Glycine dehydrogenase

Nearly 10 other amino acid dehydrogenases in addition to the above-mentioned four enzymes have been characterized as summarized in Table 1. The presence of NAD-specific glycine dehydrogenase (EC 1.4.1.10), serine dehydrogenase (EC 1.4.1.7), and NADP-specific L-amino acid dehydrogenase (EC 1.4.1.5) have been reported, but they were not substantially characterized. Tiyptophan dehydrogenase (EC 1.4.1.19, TryDH) was shown to be present in spinach leaves and to catalyze the NAD- or NADP-dependent conversion of tryptophan into indolepyruvate [38]. The enzyme is activated by the addition of calcium... 

This enzyme [EC 1.5.1.17] catalyzes the reversible reaction of 2,2 -iminodipropanoate with water and NAD+ to produce alanine, pyruvate and NADH. In the reverse reaction, alanine can be replaced as a substrate by cysteine, serine, or threonine. Glycine acts very slowly as a substrate (that is, the reaction catalyzed by strombine dehydrogenase). 

Effect of treatment with glycine and L-camitine in medium-chain acyl-coenzyme A dehydrogenase deficiency. 

---