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 α-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.
| Original language | English |
|---|---|
| Pages (from-to) | 536-540 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 371 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2008 Jul 4 |
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Keywords
- Dipeptide
- l-Amino acid α-ligase
- Ralstonia solanacearum
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Dipeptide synthesis by l-amino acid ligase from Ralstonia solanacearum. / Kino, Kuniki; Nakazawa, Yuji; Yagasaki, Makoto.
In: Biochemical and Biophysical Research Communications, Vol. 371, No. 3, 04.07.2008, p. 536-540.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dipeptide synthesis by l-amino acid ligase from Ralstonia solanacearum
AU - Kino, Kuniki
AU - Nakazawa, Yuji
AU - Yagasaki, Makoto
PY - 2008/7/4
Y1 - 2008/7/4
N2 - 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 α-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.
AB - 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 α-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.
KW - Dipeptide
KW - l-Amino acid α-ligase
KW - Ralstonia solanacearum
UR - http://www.scopus.com/inward/record.url?scp=43549091806&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=43549091806&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2008.04.105
DO - 10.1016/j.bbrc.2008.04.105
M3 - Article
VL - 371
SP - 536
EP - 540
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -