Adenosylmethionine cyclotransferase

In enzymology, an adenosylmethionine cyclotransferase (EC 2.5.1.4) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine 5'-methylthioadenosine + 2-aminobutan-4-olide
adenosylmethionine cyclotransferase
Identifiers
EC no.2.5.1.4
CAS no.9030-34-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Hence, this enzyme has one substrate, S-adenosyl-L-methionine, and two products, 5'-methylthioadenosine and 2-aminobutan-4-olide.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine alkyltransferase (cyclizing). This enzyme is also called adenosylmethioninase.

References

    • Mudd SH (January 1959). "Enzymatic cleavage of S-adenosylmethionine". The Journal of Biological Chemistry. 234 (1): 87–92. PMID 13610898.
    • Mudd SH (July 1959). "The mechanism of the enzymatic cleavage of S-adenosylmethionine to alpha-amino-gamma-butyrolactone". The Journal of Biological Chemistry. 234 (7): 1784–6. PMID 13672964.


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