Diamine transaminase
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
diamine transaminase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.29 | ||||||||
CAS no. | 9031-83-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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
- Kim K (1964). "Purification and properties of a diamine alpha-ketoglutarate transaminase from Escherichia coli". J. Biol. Chem. 239: 783–786.
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