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Beta-alanine—pyruvate transaminase

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Enzyme
beta-alanine-pyruvate transaminase
Beta-alanine-pyruvate transaminase homotetramer, Pseudomonas aeruginosa
Identifiers
EC no.2.6.1.18
CAS no.9030-47-1
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In enzymology, a beta-alanine-pyruvate transaminase (EC 2.6.1.18) is an enzyme that catalyzes the chemical reaction

L-alanine + 3-oxopropanoate {\displaystyle \rightleftharpoons } pyruvate + beta-alanine

Thus, the two substrates of this enzyme are L-alanine and 3-oxopropanoate, whereas its two products are pyruvate and beta-alanine.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:3-oxopropanoate aminotransferase. Other names in common use include beta-alanine-pyruvate aminotransferase, and beta-alanine-alpha-alanine transaminase. This enzyme participates in 4 metabolic pathways: alanine and aspartate metabolism, valine, leucine and isoleucine degradation, beta-alanine metabolism, and propanoate metabolism. It employs one cofactor, pyridoxal phosphate.

References

Transferase: nitrogenous groups (EC 2.6)
2.6.1: Transaminases
2.6.3: Oximinotransferases
2.6.99: Other
Enzymes
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Regulation
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