title: L-threo-3,4-dihydroxyphenylserine (DOPS) aldolase: a new enzyme cleaving DOPS into protocatechualdehyde and glycine.
abstract: An enzyme which cleaves L-threo-3,4-dihydroxyphenylserine into protocatechualdehyde and glycine was demonstrated in extracts of human brains. Equimolar production of protocachualdehyde and glycine was quantitatively confirmed using high-performance liquid chromatography. In subcellular fractions of the brain, the highest enzyme activity was found in cytosol and soluble fraction. L-threo-DOPS proved to be the best substrate for this enzyme. The L-erythroisomer was less active and D-threo- and D-erythro-isomers were essentially inactive. The enzyme activity has an optimal pH around 7.4, and requires pyridoxal phosphate for maximal activity.
mesh_terms: D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors; D000446:Aldehyde-Lyases / Q000378:metabolism*; D001547:Benzaldehydes / Q000378:metabolism; D002396:Catechols / Q000378:metabolism; D002540:Cerebral Cortex / Q000201:enzymology*; D015103:Droxidopa / Q000378:metabolism*; D005998:Glycine / Q000378:metabolism; D006801:Humans; D012694:Serine / Q000031:analogs & derivatives*; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D001547:Benzaldehydes; D002396:Catechols; D012694:Serine; C005581:protocatechualdehyde; D000444:Aldehyde Dehydrogenase; C051902:3,4-dihydroxyphenylserine aldolase; D000446:Aldehyde-Lyases; D015103:Droxidopa; D005998:Glycine