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L-threo-3,4-dihydroxyphenylserine (DOPS) aldolase: a new enzyme cleaving DOPS into protocatechualdehyde and glycine.
Biochem Biophys Res Commun ; 143(2): 482-8, 1987 Mar 13.
Article in En | MEDLINE | ID: mdl-3105531
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.
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Collection: 01-internacional Database: MEDLINE Main subject: Serine / Cerebral Cortex / Droxidopa / Aldehyde-Lyases Limits: Humans Language: En Journal: Biochem Biophys Res Commun Year: 1987 Document type: Article
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Serine / Cerebral Cortex / Droxidopa / Aldehyde-Lyases Limits: Humans Language: En Journal: Biochem Biophys Res Commun Year: 1987 Document type: Article
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