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Literature summary extracted from

  • Noguchi, E.; Nishikimi, M.; Yagi, K.
    Studies on the sulfhydryl group of L-galactonolactone oxidase (1981), J. Biochem., 90, 33-38.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.12 2,2'-dipyridyl disulfide
-
 Saccharomyces cerevisiae
1.3.3.12 4,4'-dipyridyl disulfide
-
 Saccharomyces cerevisiae
1.3.3.12 5,5'-dithiobis(2-nitrobenzoate)
-
 Saccharomyces cerevisiae
1.3.3.12 HgCl2
-
 Saccharomyces cerevisiae
1.3.3.12 iodoacetamide
-
 Saccharomyces cerevisiae
1.3.3.12 N-ethylmaleimide
-
 Saccharomyces cerevisiae
1.3.3.12 PCMB
-
 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.12 L-galactono-1,4-lactone + O2 Saccharomyces cerevisiae
-
 L-ascorbate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.12 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.12
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.12 L-galactono-1,4-lactone + O2
-
 Saccharomyces cerevisiae L-ascorbate + H2O2
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.3.12 FAD enzyme contains a covalently bound flavin Saccharomyces cerevisiae