In enzymology, a guanidinopropionase (EC 3.5.3.17) is an enzyme that catalyzes the chemical reaction
3-guanidinopropanoate + H2O ⇌ {\displaystyle \rightleftharpoons } beta-alanine + urea Thus, the two substrates of this enzyme are 3-guanidinopropanoate and H2O, whereas its two products are beta-alanine 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 3-guanidinopropanoate amidinopropionase. Other names in common use include GPase and GPH. It employs one cofactor, manganese.
References
Yorifuji T, Sugai I, Matsumoto H, Tabuchi A (1982). "Characterization of 3-guanidinopropionate amidinohydrolase from Pseudomonas aeruginosa and a comparative study with 4- guanidinobutyrate amidinohydrolase from another Pseudomonas". Agric. Biol. Chem. 46 (5): 1361–1363. doi:10.1271/bbb1961.46.1361.
