TY - JOUR
T1 - Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589
AU - Sato, Masaru
AU - Kirimura, Kohtaro
AU - Kino, Kuniki
N1 - Funding Information:
This study was supported in part by the 21C-COE Program ‘‘Practical Nano-Chemistry’’ of the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan, and by a Waseda University Grant for Special Research Projects (2005B-142).
PY - 2006
Y1 - 2006
N2 - D-Alanine-D-alanine ligase (Ddl) and its mutants maintain the biosynthesis of peptidoglycan, and the substrate specificity of Ddls partially affects the resistance mechanism of vancomycin-resistant enterococci. Through investigation of Ddls, Ddl from Thermotoga maritima ATCC 43589 showed novel characteristics, vis. thermostability up to 90°C and broad substrate specificity toward 15 D-amino acids, particularly D-alanine, D-cysteine, and D-serine, in that order.
AB - D-Alanine-D-alanine ligase (Ddl) and its mutants maintain the biosynthesis of peptidoglycan, and the substrate specificity of Ddls partially affects the resistance mechanism of vancomycin-resistant enterococci. Through investigation of Ddls, Ddl from Thermotoga maritima ATCC 43589 showed novel characteristics, vis. thermostability up to 90°C and broad substrate specificity toward 15 D-amino acids, particularly D-alanine, D-cysteine, and D-serine, in that order.
KW - D-alanine-D-alanine ligase
KW - D-amino acid dipeptide
KW - Thermophile
KW - Vancomycin-resistant enterococci
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U2 - 10.1271/bbb.60307
DO - 10.1271/bbb.60307
M3 - Article
C2 - 17090922
AN - SCOPUS:33751421505
SN - 0916-8451
VL - 70
SP - 2790
EP - 2792
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 11
ER -