1.1.3.8: L-gulonolactone oxidase
This is an abbreviated version!
For detailed information about L-gulonolactone oxidase, go to the full flat file.
Word Map on EC 1.1.3.8
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1.1.3.8
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l-ascorbic
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scurvy
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scurvy-prone
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levoglucosenone
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scorbutic
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dibenzothiophene
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shionogi
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lemongrass
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l-galactono-1,4-lactone
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nutrition
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medicine
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molecular biology
- 1.1.3.8
-
l-ascorbic
- scurvy
-
scurvy-prone
-
levoglucosenone
-
scorbutic
- dibenzothiophene
-
shionogi
-
lemongrass
- l-galactono-1,4-lactone
- nutrition
- medicine
- molecular biology
Reaction
Synonyms
At5g11540, AtGulLO2, AtGulLO3, AtGulLO5, GLO, GLOase, GulLO, GulLO3, GulLO5, GULO, gulonolactone oxidase, L-GulL oxidase, L-gulono-1,4-lactone dehydrogenase, L-gulono-1,4-lactone oxidase, L-gulono-gamma-lactone dehydrogenase, L-gulono-gamma-lactone oxidase, L-gulono-gamma-lactone: O2 oxidoreductase, L-gulono-gamma-lactone:oxidoreductase, L-gulonolactone oxidase, LGO
ECTree
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Cofactor
Cofactor on EC 1.1.3.8 - L-gulonolactone oxidase
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FAD
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8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis
FAD
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8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis
FAD
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8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis
FAD
the flavin adenine dinucleotide (FAD) binding domain comprises amino acids 21-155. FAD binds to the FAD binding domain via an 8-alpha-(N3-histidyl)-riboflavin linkage at the conserved histidine residue at position 54. During the catalytic reaction by Gulo, flavin accepts 2 electrons from the substrate l-gulono-gamma-lactone, thus undergoing a reduction, followed by oxidation through molecular oxygen, with the reaction presumably involving the ALO domain
flavin
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covalently bound, flavoenzyme