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Literature summary extracted from

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.11 2-amino-4-hydroxypteridin-6-carboxylic acid
-
 Alcaligenes metalcaligenes
3.5.4.11 KF
-
 Alcaligenes metalcaligenes
3.5.4.11 NaF
-
 Alcaligenes metalcaligenes
3.5.4.11 p-chloromercuribenzoate
-
 Alcaligenes metalcaligenes

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.11 Alcaligenes metalcaligenes
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.4.11
-
 Alcaligenes metalcaligenes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.11 2-amino-4-hydroxypteridine + H2O i.e. pterin Alcaligenes metalcaligenes 2,4-dihydroxypteridine + NH3 i.e. lumazine ir
3.5.4.11 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.11 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