Guanidinopropionase

From Wikipedia, the free encyclopedia

In enzymology, a guanidinopropionase (EC 3.5.3.17) is an enzyme that catalyzes the chemical reaction

3-guanidinopropanoate + H₂O 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.

[edit] References

• IUBMB entry for 3.5.3.17
• BRENDA references for 3.5.3.17 (Recommended.)
• PubMed references for 3.5.3.17
• PubMed Central references for 3.5.3.17
• Google Scholar references for 3.5.3.17
• Yorifuji T, Sugai I, Matsumoto H and 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: 1361–1363. 

[edit] External links

The CAS registry number for this enzyme class is 68821-77-2.

• IUBMB entry for 3.5.3.17

• KEGG entry for 3.5.3.17

• BRENDA entry for 3.5.3.17

• NiceZyme view of 3.5.3.17

• EC2PDB: PDB structures for 3.5.3.17

• PRIAM entry for 3.5.3.17

• PUMA2 entry for 3.5.3.17

• IntEnz: Integrated Enzyme entry for 3.5.3.17

• MetaCyc entry for 3.5.3.17

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0047972: guanidinopropionase

• AMIGO entry for GO code 0047972: guanidinopropionase