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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

Reaction

2,6-dioxo-6-phenylhexa-3-enoate
+
H2O
=
benzoate
 +
2-oxopent-4-enoate

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

     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.8 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

Engineering

Engineering on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D247A
A0A0H0ZQK0
mutant enzyme retains 29.93% enzyme activity
H275A
A0A0H0ZQK0
mutant enzyme retains 10.25% enzyme activity
S115A
A0A0H0ZQK0
mutant enzyme retains 28.92% enzyme activity
S112A
inactive enzyme
M148A
site-directed mutagenesis of the non-active-site residue
M148C
site-directed mutagenesis of the non-active-site residue
M148D
site-directed mutagenesis of the non-active-site residue
M148E
site-directed mutagenesis of the non-active-site residue
M148F
site-directed mutagenesis of the non-active-site residue
M148G
site-directed mutagenesis of the non-active-site residue
M148H
site-directed mutagenesis of the non-active-site residue
M148I
site-directed mutagenesis of the non-active-site residue
M148K
site-directed mutagenesis of the non-active-site residue
M148L
site-directed mutagenesis of the non-active-site residue
M148N
site-directed mutagenesis of the non-active-site residue
M148P
site-directed mutagenesis of the non-active-site residue
M148Q
site-directed mutagenesis of the non-active-site residue
M148R
site-directed mutagenesis of the non-active-site residue
M148S
site-directed mutagenesis of the non-active-site residue
M148T
site-directed mutagenesis of the non-active-site residue
M148V
site-directed mutagenesis of the non-active-site residue
M148W
site-directed mutagenesis of the non-active-site residue
M148Y
site-directed mutagenesis of the non-active-site residue
M148A
-
site-directed mutagenesis of the non-active-site residue
-
M148D
-
site-directed mutagenesis of the non-active-site residue
-
M148L
-
site-directed mutagenesis of the non-active-site residue
-
M148P
-
site-directed mutagenesis of the non-active-site residue
-
M148W
-
site-directed mutagenesis of the non-active-site residue
-
C261A
-
2fold decreased turnover rate, Cys-261 seems to be not involved in catalysis
F173D
-
1.5fold increased Km value, 100fold decreased turnover rate
F173G
-
8fold increased Km value, 3.5fold decreased turnover rate
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
N109A
-
similar Km value as wild-type, 200fold decreased turnover rate
N109H
-
similar Km value as wild-type, 350fold decreased turnover rate
R188K
-
5fold increased Km value,35fold decreased turnover rate
R188Q
-
first step of enzyme reaction, keto-enol tautomerization, becomes rate-limiting, 11fold increased Km value, 300fold decreased turnover rate
W264G
-
16fold increased Km value, 10fold decreased turnover rate
S114A
D237N
-
reduced activity
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
S112C
-
lower enzyme activity
S114A