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
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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
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General Information
General Information on EC 1.3.1.32 - maleylacetate reductase
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evolution
malfunction
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cells bearing a disrupted hadD gene do not grow on plates with 2,4,6-TCP
metabolism
physiological function
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maleylacetate reductase is responsible for 2,4,6-trichlorophenol degradation in Ralstonia pickettii DTP0602
mutagenesis studies show that His172 and Lys238 are essential for the catalytic activity of the enzyme (PcpE). However,the mutation of His236 to an alanine can increase the catalytic efficiency (kcat/Km) of PcpE by more than 2fold, implying that PcpE is still in an early stage of molecular evolution. The enzyme (PcpE) exhibits an extremely low but detectable level of alcohol dehalogenase activity toward ethanol and supports the notion that it is evolved from an iron-containing alcohol dehydrogenase
evolution
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mutagenesis studies show that His172 and Lys238 are essential for the catalytic activity of the enzyme (PcpE). However,the mutation of His236 to an alanine can increase the catalytic efficiency (kcat/Km) of PcpE by more than 2fold, implying that PcpE is still in an early stage of molecular evolution. The enzyme (PcpE) exhibits an extremely low but detectable level of alcohol dehalogenase activity toward ethanol and supports the notion that it is evolved from an iron-containing alcohol dehydrogenase
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last enzyme in the pentachlorophenol biodegradation pathway
metabolism
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last enzyme in the pentachlorophenol biodegradation pathway
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