L-serine ammonia-lyase

In enzymology, a L-serine ammonia-lyase (EC number|4.3.1.17) is an enzyme that catalyzes the chemical reaction

:L-serine $ightleftharpoons$ pyruvate + NH₃

Hence, this enzyme has one substrate, L-serine, and two products, pyruvate and NH₃.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine and threonine metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.

tructural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1P5J, PDB link|1PWE, PDB link|1PWH, and PDB link|2IQQ.

References

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External links

Gene Ontology (GO) codes