RRC ID 2708
著者 Sato M, Kirimura K, Kino K.
タイトル D-Amino acid dipeptide production utilizing D-alanine-D-alanine ligases with novel substrate specificity.
ジャーナル J Biosci Bioeng
Abstract D-Alanine-D-alanine ligase (Ddl) is an important enzyme in the synthesis of bacterial peptidoglycan. The genes encoding Ddls from Escherichia coli K12 (EcDdlB), Oceanobacillus iheyensis JCM 11309 (OiDdl), Synechocystis sp. PCC 6803 (SsDdl) and Thermotoga maritima ATCC 43589 (TmDdl), the genomic DNA sequences of which have been determined, were cloned and the substrate specificities of these recombinant Ddls were investigated. Although OiDdl had a high substrate specificity for D-alanine; EcDdlB, SsDdl and TmDdl showed broad substrate specificities for D-serine, D-threonine, D-cysteine and glycine, in addition to D-alanine. Four D-amino acid dipeptides were produced using EcDdlB, and D-amino acid homo-dipeptides were successfully produced at high yields except for D-threonyl-D-threonine.
巻・号 99(6)
ページ 623-8
公開日 2005-6-1
DOI 10.1263/jbb.99.623
PII S1389-1723(05)70418-7
PMID 16233841
MeSH Amino Acid Sequence Cloning, Molecular Dipeptides / chemistry* Dipeptides / metabolism* Enzyme Activation Escherichia coli / genetics Escherichia coli / metabolism* Molecular Sequence Data Peptide Synthases / chemistry* Peptide Synthases / genetics Peptide Synthases / metabolism* Protein Engineering / methods* Recombinant Proteins / metabolism Stereoisomerism Substrate Specificity
IF 2.366
引用数 15
WOS 分野 FOOD SCIENCE & TECHNOLOGY BIOTECHNOLOGY & APPLIED MICROBIOLOGY
リソース情報
病原微生物 JCM 11309?