4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B-6 biosynthesis

被引：53

作者：

Drewke, C ^{[1
]}

Klein, M ^{[1
]}

Clade, D ^{[1
]}

Arenz, A ^{[1
]}

Muller, R ^{[1
]}

Leistner, E ^{[1
]}

机构：

[1] UNIV BONN,INST PHARMAZEUT BIOL,D-53115 BONN,GERMANY

来源：

FEBS LETTERS | 1996年 / 390卷 / 02期

关键词：

Escherichia coli; vitamin B-6; pyridoxal phosphate; 3-O-phospho-L-serine; 2-oxoglutarate aminotransferase; 4-O-phosphoryl-L-threonine;

D O I：

10.1016/0014-5793(96)00652-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Escherichia coli pdxC(serC) gene codes for a transaminase (EC 2.6.1.52). The gene is involved in both pyridoxine (vitamin B-6) and serine biosynthesis and was overexpressed as a MalE/PdxC(SerC) fusion protein. The fusion protein was purified by affinity chromatography on an amylose resin and hydrolyzed in the presence of protease factor Xa. Both the fusion protein and the PdxC(SerC) protein were characterized (K-M value, turnover number, optimum pH). Both enzymes used 4-O-phosphoryl-L-threonine rather than 4-hydroxy-L-threonine as a substrate indicating that the phosphorylated rather than the non-phosphorylated amino acid is involved in pyridoxine biosynthesis, Pyridoxal phosphate was shown to be the cofactor for both enzymes and therefore seems to be involved in its own biosynthesis.

引用

页码：179 / 182

页数：4

共 26 条

[1] A GENE FROM SACCHAROMYCES-CEREVISIAE WHICH CODES FOR A PROTEIN WITH SIGNIFICANT HOMOLOGY TO THE BACTERIAL 3-PHOSPHOSERINE AMINOTRANSFERASE [J].