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3.7.1.9: 2-hydroxymuconate-6-semialdehyde hydrolase

This is an abbreviated version!
For detailed information about 2-hydroxymuconate-6-semialdehyde hydrolase, go to the full flat file.

Word Map on EC 3.7.1.9

Reaction

2-hydroxymuconate-6-semialdehyde
+
H2O
=
formate
 +
2-oxopent-4-enoate

Synonyms

1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase, 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate, 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase, 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase, 2-hydroxymuconate semialdehyde hydrolase, 2-hydroxymuconate-semialdehyde hydrolase, 2-hydroxymuconic semialdehyde hydrolase, 6-isopropyl-HODA hydrolase, CumD, HcdC, HMSH, HOD, HOD hydrolase, hydrolase, 2-hydroxymuconate semialdehyde, hydroxymuconic semialdehyde hydrolase, meta-cleavage compound hydrolase, meta-cleavage product hydrolase, MfhA, TodF, XylF

ECTree

     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.9 2-hydroxymuconate-6-semialdehyde hydrolase

Engineering

Engineering on EC 3.7.1.9 - 2-hydroxymuconate-6-semialdehyde hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D233A
-
residual activity of 62.6%
S101A
-
residual activity of 43.1%
D233A
-
residual activity of 62.6%
-
S101A
-
residual activity of 43.1%
-
A129V
A129V/I199V/V227I
-
combination of mutations incompatible for correct folding
D224A
-
aggregates into inclusion bodies and thus can not be purified
F104M
-
mutation does not have any significant effect on enzyme characteristics
H252A
-
aggregates into inclusion bodies and thus can not be purified
I199V
I199V/V2271
-
combination of mutations incompatible for correct folding
S103A
S34A
-
lower Km and turnover rates compared to wild-type
S34G
-
lower Km and turnover rates compared to wild-type
V227I
A129V
A129V/I199V/V227I
-
combination of mutations incompatible for correct folding
-
I199V
I199V/V2271
-
combination of mutations incompatible for correct folding
-
S103A
-
the mutant has 100000fold lower activity than that of the wild type enzyme
-
V227I
D224A
-
aggregates into inclusion bodies and thus can not be purified
-
H252A
-
aggregates into inclusion bodies and thus can not be purified
-
S103A
-
has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
-
C254S
-
1% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes
D228A
-
activity below detection
D65V
-
activity below detection. Unstable, decreases in cellular extrects after 10 min
F108M
-
18% of the activity of wild-type enzyme, enzyme displays greater thermostability than the wild-type enzyme
H249A
-
26% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes, severe decrease in protein stability compared to wild-type enzyme
H256A
-
activity below detection
H36A
-
15% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
S107A
-
activity below detection
S107C
-
0.44% of the activity of wild-type enzyme
S152A
-
80% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme