Literature DB >> 3105531

L-threo-3,4-dihydroxyphenylserine (DOPS) aldolase: a new enzyme cleaving DOPS into protocatechualdehyde and glycine.

M Naoi, T Takahashi, N Kuno, T Nagatsu.   

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.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3105531     DOI: 10.1016/0006-291x(87)91379-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558.

Authors:  J Q Liu; S Ito; T Dairi; N Itoh; M Kataoka; S Shimizu; H Yamada
Journal:  Appl Environ Microbiol       Date:  1998-02       Impact factor: 4.792

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.