1.14.13.242: 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase
This is an abbreviated version!
For detailed information about 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.242
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1.14.13.242
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flavin
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flavoproteins
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fad
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hydroxylases
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mesorhizobium
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flavoenzyme
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electrophilic
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loti
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acyclic
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flavin-dependent
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ring-cleavage
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hydride
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isoalloxazine
- 1.14.13.242
- flavin
- flavoproteins
- fad
- hydroxylases
-
mesorhizobium
-
flavoenzyme
-
electrophilic
- loti
-
acyclic
-
flavin-dependent
-
ring-cleavage
-
hydride
- isoalloxazine
Reaction
Synonyms
2-methyl-3-hydroxypyridine 5-carboxylic acid dioxygenase, 2-methyl-3-hydroxypyridine 5-carboxylic acid oxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, 3-hydroxy-2-methylpyridine carboxylate dioxygenase, 3-hydroxy-2-methylpyridinecarboxylate dioxygenase, EC 1.14.12.4, methylhydroxypyridine carboxylate dioxygenase, methylhydroxypyridinecarboxylate oxidase, MHPCO, mlr6788
ECTree
1.14.13.242 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.13.242 - 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Y270A
Y270F
Y270A
Y270F
Y270A
Y270F
Y223E
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the mutant shows reduced activity compared to the wild type enzyme
Y223F
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the mutant shows reduced activity compared to the wild type enzyme
Y223H
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the mutant shows reduced activity compared to the wild type enzyme
Y223T
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the mutant shows reduced activity compared to the wild type enzyme
Y82F
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the mutant shows reduced activity compared to the wild type enzyme
Y82H
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the mutant shows reduced activity compared to the wild type enzyme
Y82R
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the mutant shows reduced activity compared to the wild type enzyme
Y270A
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270A
less than 0.1% of the pyridine ring cleavage capacity of wild-type
Y270F
the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
Y270F
about 1.5% of the pyridine ring cleavage capacity of wild-type
Y270A
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the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
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Y270A
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less than 0.1% of the pyridine ring cleavage capacity of wild-type
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Y270F
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the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
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Y270F
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about 1.5% of the pyridine ring cleavage capacity of wild-type
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Y270A
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the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
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Y270A
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less than 0.1% of the pyridine ring cleavage capacity of wild-type
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Y270F
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the mutant shows reduced ring opening activity but increased NADH oxidation activity compared to the wild type enzyme
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Y270F
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about 1.5% of the pyridine ring cleavage capacity of wild-type
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