Guanidinobutyrase

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In enzymology, a guanidinobutyrase (EC 3.5.3.7) is an enzyme that catalyzes the chemical reaction

4-guanidinobutanoate + H2O \rightleftharpoons 4-aminobutanoate + urea

Thus, the two substrates of this enzyme are 4-guanidinobutanoate and H2O, whereas its two products are 4-aminobutanoate and urea.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is 4-guanidinobutanoate amidinohydrolase. Other names in common use include gamma-guanidobutyrase, 4-guanidinobutyrate amidinobutyrase, gamma-guanidinobutyrate amidinohydrolase, G-Base, GBH, and guanidinobutyrate ureahydrolase. This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, manganese.

[edit] References

  • IUBMB entry for 3.5.3.7
  • BRENDA references for 3.5.3.7 (Recommended.)
  • PubMed references for 3.5.3.7
  • PubMed Central references for 3.5.3.7
  • Google Scholar references for 3.5.3.7
  • Mora J, Tarrab R, Martuscelli J, Soberon G (1965). "Characteristics of arginases from ureotelic and non-ureotelic animals". Biochem. J. 96: 588–94. PMID 5862400. 
  • Nguyen Van Thoai Thome-Beau F, Olomucki A (1966). "[Induction and specificity of enzymes of the new catabolic arginine pathway]". Biochim. Biophys. Acta. 115: 73–80. PMID 5936244. 
  • Yorifuji T, Kato M, Kobayashi T, Ozaki S and Ueno S (1980). "4-Guanidinobutyrate amidinohydrolase from Pseudomonas sp ATCC 14676: purification to homogeneity and properties". Agric. Biol. Chem. 44: 1127–1134. 
  • K (1983). "Distribution of amidinohydrolases among Pseudomonas and comparative studies of some purified enzymes by one-dimensional peptide mapping". Agric. Biol. Chem. 47: 2825–2830. 

[edit] External links

The CAS registry number for this enzyme class is 9013-69-8.

[edit] Gene Ontology (GO) codes