenyl benzoates
-
-
?
additional information
?
-
-
enzyme is involved in the degradative pathway for dibenzofuran
-
-
?
additional information
?
-
-
enzyme is involved in the degradative pathway for dibenzofuran
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-hydroxypenta-2,4-dienoate + benzoate
the enzyme is involved in the biodegradation of biphenyl
-
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
i.e. HOPDA
-
-
?
4,11-dicarboxy-8-hydroxy-9-methoxy-2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate + H2O
5-carboxyvanillate + 4-carboxy-2-hydroxypenta-2,4-dienoate
the enzyme is involved in the catabolism of 2,2'-dihydroxy-3,3'-dimethoxy-5,5'-dicarboxybiphenyl, a lignin-derived biphenyl
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
-
-
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
-
-
enzyme is involved in metabolism of 2,2'-dihydroxybiphenyl
-
?
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
-
-
enzyme is involved in metabolism of 2,2'-dihydroxybiphenyl
-
?
additional information
?
-
MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon
-
-
?
additional information
?
-
-
enzyme is involved in the degradation of biphenyl
-
-
?
additional information
?
-
-
enzyme is involved in the degradation of biphenyl
-
-
?
additional information
?
-
MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon
-
-
?
additional information
?
-
MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon
-
-
?
additional information
?
-
-
enzyme is involved in the degradative pathway for dibenzofuran
-
-
?
additional information
?
-
-
enzyme is involved in the degradative pathway for dibenzofuran
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+-dependent enzyme. 4,11-Dicarboxy-8-hydroxy-9-methoxy-2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate coordinates to the Zn2+ in a bidentate manner via the 1-carboxylate and 2-oxo groups
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
competitively inhibits
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
competitively inhibits
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
competetively inhibits the enzyme more effectively than (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
competitively inhibits
additional information
-
no effects by n-propanol and 2-propanol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00075
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.00104
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.14
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate
pH 7.0, 30°C
0.0033
4,11-dicarboxy-8-hydroxy-9-methoxy-2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate
pH 7, 25°C
0.31
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
pH 7.5, 25°C
0.00013
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid
-
-
0.00065
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid
-
-
0.00019
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
not chlorinated
0.00047
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
not chlorinated
0.00033
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.0129
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.00043
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.00046
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.0036
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.004
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.0049
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.018
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.00054
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.0069
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.00028
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148D
0.00044
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148S
0.00047
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148W
0.00058
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148R
0.00074
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148H
0.00075
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, wild-type enzyme
0.00078
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148I
0.00079
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148T
0.00097
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148C
0.0002
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, without methanol
0.0003
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
wild-type at 3.2°C
0.00085
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, with 494 mM methanol
0.002
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, with 12940 mM methanol
0.0028
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
S112C mutant at 25°C
0.008
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
pH 7.5, 25°C
0.0017
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
-
mutant D237N
0.002
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
-
His6-BphD
0.037
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
-
mutant H265A
0.0373
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
-
mutant S112A
additional information
additional information
-
values between 0.00013 and 0.00106 mM for processing of the 6-acryl-2-hydroxy-6-ketohexa-2,4-dienoic acid substrates
-
additional information
additional information
-
in the steady-state hydrolysis of HOPDA, kcat/Km values are independent of methanol concentration, while both kcat and Km values increase with methanol concentration, stopped-flow spectrophotometry and steady-state kinetics, overview
-
additional information
additional information
pre-steady-state kinetic burst of BphD
-
additional information
additional information
Michaelis-Menten steady-state kinetics, stopped-flow measurements
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
11.2
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.00059
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
11.61
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate
pH 7.0, 30°C
9.7
4,11-dicarboxy-8-hydroxy-9-methoxy-2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate
pH 7, 25°C
0.33
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
pH 7.5, 25°C
3.13
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid
-
-
33.7
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid
-
-
4.18
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
not chlorinated
7.6
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
not chlorinated
1.74
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
15.3
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
1.03
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.0089
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.0172
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
9.6
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, wild-type enzyme
0.066
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
pH 7.5, 25°C
0.27
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
S112C mutant at 25°C
0.98
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
wild-type at 3.2°C
2 - 8
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, with 12940 mM methanol
6.5
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
wild-type at 25°C
6.5
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, without methanol
26
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, with 494 mM methanol
0.0009
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
-
mutant S112A
0.0016
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
-
mutant H265A
0.028
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
-
mutant D237N
additional information
additional information
-
values between 0.88 and 5.85 s-1 for processing of the 6-acryl-2-hydroxy-6-ketohexa-2,4-dienoic acid substrates
-
additional information
additional information
-
in the steady-state hydrolysis of HOPDA, kcat/Km values are independent of methanol concentration, while both kcat and Km values increase with methanol concentration, stopped-flow spectrophotometry and steady-state kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
pH 7.5, 25°C
12800
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, wild-type enzyme
9
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
pH 7.5, 25°C
14
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, with 12940 mM methanol
31
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, with 494 mM methanol
32
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
pH 7.5, 25°C, recombinant wild-type BphD, without methanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0036
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.00057
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2600
-
in 0.05 mM 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid, 50 mM Tris, pH 7.5 at 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
pH 5.0: about 65% of maximal activity, pH 9.0: about 85% of maximal activity, pH 10.0: about 35 % of maximal activity
6.5 - 8.7
-
pH 6.5: about 65% of maximal activity, pH 8.7: about 25% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 55
15°C: about 45% of maximal activity, 55°C: about 70% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
rapid acylation of the H265Q variant during C-C bond cleavage suggests that the serinate forms via a substrate-assisted mechanism in the reaction
metabolism
physiological function
additional information
evolution
meta-cleavage product (MCP) hydrolases are members of the alpha/beta-hydrolase superfamily that utilize a Ser-His-Asp triad to catalyze the hydrolysis of a C?C bond
evolution
-
BphD belongs to meta-cleavage product (MCP) hydrolases which possesses an alpha/beta-hydrolase fold and utilizes a Ser-His-Asp triad during catalysis
evolution
the enzyme belongs to the alpha/beta-hydrolase superfamily
metabolism
-
BphD is a meta-cleavage product (MCP) hydrolase which catalyzes C-C bond fission in the aerobic catabolism of aromatic compounds by bacteria utilizing a Ser-His-Asp triad to catalyze hydrolysis via an acyl-enzyme intermediate
metabolism
BphD is the MCP hydrolase from the biphenyl degradation pathway and hydrolyzes 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to 2-hydroxypenta-2,4-dienoic acid (HPD) and benzoate
metabolism
-
meta-cleavage product hydrolase BphD is the fourth enzyme of the biphenyl catabolic pathway
metabolism
the enzyme is involved in the biodegradation of biphenyl
physiological function
the enzyme is involved in the intracellular survival of pathogen Mycobacterium tuberculosis
physiological function
the enzyme catalyse the hydrolysis of vinylogous 1,5-diketone meta-cleavage products generated during the biodegradation of various aromatic compounds
physiological function
the enzyme catalyse the hydrolysis of vinylogous 1,5-diketone meta-cleavage products generated during the biodegradation of various aromatic compounds
physiological function
the enzyme is involved in the catabolism of 2,2'-dihydroxy-3,3'-dimethoxy-5,5'-dicarboxybiphenyl, a lignin-derived biphenyl
physiological function
-
the enzyme is involved in the intracellular survival of pathogen Mycobacterium tuberculosis
physiological function
-
the enzyme catalyse the hydrolysis of vinylogous 1,5-diketone meta-cleavage products generated during the biodegradation of various aromatic compounds
additional information
-
energy profiles of three individual pathways along substrate-assisted acylation (Ser112-His265-Asp237 involved) and deacylation pathways
additional information
structure analysis of wild-type and mutant enzymes, and molecular dynamics simulations of wild-type enzyme and mutants M148R and M148W. The catalytic triad residues of enzyme BphD are Ser112, Asp237, and His265. The most stable salt bridge between subunits of BphD wild-type and BphD mutant M148P is Glu434-Arg719, which has 58% and 85% occupied percentages in each trajectory, respectively
additional information
-
structure analysis of wild-type and mutant enzymes, and molecular dynamics simulations of wild-type enzyme and mutants M148R and M148W. The catalytic triad residues of enzyme BphD are Ser112, Asp237, and His265. The most stable salt bridge between subunits of BphD wild-type and BphD mutant M148P is Glu434-Arg719, which has 58% and 85% occupied percentages in each trajectory, respectively
Show AA Sequence and Transmembrane Helices (667 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
29000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
octamer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant S114A in complex with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, 8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid, or 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid, sitting drop vapor diffusion, 0.001 ml of 8 mg/ml protein solution is mixed with 0.001 ml of precipitant solution containing 200 mM KSCN, 24% PEG 3350, and 100 mM bis-tris propane, pH 7.0, soaking of S114A crystals in 0.01 ml of precipitant solution supplemented with 15 mM of each ligand for 30-60 min, X-ray diffractin structure determination and analysis at 1.8-2.1 A resolution, molecular replacement
BphD H265Q and S112A/H265Q mutants in complex with substrate 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, sitting drop vapour diffusion method, 0.001 ml of protein solution containing 4 mg/ml protein in 20 mM HEPES, pH 7.5, 20°C, 9 days, is mixed with 0.001 ml of reservoir solution containing 2.4 M malonate at pH 6.0-7.0, X-ray diffraction structure determination and analysis at 1.3 A and 1.9 A resolutions, respectively
enzyme structure determination and analysis, PDB IDs 2OG1, 2PU5, 2RI6, 2PU7, 2PUH and 2PUJ
S112A and H265Q mutants crystal structure analysis, PDB IDs 2PUH and 3V1N, modeling
-
wild-type, the S112C variant and S112C incubated with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid by hanging drop vapor diffusion method at 20°C, to 1.6 A resolution, interaction between conserved active side residues and dienoate moiety of the substrate, the residue His265 is hydrogen-bonded to the 2-hydroxy/oxo substituent of the substrate, consistent with a role in catalyzing ketonization
-
at 2.4 A resolution, active-site residues are Ser110, Asp235 and His263, situated inside the cavity between the core and the lid domains, this substrate binding pocket has a hydrophobic and hydrophilic region
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C261A
-
2fold decreased turnover rate, Cys-261 seems to be not involved in catalysis
H114A
-
reduced activity, is able to accept the 6-phenyl-containing substrate, on a shorter time scale
H263A
-
overal structure similar, but asymmetry of the enzyme dimer more pronounced than for the native enzyme
R188Q
-
first step of enzyme reaction, keto-enol tautomerization, becomes rate-limiting, 11fold increased Km value, 300fold decreased turnover rate
S114A
H265A
H265Q
R190K
-
similar Km value as wild-type, 700fold decreased turnover rate
R190Q
-
14fold increased Km value, 400fold decreased turnover rate
S112A
S112A/H265Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S114A
S114A
active site HsaD mutant, catalytically impaired and binds 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid with an altered dissociation constant compared to the wild-type enzyme
S114A
-
active site HsaD mutant, catalytically impaired and binds 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid with an altered dissociation constant compared to the wild-type enzyme
H265A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H265Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme and does not show formation of the carbanion catalytic intermediate in contrast to the wild-type enzyme
H265Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, rapid acylation of the variant during C-C bond cleavage suggesting that the serinate forms via a substrate-assisted mechanism in the reaction
S112A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S114A
-
ca. 40fold reduction in activity for the His tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
S114A
-
ca. 40fold reduction in activity for the His tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
more than 60% of the activity is retained after incubation at pH 5.0-9.0 at 30°C for 10 min
755881
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
1 h, the enzyme retains more than 60% residual activity
60
60
1 h, the enzyme retains less than 60% residual activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 48 h, 10% loss of isoenzyme H1 activity, 20% loss of isoenzyme H2 activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
BphD mutants purified by affinity chromatography to more than 95% homogeneity
-
MhpC mutants purified by anion exchange chromatography to more than 95% homogeneity
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
BphD mutants expressed in a pET-14b vector as an N-terminal His6 fusion protein
-
expression in Escherichia coli
gene bphD, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
into the pET-14b vector, overexpression in Escherichia coli BL21(DE3) cells
-
overexpression in Pseudomonas putida KT2442 containing vector pSS316
-
overexpression of wild-type and mutant BphDs in Escherichia coli strain Rosetta(DE3)pLysS
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
environmental protection
potential enzyme resource for the biodegradation of biphenyl, bioremediation of the environmental pollution caused by biphenyl/polychlorinated biphenyls
molecular biology
degradation
-
key determinant in the aerobic transformation of polychlorinated biphenyls by divergent biphenyl degraders
degradation
-
key determinant in the aerobic transformation of polychlorinated biphenyls by divergent biphenyl degraders
molecular biology
-
open reading frame corresponding to the pcbD gene consists of 855 base pairs with an ATG initiation codon and a TGA termination codon, able to encode a polypeptide with a molecular weight of 31732 containing 284 amino acid residues, deduced amino acid sequence has 62% identity with those of the HOPDA hydrolases of Pseudomonas putida KF715, P. pseudoalcaligenes KF707, and Burkholderia cepacia LB400, and also significant homology with those of other hydrolytic enzymes including esterase, transferase, and peptidase
molecular biology
-
the deduced amino acid sequence of CarC shows 30.3, 31.3, and 31.8% identity with meta-cleavage compound hydrolases TodF, XylF, and DmpD, respectively, from other Pseudomonas
molecular biology
-
upstream of bphC are five ORFs, including bphD, exhibiting low homology with, and a different gene order from, previously characterized bph genes
molecular biology
-
the deduced amino acid sequence of CarC shows 30.3, 31.3, and 31.8% identity with meta-cleavage compound hydrolases TodF, XylF, and DmpD, respectively, from other Pseudomonas
molecular biology
-
open reading frame corresponding to the pcbD gene consists of 855 base pairs with an ATG initiation codon and a TGA termination codon, able to encode a polypeptide with a molecular weight of 31732 containing 284 amino acid residues, deduced amino acid sequence has 62% identity with those of the HOPDA hydrolases of Pseudomonas putida KF715, P. pseudoalcaligenes KF707, and Burkholderia cepacia LB400, and also significant homology with those of other hydrolytic enzymes including esterase, transferase, and peptidase
molecular biology
-
upstream of bphC are five ORFs, including bphD, exhibiting low homology with, and a different gene order from, previously characterized bph genes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Omori, T.; Sugimura, K.; Ishigooka, H.; Minoda, Y.
Purification and some propertiees of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolyzing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl
Agric. Biol. Chem.
50
931-937
1986
Pseudomonas cruciviae, Pseudomonas cruciviae S93 B1
-
brenda
Buenz, P.V.; Falchetto, R.; Cook, A.M.
Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran in Sphingomonas sp. strain RW1
Biodegradation
4
171-178
1993
Sphingomonas sp., Sphingomonas sp. RW1
brenda
Ahmad, S.; Fraser, J.; Sylvestre, M.; Larose, A.; Khan, A.; Bergeron, J.; Juteau, J.M.; Sondossi, M.
Sequence of the bphD gene encoding 2-hydroxy-6-oxo-(phenylchlorophenyl) hexa-2,4-dienoic acid (HOP/cPCA) hydrolase involved in the biphenyl/polychlorinated biphenyl degradation pathway in Comamonas testosteroni: evidence suggesting involvement of Ser112 in catalytic activity
Gene
156
69-74
1995
Comamonas testosteroni (Q59324)
brenda
Kim, E.; Kim, Y.; Kim, C.K.
Genetic structures of the genes encoding 2,3-dihydroxybiphenyl 1,2-dioxygenase and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase from biphenyl- and 4-chlorobiphenyl-degrading Pseudomonas sp. strain DJ-12
Appl. Environ. Microbiol.
62
262-265
1996
Pseudomonas sp., Pseudomonas sp. DJ-12
brenda
Lau, P.C.K.; Garnon, J.; Labbe, D.; Wang, Y.
Location and sequence analysis of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase-encoding gene (bpdF) of the biphenyl polychlorinated biphenyl degradation pathway in Rhodococcus sp. M5
Gene
171
53-57
1996
Rhodococcus sp.
brenda
Horsman, G.P.; Ke, J.; Dai, S.; Seah, S.Y.; Bolin, J.T.; Eltis, L.D.
Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway
Biochemistry
45
11071-11086
2006
Paraburkholderia xenovorans
brenda
Li, J.J.; Li, C.; Blindauer, C.A.; Bugg, T.D.
Evidence for a gem-diol reaction intermediate in bacterial C-C hydrolase enzymes BphD and MhpC from 13C NMR spectroscopy
Biochemistry
45
12461-12469
2006
Escherichia coli, Paraburkholderia xenovorans
brenda
Li, C.; Li, J.J.; Montgomery, M.G.; Wood, S.P.; Bugg, T.D.
Catalytic role for arginine 188 in the C-C hydrolase catalytic mechanism for Escherichia coli MhpC and Burkholderia xenovorans LB400 BphD
Biochemistry
45
12470-12479
2006
Escherichia coli, Paraburkholderia xenovorans
brenda
Speare, D.M.; Olf, P.; Bugg, T.D.
Hammett analysis of a C-C hydrolase-catalysed reaction using synthetic 6-aryl-2-hydroxy-6-ketohexa-2,4-dienoic acid substrates
Chem. Commun. (Camb. )
2002
2304-2305
2002
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Seah, S.Y.; Labbe, G.; Kaschabek, S.R.; Reifenrath, F.; Reineke, W.; Eltis, L.D.
Comparative specificities of two evolutionarily divergent hydrolases involved in microbial degradation of polychlorinated biphenyls
J. Bacteriol.
183
1511-1516
2001
Rhodococcus globerulus, Rhodococcus globerulus P6
brenda
Seah, S.Y.; Labbe, G.; Nerdinger, S.; Johnson, M.R.; Snieckus, V.; Eltis, L.D.
Identification of a serine hydrolase as a key determinant in the microbial degradation of polychlorinated biphenyls
J. Biol. Chem.
275
15701-15708
2000
Burkholderia cepacia, Burkholderia cepacia LB400
brenda
Lim, J.; Lee, J.; Lim, J.; Min, K.R.; Kim, C.; Kim, Y.
Characterization of the pcbD gene encoding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase from Pseudomonas sp. P20
J. Microbiol. Biotechnol.
10
258-263
2000
Pseudomonas sp., Pseudomonas sp. P20
-
brenda
Nandhagopal, N.; Yamada, A.; Hatta, T.; Masai, E.; Fukuda, M.; Mitsui, Y.; Senda, T.
Crystal structure of 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic acid (HPDA) hydrolase (BphD enzyme) from the Rhodococcus sp. strain RHA1 of the PCB degradation pathway
J. Mol. Biol.
309
1139-1151
2001
Rhodococcus sp. (Q9KWQ6), Rhodococcus sp., Rhodococcus sp. RHA1 (Q9KWQ6)
brenda
Mukerjee-Dhar, G.; Shimura, M.; Miyazawa, D.; Kimbara, K.; Hatta, T.
bph genes of the thermophilic PCB degrader, Bacillus sp. JF8: characterization of the divergent ring-hydroxylating dioxygenase and hydrolase genes upstream of the Mn-dependent BphC
Microbiology
151
4139-4151
2005
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) JF8
brenda
Speare, D.M.; Fleming, S.M.; Beckett, M.N.; Li, J.J.; Bugg, T.D.
Synthetic 6-aryl-2-hydroxy-6-ketohexa-2,4-dienoic acid substrates for C-C hydrolase BphD: investigation of a general base catalytic mechanism
Org. Biomol. Chem.
2
2942-2950
2004
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Riddle, R.R.; Gibbs, P.R.; Willson, R.C.; Benedik, M.J.
Purification and properties of 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid hydrolase involved in microbial degradation of carbazole
Protein Expr. Purif.
28
182-189
2003
Pseudomonas sp., Pseudomonas sp. LD2
brenda
Lack, N.; Yam, K.; Lowe, E.; Horsman, G.; Owen, R.; Sim, E.; Eltis, L.
Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism
J. Biol. Chem.
285
434-443
2010
Mycobacterium tuberculosis (P9WNH5), Mycobacterium tuberculosis H37Rv (P9WNH5)
brenda
Ruzzini, A.C.; Horsman, G.P.; Eltis, L.D.
The catalytic serine of MCP hydrolases is activated differently for C-O bond cleavage than for C-C bond cleavage
Biochemistry
51
5831-5840
2012
Paraburkholderia xenovorans
brenda
Ruzzini, A.C.; Ghosh, S.; Horsman, G.P.; Foster, L.J.; Bolin, J.T.; Eltis, L.D.
Identification of an acyl-enzyme intermediate in a meta-cleavage product hydrolase reveals the versatility of the catalytic triad
J. Am. Chem. Soc.
134
4615-4624
2012
Paraburkholderia xenovorans (P47229)
brenda
Kohler, H.P.; Schmid, A.; van der Maarel, M.
Metabolism of 2,2'-dihydroxybiphenyl by Pseudomonas sp. strain HBP1: production and consumption of 2,2',3-trihydroxybiphenyl
J. Bacteriol.
175
1621-8
1993
Pseudomonas sp., Pseudomonas sp. HBP1
brenda
Siirola, E.; Frank, A.; Grogan, G.; Kroutil, W.
C-C hydrolases for biocatalysis
Adv. Synth. Catal.
355
1677-1691
2013
Paraburkholderia xenovorans (P47229), Rhodococcus sp. (Q75WN8), Rhodococcus sp. RHA1 (Q75WN8)
-
brenda
Zhou, H.; Qu, Y.; Kong, C.; Shen, E.; Wang, J.; Zhang, X.; Ma, Q.; Zhou, J.
The key role of a non-active-site residue Met148 on the catalytic efficiency of meta-cleavage product hydrolase BphD
Appl. Microbiol. Biotechnol.
97
10399-10411
2013
Dyella ginsengisoli (B5SU85), Dyella ginsengisoli LA-4 (B5SU85)
brenda
Li, Y.; Zhang, R.; Du, L.; Zhang, Q.; Wang, W.
Insight into the catalytic mechanism of meta-cleavage product hydrolase BphD: a quantum mechanics/molecular mechanics study
RSC Adv.
5
66591-66597
2015
Paraburkholderia xenovorans
-
brenda
Kuatsjah, E.; Chan, A.; Hurst, T.; Snieckus, V.; Murphy, M.; Eltis, L.
Metal- and serine-dependent meta-cleavage product hydrolases utilize similar nucleophile-activation strategies
ACS Catal.
8
11622-11632
2018
Sphingobium sp. SYK-6 (G2IN02)
-
brenda
Jia, Y.; Wang, J.; Ren, C.; Nahurira, R.; Khokhar, I.; Wang, J.; Fan, S.; Yan, Y.
Identification and characterization of a meta-cleavage product hydrolase involved in biphenyl degradation from Arthrobacter sp. YC-RL1
Appl. Microbiol. Biotechnol.
103
6825-6836
2019
Arthrobacter sp. YC-RL1 (A0A0H0ZQK0)
brenda
Dong, L.; Zhang, S.; Liu, Y.
A water-assisted nucleophilic mechanism utilized by BphD, the meta-cleavage product hydrolase in biphenyl degradation
J. Mol. Graph. Model.
76
448-455
2017
Paraburkholderia xenovorans (P47229)
brenda
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