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B6db references: a26b

type Journal Article
authors Wei Jiang, Bingzhao Xia, Junjie Huang and Ziduo Liu
title Characterization of a serine hydroxymethyltransferase for l-serine enzymatic production from Pseudomonas plecoglossicida
journal World Journal of Microbiology and Biotechnology
Activity 2.1.2.1
Family 2.1.2.1
sel selected
year (2013)
volume 29
number 11
pages 2067-2076
 
abstract Pseudomonas plecoglossicida, a bacterium strain that exhibits high Serine hydroxymethyltransferase (SHMT) activity, was isolated from the seawater. A full-length glyA encoding SHMT was obtained by a modified thermal asymmetric interlaced-PCR (TRIL-PCR), which consisted of 1,254 bp, encoded a 417 amino acid polypeptide, and shared the highest identity (75 %) with a glyA gene from Acinetobacter radioresistens CMC-1. Recombinant glyA gene was expressed in Escherichia coli BL21 (DE3) and purified by electrophoretic homogeneity. The enzyme showed the optimal activity at pH 8.0 and 40 C, and remained stable in high alkali conditions. Using SHMT to produce l-serine by catalyzing the reaction of glycine and tetrahydrofolate is one of the most promising routes to synthesize l-serine, achieving 33.4 mM l-serine at the 12th h of the enzymatic reaction with the substrates of glycine (133 mM) and formaldehyde (13.3 mM). The properties make the SHMT a candidate for further enzymatic studies and industrial applications.
last changed 2014/03/06 15:32

B6db references