1.1.3.12: pyridoxine 4-oxidase
This is an abbreviated version!
For detailed information about pyridoxine 4-oxidase, go to the full flat file.
Word Map on EC 1.1.3.12
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1.1.3.12
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pyridoxal
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mesorhizobium
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loti
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fad
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synthesis
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chaperonins
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nitrogen-fixing
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luteolum
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microbacterium
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4-dehydrogenase
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symbiotic
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pyridoxamine
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pyridoxamine-pyruvate
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hydride
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aminotransferase
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glucose-methanol-choline
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fad-dependent
- 1.1.3.12
- pyridoxal
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mesorhizobium
- loti
- fad
- synthesis
- chaperonins
-
nitrogen-fixing
- luteolum
-
microbacterium
-
4-dehydrogenase
-
symbiotic
- pyridoxamine
-
pyridoxamine-pyruvate
-
hydride
- aminotransferase
-
glucose-methanol-choline
-
fad-dependent
Reaction
Synonyms
oxidase, pyridoxol 4-, PN 4-oxidase, PNO, PNOX, pyridoxin 4-oxidase, pyridoxine-4-oxidase, pyridoxol 4-oxidase
ECTree
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General Information
General Information on EC 1.1.3.12 - pyridoxine 4-oxidase
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evolution
the enzyme belongs to the glucose methanol choline (GMC) oxidoreductase family of enzymes. Active site Pro504 in PNOX corresponds to Asn or His of the conserved His-Asn or His-His pair in other GMC oxidoreductase active sites
metabolism
additional information
first enzyme in pathway I for the degradation of pyridoxine
in the active site, His460, His462, and Pro504 are located on the re-face of the isoalloxazine ring of FAD, pyridoxamine binds to the active site through several hydrogen bonds, mode, overview. His462 may act as a general base for the abstraction of a proton from the 4'-hydroxyl of pyridoxine. His460 may play a role in the binding and positioning of pyridoxine
additional information
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in the active site, His460, His462, and Pro504 are located on the re-face of the isoalloxazine ring of FAD, pyridoxamine binds to the active site through several hydrogen bonds, mode, overview. His462 may act as a general base for the abstraction of a proton from the 4'-hydroxyl of pyridoxine. His460 may play a role in the binding and positioning of pyridoxine