1.3.1.32: maleylacetate reductase
This is an abbreviated version!
For detailed information about maleylacetate reductase, go to the full flat file.
Word Map on EC 1.3.1.32
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1.3.1.32
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chlorocatechols
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cycloisomerase
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dienelactone
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2,4-dichlorophenoxyacetate
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chloroaromatic
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2-chloromaleylacetate
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resorcinol
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chloromuconate
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hydroxyquinol
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eutrophus
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intradiol
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beta-ketoadipate
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3-chlorobenzoate
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4-chlorocatechol
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lysr-type
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cis-dienelactone
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muconate
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dehalogenation
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sphingobium
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trans-dienelactone
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opacus
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chlorophenolicum
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4-fluorobenzoate
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protoanemonin
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2-chloro
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biotechnology
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environmental protection
- 1.3.1.32
- chlorocatechols
-
cycloisomerase
- dienelactone
- 2,4-dichlorophenoxyacetate
-
chloroaromatic
- 2-chloromaleylacetate
- resorcinol
-
chloromuconate
- hydroxyquinol
- eutrophus
-
intradiol
-
beta-ketoadipate
- 3-chlorobenzoate
- 4-chlorocatechol
-
lysr-type
- cis-dienelactone
- muconate
-
dehalogenation
-
sphingobium
- trans-dienelactone
- opacus
- chlorophenolicum
- 4-fluorobenzoate
- protoanemonin
-
2-chloro
- biotechnology
- environmental protection
Reaction
Synonyms
GraC, hadD, hqdD, HqoD, HxqD, MAA reductase, maleoylacetate reductase, maleylacetate reductase, MAR, PcpE, pdcF, PnpD, TcpD, tfdF, tsdD
ECTree
1.3.1.32 maleylacetate reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.3.1.32 - maleylacetate reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H172A
H236A
H237A
H241A
H251A
K140A
K238A
H172A
H237A
H241A
H251A
K238A
H236A
kcat/Km for 2-maleylacetate is 2.3fold higher as compared to wild-type value
H236A
mutation increases the catalytic efficiency (kcat/Km) of the enzyme (PcpE) by more than 2fold
H237A
kcat/Km for 2-maleylacetate is 3.2fold lower as compared to wild-type value
H237A
Km and kcat are augmented with a reduction in the catalytic efficiency kcat/Km
H241A
kcat/Km for 2-maleylacetate is 1.2fold lower as compared to wild-type value
H241A
Km and kcat are augmented with a reduction in the catalytic efficiency kcat/Km
H251A
kcat/Km for 2-maleylacetate is 2.6fold lower as compared to wild-type value
H251A
Km and kcat are augmented with a reduction in the catalytic efficiency kcat/Km
K140A
kcat/Km for 2-maleylacetate is 5.3fold lower as compared to wild-type value
K140A
the mutant exhibits a 4fold increase in Km and a slight decrease in kcat compared to the wild type enzyme, resulting in a 5.3-fold decrease of the catalytic efficiency kcat/Km
H237A
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kcat/Km for 2-maleylacetate is 3.2fold lower as compared to wild-type value
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H237A
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Km and kcat are augmented with a reduction in the catalytic efficiency kcat/Km
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H241A
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kcat/Km for 2-maleylacetate is 1.2fold lower as compared to wild-type value
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H241A
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Km and kcat are augmented with a reduction in the catalytic efficiency kcat/Km
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H251A
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kcat/Km for 2-maleylacetate is 2.6fold lower as compared to wild-type value
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H251A
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Km and kcat are augmented with a reduction in the catalytic efficiency kcat/Km
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