3.7.1.8: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase
This is an abbreviated version!
For detailed information about 2,6-dioxo-6-phenylhexa-3-enoate hydrolase, go to the full flat file.
Word Map on EC 3.7.1.8
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3.7.1.8
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biphenyls
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hydrolases
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dioxygenase
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hopdas
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benzoate
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1,2-dioxygenase
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2-hydroxypenta-2,4-dienoate
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molecular biology
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cumene
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oxyanion
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2,3-dihydroxybiphenyl
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polychlorinated
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rhodococcus
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sphingomonas
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ring-hydroxylating
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2-hydroxy-6-oxohepta-2,4-dienoate
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2-hydroxymuconic
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4-chlorobiphenyl
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wittichii
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xenovorans
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extradiol
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ser-his-asp
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isopropylbenzene
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dibenzofuran
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acyl-enzyme
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carbanion
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degradation
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environmental protection
- 3.7.1.8
- biphenyls
- hydrolases
- dioxygenase
- hopdas
- benzoate
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1,2-dioxygenase
- 2-hydroxypenta-2,4-dienoate
- molecular biology
- cumene
-
oxyanion
- 2,3-dihydroxybiphenyl
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polychlorinated
- rhodococcus
- sphingomonas
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ring-hydroxylating
- 2-hydroxy-6-oxohepta-2,4-dienoate
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2-hydroxymuconic
- 4-chlorobiphenyl
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wittichii
- xenovorans
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extradiol
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ser-his-asp
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isopropylbenzene
- dibenzofuran
- acyl-enzyme
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carbanion
- degradation
- environmental protection
Reaction
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, HOHPDA hydrolase, HOPD hydrolase, HOPDA hydrolase, HPDA hydrolase, HsaD, hydrolase, 2,6-dioxo-6-phenylhexa-3-enoate, LigY, MCP hydrolase, meta-cleavage product hydrolase, MhpC
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General Information
General Information on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase
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evolution
malfunction
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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
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
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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
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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
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meta-cleavage product hydrolase BphD is the fourth enzyme of the biphenyl catabolic pathway
metabolism
A0A0H0ZQK0
the enzyme is involved in the biodegradation of biphenyl
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
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the enzyme is involved in the intracellular survival of pathogen Mycobacterium tuberculosis
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physiological function
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the enzyme catalyse the hydrolysis of vinylogous 1,5-diketone meta-cleavage products generated during the biodegradation of various aromatic compounds
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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
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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
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