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A novel serine hydroxymethyltransferase from Arthrobacter nicotianae: characterization and improving catalytic efficiency by rational design.

Abstract：

BACKGROUND:Serine hydroxymethyltransferase (SHMT) is the key enzyme in L-serine enzymatic production, suggesting the importance of obtaining a SHMT with high activity. RESULTS:Here, a novel SHMT gene, glyA, was obtained through degenerate oligonucleotide-primed PCR and encoded a novel SHMT with 54.3% similarity to the known SHMT from Escherichia coli. The obtained protein AnSHMT showed the optimal activity at 40 °C and pH 7.5, and was more stable in weakly alkali conditions (pH 6.5-8.5) than Hyphomicrobium methylovorum's SHMT (pH 6.0-7.5), In order to improve the catalytic efficiency of the wild type, the site-directed mutagenesis based on sequences alignment and bioinformatics prediction, was used and the catalytic efficiency of the mutant I249L was found to be 2.78-fold higher than that of the wild-type, with the replacement of isoleucine by leucine at the 249 position. CONCLUSIONS:This research provides useful information about the interesting site, and the application of DOP-PCR in cloning a novel glyA gene.

journal_name

BMC Biotechnol

journal_title

BMC biotechnology

authors

Jiang W,Chen L,Hu N,Yuan S,Li B,Liu Z

doi

10.1186/s12896-014-0093-9

subject

Has Abstract

pub_date

2014-11-14 00:00:00

pages

93

issn

1472-6750

pii

s12896-014-0093-9

journal_volume

14

pub_type

杂志文章

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