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Diamine transaminase

From Wikipedia, the free encyclopedia
diamine transaminase
Identifiers
EC no.2.6.1.29
CAS no.9031-83-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a diamine transaminase (EC 2.6.1.29) is an enzyme that catalyzes the chemical reaction:

an alpha,omega-diamine + 2-oxoglutarate an omega-aminoaldehyde + L-glutamate

Thus, the two substrates of this enzyme are alpha,omega-diamine and 2-oxoglutarate, whereas its two products are omega-aminoaldehyde and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is diamine:2-oxoglutarate aminotransferase. Other names in common use include amine transaminase, amine-ketoacid transaminase, diamine aminotransferase, and diamine-ketoglutaric transaminase. This enzyme participates in urea cycle and metabolism of amino groups.

References

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  • Kim K (1964). "Purification and properties of a diamine alpha-ketoglutarate transaminase from Escherichia coli". J. Biol. Chem. 239: 783–786.