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Dipeptide synthesis by L-amino acid ligase from Ralstonia solanacearum.

Abstract：

:Despite its utility, dipeptides have not been widely used due to the absence of an efficient manufacturing method. Recently, a novel method for effective production of dipeptides using l-amino acid alpha-ligase (Lal) is presented. Lal, which is only identified in Bacillus subtilis, catalyzes dipeptide synthesis from unprotected amino acids in an ATP-dependent manner. However, not all the dipeptide can be synthesized by Lal from B. subtilis (BsLal) due to its substrate specificity. Here, we attempted to find a novel Lal exhibiting different substrate specificity from BsLal. By in silico screening based on the amino acid sequence of BsLal, RSp1486a an unknown protein from Ralstonia solanacearum was found to show the Lal activity. RSp1486a exhibited different substrate specificity from BsLal, and preferably synthesized hetero-dipeptides where more bulky amino acid was placed at N terminus and less bulky amino acid was placed at C terminus in opposition to those synthesized by BsLal.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kino K,Nakazawa Y,Yagasaki M

doi

10.1016/j.bbrc.2008.04.105

subject

Has Abstract

pub_date

2008-07-04 00:00:00

pages

536-40

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)00798-5

journal_volume

371

pub_type

杂志文章

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