A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC
4.2.1.14, D-serine dehydratase) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC
3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine.