A novel l-amino acid ligase from bacillus licheniformis

Kuniki Kino; Atsushi Noguchi; Yuji Nakazawa; Makoto Yagasaki

doi:10.1263/jbb.106.313

A novel l-amino acid ligase from bacillus licheniformis

Kuniki Kino^*, Atsushi Noguchi, Yuji Nakazawa, Makoto Yagasaki

^*Corresponding author for this work

School of Advanced Science and Engineering

Research output: Contribution to journal › Article › peer-review

33 Citations (Scopus)

Abstract

l-Amino acid α-ligase (EC 6.3.2.28) catalyzed formation of α-peptide bond in unprotected l-amino acids in an ATP-dependent manner. BL00235 gene in Bacillus licheniformis NBRC12200 coded as a new l-amino acid ligase. BL00235 substrate specificity was strict; only methionine or leucine was acceptable as dipeptide N-terminal residues.

Original language	English
Pages (from-to)	313-315
Number of pages	3
Journal	Journal of Bioscience and Bioengineering
Volume	106
Issue number	3
DOIs	https://doi.org/10.1263/jbb.106.313
Publication status	Published - 2008 Sept

Keywords

Bacillus licheniformis
dipeptide
enzymatic method
l-amino acid
α-ligase

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1263/jbb.106.313

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title = "A novel l-amino acid ligase from bacillus licheniformis",

abstract = "l-Amino acid α-ligase (EC 6.3.2.28) catalyzed formation of α-peptide bond in unprotected l-amino acids in an ATP-dependent manner. BL00235 gene in Bacillus licheniformis NBRC12200 coded as a new l-amino acid ligase. BL00235 substrate specificity was strict; only methionine or leucine was acceptable as dipeptide N-terminal residues.",

keywords = "Bacillus licheniformis, dipeptide, enzymatic method, l-amino acid, α-ligase",

author = "Kuniki Kino and Atsushi Noguchi and Yuji Nakazawa and Makoto Yagasaki",

note = "Funding Information: We would like to thank the members of the Tokyo BioFrontier Laboratories, Kyowa Hakko Kogyo Co. Ltd., Tokyo, Japan for the NMR and sequence analyses. This work was done at the Center for Practical Chemical Wisdom supported by Global COE Program of the Ministry of Education, Culture, Sports, Science and Technology, Japan.",

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month = sep,

doi = "10.1263/jbb.106.313",

language = "English",

volume = "106",

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T1 - A novel l-amino acid ligase from bacillus licheniformis

AU - Kino, Kuniki

AU - Noguchi, Atsushi

AU - Nakazawa, Yuji

AU - Yagasaki, Makoto

N1 - Funding Information: We would like to thank the members of the Tokyo BioFrontier Laboratories, Kyowa Hakko Kogyo Co. Ltd., Tokyo, Japan for the NMR and sequence analyses. This work was done at the Center for Practical Chemical Wisdom supported by Global COE Program of the Ministry of Education, Culture, Sports, Science and Technology, Japan.

PY - 2008/9

Y1 - 2008/9

N2 - l-Amino acid α-ligase (EC 6.3.2.28) catalyzed formation of α-peptide bond in unprotected l-amino acids in an ATP-dependent manner. BL00235 gene in Bacillus licheniformis NBRC12200 coded as a new l-amino acid ligase. BL00235 substrate specificity was strict; only methionine or leucine was acceptable as dipeptide N-terminal residues.

AB - l-Amino acid α-ligase (EC 6.3.2.28) catalyzed formation of α-peptide bond in unprotected l-amino acids in an ATP-dependent manner. BL00235 gene in Bacillus licheniformis NBRC12200 coded as a new l-amino acid ligase. BL00235 substrate specificity was strict; only methionine or leucine was acceptable as dipeptide N-terminal residues.

KW - Bacillus licheniformis

KW - dipeptide

KW - enzymatic method

KW - l-amino acid

KW - α-ligase

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DO - 10.1263/jbb.106.313

M3 - Article

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SN - 1389-1723

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JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

IS - 3

ER -

A novel l-amino acid ligase from bacillus licheniformis

Abstract

Keywords

ASJC Scopus subject areas

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