Diamine transaminase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 2.6.1.29
- BRENDA references for 2.6.1.29 (Recommended.)
- PubMed references for 2.6.1.29
- PubMed Central references for 2.6.1.29
- Google Scholar references for 2.6.1.29
- Kim K (1964). "Purification and properties of a diamine alpha-ketoglutarate transaminase from Escherichia coli". J. Biol. Chem. 239: 783–786.
[edit] External links
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- The CAS registry number for this enzyme class is 9031-83-8.