D-Amino Acid Dipeptide Production Utilizing D-Alanine-D-Alanine Ligases with Novel Substrate Specificity(Enzymology, Protein Engineering, and Enzyme Technology)
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概要
- 論文の詳細を見る
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.
- 社団法人日本生物工学会の論文
- 2005-06-25
著者
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Kino Kuniki
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University
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KIRIMURA Kohtaro
Department of Applied Chemistry, School of Science and Engineering, Waseda University
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Kino K
Department Of Applied Chemistry School Of Science And Engineering Waseda University
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Kino Kuniki
Department Of Applied Chemistry Faculty Of Science And Engineering Waseda University
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Kino Kuniki
Department Of Applied Chemistry School Of Science And Engineering Waseda University
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Sato Masaru
Department of Oral Pathology, Asahi University School of Dentistry
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Kino Kuniki
Dep. Of Applied Chemistry Fac. Of Sci. And Engineering Waseda Univ. 3-4-1 Ohkubo Shinjuku-ku Tokyo 1
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Kirimura Kohtaro
Department Of Applied Chemistry Faculty Of Science And Engineering Waseda University
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Sato Masaru
Department Of Applied Chemistry School Of Advanced Science And Engineering Faculty Of Science And En
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