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
-
1,2-dioxygenase
- 2-hydroxypenta-2,4-dienoate
- molecular biology
- cumene
-
oxyanion
- 2,3-dihydroxybiphenyl
-
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
ECTree
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Engineering
Engineering on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase
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C261A
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2fold decreased turnover rate, Cys-261 seems to be not involved in catalysis
H114A
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reduced activity, is able to accept the 6-phenyl-containing substrate, on a shorter time scale
H263A
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overal structure similar, but asymmetry of the enzyme dimer more pronounced than for the native enzyme
R188Q
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first step of enzyme reaction, keto-enol tautomerization, becomes rate-limiting, 11fold increased Km value, 300fold decreased turnover rate
S114A
H265A
H265Q
R190K
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similar Km value as wild-type, 700fold decreased turnover rate
R190Q
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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
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
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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
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H265A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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
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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
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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ca. 40fold reduction in activity for the His tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
S114A
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ca. 40fold reduction in activity for the His tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
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