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L-serine ammonia-lyase

The enzyme <small>L</small>-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction

<small>L</small>-serine = pyruvate + NH<sub>3</sub> (overall reaction)
:(1a) <small>L</small>-serine = 2-aminoprop-2-enoate + H<sub>2</sub>O
:(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
:(1c) 2-iminopropanoate + H<sub>2</sub>O = pyruvate + NH<sub>3</sub> (spontaneous)

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

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .

References