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
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3.7.1.9
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catechols
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extradiol
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sphingomonas
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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2-hydroxy-6-oxohepta-2,4-dienoate
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lignin-related
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4-hydroxy-2-oxovalerate
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xylf
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paucimobilis
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5-carboxyvanillate
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4-oxalocrotonate
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m-cresol
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isopropylbenzene
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toluate
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3-methylcatechol
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molecular biology
- 3.7.1.9
- catechols
-
extradiol
- sphingomonas
- 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
- 2-hydroxy-6-oxohepta-2,4-dienoate
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lignin-related
- 4-hydroxy-2-oxovalerate
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xylf
- paucimobilis
- 5-carboxyvanillate
- 4-oxalocrotonate
- m-cresol
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isopropylbenzene
- toluate
- 3-methylcatechol
- molecular biology
Reaction
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
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Engineering
Engineering on EC 3.7.1.9 - 2-hydroxymuconate-6-semialdehyde hydrolase
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A129V
A129V/I199V/V227I
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combination of mutations incompatible for correct folding
D224A
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aggregates into inclusion bodies and thus can not be purified
F104M
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mutation does not have any significant effect on enzyme characteristics
H252A
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aggregates into inclusion bodies and thus can not be purified
I199V
I199V/V2271
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combination of mutations incompatible for correct folding
S103A
V227I
A129V
A129V/I199V/V227I
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combination of mutations incompatible for correct folding
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I199V
I199V/V2271
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combination of mutations incompatible for correct folding
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S103A
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the mutant has 100000fold lower activity than that of the wild type enzyme
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V227I
D224A
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aggregates into inclusion bodies and thus can not be purified
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H252A
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aggregates into inclusion bodies and thus can not be purified
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S103A
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has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
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C254S
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1% of the activity of wild-type enzyme, expressed at lower levels than the other mutant enzymes
D65V
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activity below detection. Unstable, decreases in cellular extrects after 10 min
F108M
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18% of the activity of wild-type enzyme, enzyme displays greater thermostability than the wild-type enzyme
H249A
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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
H36A
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15% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
S152A
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80% of the activity of wild-type enzyme, severe decrease in protein stability over that of the wild-type enzyme
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improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
A129V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate
I199V
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
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has 600000fold lower activity than that of the wild-type enzyme, can be found in the soluble fraction and thus can be purified
S103A
the mutant has 100000fold lower activity than that of the wild type enzyme
V227I
the kcat/Km value of the single mutant is higher than that of the wild type enzyme
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improved catalytic efficiency than the wild type enzyme, possesses a more appropiate binding pocket for substrates with smaller C6 substituents
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A129V
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the kcat/Km value of the single mutant is higher than that of the wild type enzyme. The mutant shows the highest kcat/Km value for 2-hydroxy-6-oxohepta-2,4-dienoate
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I199V
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the kcat/Km value of the single mutant is higher than that of the wild type enzyme
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V227I
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the kcat/Km value of the single mutant is higher than that of the wild type enzyme
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