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B6db references: 20033172

type Journal Article
authors Zheng C, Nie L, Qian L, Wang Z, Liu G, Liu J.
title K30, H150, and H168 Are Essential Residues for Coordinating Pyridoxal 5'-Phosphate of O-Acetylserine Sulfhydrylase from Acidithiobacillus ferrooxidans
journal Curr Microbiol
sel selected
ui 20033172
year (2009)
volume 60
pages 461-5
keywords Amino Acid Sequence
abstract O-acetylserine sulfhydrylase (OASS) is a key enzyme involved in the pathway of the cysteine biosynthesis. The gene of OASS from Acidithiobacillus ferrooxidans ATCC 23270 was cloned and expressed in E. coli, the soluble protein was purified by one-step affinity chromatography to apparent homogeneity. Colors and UV-vis scanning results of the recombinant protein confirmed that it was a pyridoxal 5'-phosphate (PLP)-containing protein. Sequence alignment and site-directed mutation of the enzyme revealed that the cofactor PLP is covalently bound in Schiff base linkage with K30, as well as the two residues H150 and H168 were the crucial residues for PLP binding and stabilization.
last changed 2010/06/16 17:35

B6db references