Methylguanidinase

From Wikipedia, the free encyclopedia

In enzymology, a methylguanidinase (EC 3.5.3.16) is an enzyme that catalyzes the chemical reaction

methylguanidine + H₂O methylamine + urea

Thus, the two substrates of this enzyme are methylguanidine and H₂O, whereas its two products are methylamine 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 methylguanidine amidinohydrolase. This enzyme is also called methylguanidine hydrolase.

[edit] References

• IUBMB entry for 3.5.3.16
• BRENDA references for 3.5.3.16 (Recommended.)
• PubMed references for 3.5.3.16
• PubMed Central references for 3.5.3.16
• Google Scholar references for 3.5.3.16
• Nakajima M, Shirokane Y, Mizusawa K (1980). "A new amidinohydrolase, methylguanidine amidinohydrolase from Alcaligenes sp. N-42". FEBS. Lett. 110: 43–6. PMID 7353662. 

[edit] External links

The CAS registry number for this enzyme class is 73200-93-8.

• IUBMB entry for 3.5.3.16

• KEGG entry for 3.5.3.16

• BRENDA entry for 3.5.3.16

• NiceZyme view of 3.5.3.16

• EC2PDB: PDB structures for 3.5.3.16

• PRIAM entry for 3.5.3.16

• PUMA2 entry for 3.5.3.16

• IntEnz: Integrated Enzyme entry for 3.5.3.16

• MetaCyc entry for 3.5.3.16

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0050098: methylguanidinase

• AMIGO entry for GO code 0050098: methylguanidinase