Guanidinoacetase

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
guanidinoacetase
Identifiers
EC number 3.5.3.2
CAS number 9024-92-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a guanidinoacetase (EC 3.5.3.2) is an enzyme that catalyzes the chemical reaction

guanidinoacetate + H2O glycine + urea

Thus, the two substrates of this enzyme are guanidinoacetate and H2O, whereas its two products are glycine 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 guanidinoacetate amidinohydrolase. This enzyme is also called glycocyaminase. It employs one cofactor, manganese.

References[edit]

  • ROCHE J, LACOMBE G, GIRARD H (1950). "[On the specificity of certain bacterial deguanidases generating urea and on arginindihydrolase.]". Biochim. Biophys. Acta. 6 (1): 210–6. doi:10.1016/0006-3002(50)90093-x. PMID 14791411. 
  • Yorifuji T, Tamai H, Usami H (1977). "Purification, crystallization and properties of Mn2+ dependent guanidoacetate amidinohydrolase from a Pseudomonas". Agric. Biol. Chem. 41 (6): 959–966. doi:10.1271/bbb1961.41.959.