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Methylguanidinase

From Wikipedia, the free encyclopedia
methylguanidinase
Identifiers
EC no.3.5.3.16
CAS no.73200-93-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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.

References

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  • Nakajima M, Shirokane Y, Mizusawa K (1980). "A new amidinohydrolase, methylguanidine amidinohydrolase from Alcaligenes sp. N-42". FEBS Lett. 110 (1): 43–6. doi:10.1016/0014-5793(80)80018-4. PMID 7353662.