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Literature summary for 1.4.3.19 extracted from

  • Settembre, E.C.; Dorrestein, P.C.; Park, J.H.; Augustine, A.M.; Begley, T.P.; Ealick, S.E.
    Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis (2003), Biochemistry, 42, 2971-2981.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.12
-
Gly
-
Bacillus subtilis
1.17
-
cyclopropylglycine
-
Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclopropylglycine + H2O + O2 Bacillus subtilis enzyme is required for the biosynthesis of the thiazole moiety of thiamine diphosphate ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O31616
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclopropylglycine + H2O + O2
-
Bacillus subtilis ?
-
?
cyclopropylglycine + H2O + O2 enzyme is required for the biosynthesis of the thiazole moiety of thiamine diphosphate Bacillus subtilis ?
-
?
D-Ala + H2O + O2 no activity with D-Ala Bacillus subtilis pyruvate + NH3 + H2O2
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.4
-
D-Ala
-
Bacillus subtilis
1.14
-
cyclopropylglycine
-
Bacillus subtilis
1.2
-
Gly
-
Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
FAD FAD-dependent enzyme Bacillus subtilis