Dipeptide synthesis by l-amino acid ligase from Ralstonia solanacearum

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 s...

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Published inBiochemical and biophysical research communications Vol. 371; no. 3; pp. 536 - 540
Main Authors Kino, Kuniki, Nakazawa, Yuji, Yagasaki, Makoto
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 04.07.2008
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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.
AbstractList 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.
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 a-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.
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.
Author Nakazawa, Yuji
Kino, Kuniki
Yagasaki, Makoto
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  surname: Kino
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Cites_doi 10.1038/282410a0
10.1128/AEM.01249-07
10.1007/s00203-004-0743-8
10.1046/j.1364-3703.2002.00102.x
10.1271/bbb.59.1398
10.1016/j.bbrc.2006.11.016
10.1016/j.jbiotec.2004.07.017
10.1128/JB.187.15.5195-5202.2005
10.1263/jbb.99.623
10.1016/S0899-9007(00)00321-X
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Keywords Dipeptide
Ralstonia solanacearum
l-Amino acid α-ligase
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References Sambrook, Fritsch, Maniatis (bib9) 1989
Genin, Boucher (bib13) 2002; 3
Fürst, Kuhn (bib1) 2000; 16
Takagi, Shiomi, Ueda, Amano (bib3) 1979; 282
Sato, Kirimura, Kino (bib11) 2005; 99
Monter, Herzog, Stehle, Fürst (bib4) 1991; 14
Tabata, Ikeda, Hashimoto (bib7) 2005; 187
Kino, Kuratsu, Noguchi, Kokubo, Nakazawa, Arai, Yagasaki, Kirimura (bib10) 2007; 352
amino acid amide hydrolase, U.S. patent 7,037,673, 2006.
Steinborn, Hajirezaei, Hofemeister (bib12) 2005; 183
Tabata, Hashimoto (bib8) 2007; 73
Matsufuji, Matsui, Ohshige, Kawasaki, Osajima, Osajima (bib2) 1995; 59
H. Nozaki, I. Kira, S. Suzuki, K. Yokozeki, Dipeptide production method
amino acid amide hydrolase used therin, and production method of
Yokozeki, Hara (bib6) 2005; 115
Monter (10.1016/j.bbrc.2008.04.105_bib4) 1991; 14
Tabata (10.1016/j.bbrc.2008.04.105_bib7) 2005; 187
Tabata (10.1016/j.bbrc.2008.04.105_bib8) 2007; 73
Yokozeki (10.1016/j.bbrc.2008.04.105_bib6) 2005; 115
Fürst (10.1016/j.bbrc.2008.04.105_bib1) 2000; 16
Sambrook (10.1016/j.bbrc.2008.04.105_bib9) 1989
Takagi (10.1016/j.bbrc.2008.04.105_bib3) 1979; 282
10.1016/j.bbrc.2008.04.105_bib5
Kino (10.1016/j.bbrc.2008.04.105_bib10) 2007; 352
Genin (10.1016/j.bbrc.2008.04.105_bib13) 2002; 3
Sato (10.1016/j.bbrc.2008.04.105_bib11) 2005; 99
Matsufuji (10.1016/j.bbrc.2008.04.105_bib2) 1995; 59
Steinborn (10.1016/j.bbrc.2008.04.105_bib12) 2005; 183
References_xml – volume: 99
  start-page: 623
  year: 2005
  end-page: 628
  ident: bib11
  article-title:
  publication-title: J. Biosci. Bioeng.
  contributor:
    fullname: Kino
– volume: 352
  start-page: 351
  year: 2007
  end-page: 359
  ident: bib10
  article-title: Novel substrate specificity of glutathione synthesis enzymes from
  publication-title: Biochem. Biophys. Res. Commun.
  contributor:
    fullname: Kirimura
– volume: 16
  start-page: 603
  year: 2000
  end-page: 606
  ident: bib1
  article-title: Amino-acid substrates in new bottles: implications for clinical nutrition in the 21st century
  publication-title: Nutrition
  contributor:
    fullname: Kuhn
– volume: 59
  start-page: 1398
  year: 1995
  end-page: 1401
  ident: bib2
  article-title: Antihypertensive effects of angiotensin fragments in SHR
  publication-title: Biosci. Biotechnol. Biochem.
  contributor:
    fullname: Osajima
– volume: 3
  start-page: 11
  year: 2002
  end-page: 118
  ident: bib13
  article-title:
  publication-title: Mol. Plant Pathol.
  contributor:
    fullname: Boucher
– volume: 282
  start-page: 410
  year: 1979
  end-page: 412
  ident: bib3
  article-title: A novel analgesic dipeptide from bovine brain is a possible Met-enkephalin releaser
  publication-title: Nature
  contributor:
    fullname: Amano
– year: 1989
  ident: bib9
  article-title: Molecular cloning: a laboratory manual
  contributor:
    fullname: Maniatis
– volume: 73
  start-page: 6378
  year: 2007
  end-page: 6385
  ident: bib8
  article-title: Fermentative production of
  publication-title: Appl. Environ. Microbiol.
  contributor:
    fullname: Hashimoto
– volume: 183
  start-page: 71
  year: 2005
  end-page: 79
  ident: bib12
  article-title: bac genes for recombinant bacilysin and anticapsin production in
  publication-title: Arch. Microbiol.
  contributor:
    fullname: Hofemeister
– volume: 115
  start-page: 211
  year: 2005
  end-page: 220
  ident: bib6
  article-title: A novel and efficient enzymatic method for production of peptides from unprotected starting materials
  publication-title: J. Biotechnol.
  contributor:
    fullname: Hara
– volume: 187
  start-page: 5195
  year: 2005
  end-page: 5202
  ident: bib7
  article-title:
  publication-title: J. Bacteriol.
  contributor:
    fullname: Hashimoto
– volume: 14
  start-page: 183
  year: 1991
  end-page: 191
  ident: bib4
  article-title: Kinetically controlled synthesis of dipeptides using ficinas biocatalyst
  publication-title: Biotechnol. Appl. Biochem.
  contributor:
    fullname: Fürst
– volume: 282
  start-page: 410
  year: 1979
  ident: 10.1016/j.bbrc.2008.04.105_bib3
  article-title: A novel analgesic dipeptide from bovine brain is a possible Met-enkephalin releaser
  publication-title: Nature
  doi: 10.1038/282410a0
  contributor:
    fullname: Takagi
– volume: 73
  start-page: 6378
  year: 2007
  ident: 10.1016/j.bbrc.2008.04.105_bib8
  article-title: Fermentative production of l-alanyl-l-glutamine by a metabolically engineered Escherichia coli strain expressing l-amino acid ligase
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.01249-07
  contributor:
    fullname: Tabata
– volume: 183
  start-page: 71
  year: 2005
  ident: 10.1016/j.bbrc.2008.04.105_bib12
  article-title: bac genes for recombinant bacilysin and anticapsin production in Bacillus host strains
  publication-title: Arch. Microbiol.
  doi: 10.1007/s00203-004-0743-8
  contributor:
    fullname: Steinborn
– volume: 3
  start-page: 11
  year: 2002
  ident: 10.1016/j.bbrc.2008.04.105_bib13
  article-title: Ralstonia solanacearum: secrets of a major pathogen unveiled by analysis of its genome
  publication-title: Mol. Plant Pathol.
  doi: 10.1046/j.1364-3703.2002.00102.x
  contributor:
    fullname: Genin
– year: 1989
  ident: 10.1016/j.bbrc.2008.04.105_bib9
  contributor:
    fullname: Sambrook
– volume: 59
  start-page: 1398
  year: 1995
  ident: 10.1016/j.bbrc.2008.04.105_bib2
  article-title: Antihypertensive effects of angiotensin fragments in SHR
  publication-title: Biosci. Biotechnol. Biochem.
  doi: 10.1271/bbb.59.1398
  contributor:
    fullname: Matsufuji
– volume: 352
  start-page: 351
  year: 2007
  ident: 10.1016/j.bbrc.2008.04.105_bib10
  article-title: Novel substrate specificity of glutathione synthesis enzymes from Streptococcus agalactiae and Clostridium acetobutylicum
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2006.11.016
  contributor:
    fullname: Kino
– volume: 115
  start-page: 211
  year: 2005
  ident: 10.1016/j.bbrc.2008.04.105_bib6
  article-title: A novel and efficient enzymatic method for production of peptides from unprotected starting materials
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2004.07.017
  contributor:
    fullname: Yokozeki
– volume: 187
  start-page: 5195
  year: 2005
  ident: 10.1016/j.bbrc.2008.04.105_bib7
  article-title: ywfE in Bacillus subtilis codes for a novel enzyme, l-amino acid ligase
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.187.15.5195-5202.2005
  contributor:
    fullname: Tabata
– volume: 99
  start-page: 623
  year: 2005
  ident: 10.1016/j.bbrc.2008.04.105_bib11
  article-title: d-amino acid dipeptide production utilizing d-alanine-d-alanine ligases with novel substrate specificity
  publication-title: J. Biosci. Bioeng.
  doi: 10.1263/jbb.99.623
  contributor:
    fullname: Sato
– volume: 16
  start-page: 603
  year: 2000
  ident: 10.1016/j.bbrc.2008.04.105_bib1
  article-title: Amino-acid substrates in new bottles: implications for clinical nutrition in the 21st century
  publication-title: Nutrition
  doi: 10.1016/S0899-9007(00)00321-X
  contributor:
    fullname: Fürst
– ident: 10.1016/j.bbrc.2008.04.105_bib5
– volume: 14
  start-page: 183
  year: 1991
  ident: 10.1016/j.bbrc.2008.04.105_bib4
  article-title: Kinetically controlled synthesis of dipeptides using ficinas biocatalyst
  publication-title: Biotechnol. Appl. Biochem.
  contributor:
    fullname: Monter
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Snippet Despite its utility, dipeptides have not been widely used due to the absence of an efficient manufacturing method. Recently, a novel method for effective...
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SubjectTerms Bacillus subtilis
Dipeptide
Dipeptides - biosynthesis
Dipeptides - chemistry
Escherichia coli - genetics
l-Amino acid α-ligase
Peptide Synthases - chemistry
Peptide Synthases - genetics
Peptide Synthases - isolation & purification
Plant Proteins - chemistry
Plant Proteins - genetics
Plant Proteins - isolation & purification
Protein Conformation
Ralstonia solanacearum
Ralstonia solanacearum - enzymology
Ralstonia solanacearum - genetics
Substrate Specificity
Title Dipeptide synthesis by l-amino acid ligase from Ralstonia solanacearum
URI https://dx.doi.org/10.1016/j.bbrc.2008.04.105
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Volume 371
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