EC Number |
Natural Substrates |
---|
1.1.3.8 | L-gulono-1,4-lactone + O2 |
- |
1.1.3.8 | L-gulono-1,4-lactone + O2 |
key enzyme for L-ascorbic acid biosynthesis |
1.1.3.8 | L-gulono-1,4-lactone + O2 |
the enzyme has a configurational specificity for the hydroxyl group at C(2) |
1.1.3.8 | L-gulono-1,4-lactone + O2 |
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. Through this process, 2-oxo-l-gulono-gamma-lactone and hydrogen peroxide are produced, and L-ascorbic acid is formed by nonenzymatic isomerisation of the former product |
1.1.3.8 | more |
examination of metabolic role of vitamin C synthesis in cells or animals that, during evolution, have lost the ability to make ascorbic acid |
1.1.3.8 | more |
presence of a alternative pathway for vitamin C production in plants which can circumvent steps of the D-mannose pathway |
1.1.3.8 | more |
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37 |