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Literature summary for 3.5.4.11 extracted from

  • Levenberg, B.; Hayaishi, O.
    A bacterial pterin deaminase (1959), J. Biol. Chem., 234, 955-961.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-amino-4-hydroxypteridin-6-carboxylic acid
-
Alcaligenes metalcaligenes
KF
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Alcaligenes metalcaligenes
NaF
-
Alcaligenes metalcaligenes
p-chloromercuribenzoate
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Alcaligenes metalcaligenes

Organism

Organism UniProt Comment Textmining
Alcaligenes metalcaligenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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Alcaligenes metalcaligenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-amino-4-hydroxypteridine + H2O i.e. pterin Alcaligenes metalcaligenes 2,4-dihydroxypteridine + NH3 i.e. lumazine ir
additional information Only pteridines possessing the pterin structure (i.e. the 2-amino and 4-hydroxyl functional groups) are deaminated. The nature of the substitution at carbon 6 is relatively unimportant. However, an hydroxyl group at this position results in an inactive substance. Carbon 7 must be unsubstituted, since blocking of this position by a methyl or carboxyl function destroys the ability of the pterin to serve as a substrate. An N-5-formylated and reduced pterin is not deaminated Alcaligenes metalcaligenes ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3 6.7 although the reaction proceeds in the complete absence of phosphate, the rate of deamination is slightly faster in phosphate than in Tris buffer Alcaligenes metalcaligenes