HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase
for references in articles please use BRENDA:EC3.7.1.8
Word Map on EC 3.7.1.8
- 3.7.1.8
- biphenyls
-
dioxygenase
- benzoate
- hopdas
- 2-hydroxypenta-2,4-dienoate
- cumene
- 2,3-dihydroxybiphenyl
-
1,2-dioxygenase
- molecular biology
-
fluorescens
-
oxyanion
- sphingomonas
- rhodococcus
- dibenzofuran
- xenovorans
-
extradiol
-
isopropylbenzene
-
ser-his-asp
-
polychlorinated
-
acyl-enzyme
-
2-hydroxymuconic
- 4-chlorobiphenyl
-
deacylation
- wittichii
-
carbanion
- degradation
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.7.1.8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
2,6-dioxo-6-phenylhexa-3-enoate hydrolase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
general base and nucleophilic catalytic reaction mechanisms, overview
-
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
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-C bonds in ketonic substances
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
102925-38-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
the enzyme belongs to the alpha/beta-hydrolase superfamily
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
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
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 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
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-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
-
-
-
-
?
4,5-9,10-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-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-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
-
-
?
4,5-9,10-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 SUBSTRATES
NATURAL PRODUCTS
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-oxopent-4-enoate + salicylate + H+
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
P47229
i.e. HOPDA
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
B5SU85
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
B5SU85
-
-
-
?
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
P47229
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
Q75WN8
-
-
-
?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
Q75WN8
-
-
-
?
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
?
-
P47229
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
?
-
Q75WN8
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
?
-
Q75WN8
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.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
competitively inhibits
additional information
-
no effects by n-propanol and 2-propanol
-
(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
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
-
-
0.31
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
0.0012
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148K; pH 7.0, 25°C, mutant M148V
0.0014
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148E; pH 7.0, 25°C, mutant M148L; pH 7.0, 25°C, mutant M148N
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
-
-
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
-
-
1.5
2,6-dioxo-6-phenylhexa-3-enoate
pH 7.0, 25°C, mutant M148S; pH 7.0, 25°C, mutant M148Y
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.7
-
pH 6.5: about 65% of maximal activity, pH 8.7: about 25% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
monomer
-
1 * 29000, isoenzyme H2, SDS-PAGE; 1 * 31000, isoenzyme H1, SDS-PAGE
monomer
-
1 * 29000, isoenzyme H2, SDS-PAGE; 1 * 31000, isoenzyme H1, SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 48 h, 10% loss of isoenzyme H1 activity, 20% loss of isoenzyme H2 activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
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, rapid acylation of the variant during C-C bond cleavage suggesting that the serinate forms via a substrate-assisted mechanism in the reaction
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 3.7.1.8)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
