Substrate spectrum of tyrocidine thioesterase probed with randomized peptide N-acetylcysteamine thioesters.
Apparent kinetic constants k(cat) and K(m) were determined for tyrocidine thioesterase (TycC TE) using randomized peptide N-acetylcysteamine thioesters as substrate analogues. The enzyme has been found to be adequately active for the synthesis of positional-scanning libraries for novel antibiotic screening with reduced k(cat)/K(m) in the range of 2 to 82 folds lower than that of the wild-type sequence
Xie
Guiyang
G
Department of Chemistry and Biotechnology Research Institute, The Hong Kong University of Science and Technology, Kowloon, SAR, Hong Kong, China.
Uttamchandani
Mahesh
M
Chen
Grace Y J
GY
Bu
Xianzhang
X
Lin
San San
SS
Wong
Ka Man
KM
Yan
Weili
W
Yao
Shao Q
SQ
Guo
Zhihong
Z
D000111:Acetylcysteine / Q000737:chemistry; D000890:Anti-Infective Agents / Q000138:chemical synthesis / Q000493:pharmacokinetics; D004950:Esterases / Q000378:metabolism*; D007700:Kinetics; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000493:pharmacokinetics; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000737:chemistry; D014440:Tyrocidine / Q000378:metabolism*
D000890:Anti-Infective Agents; D009842:Oligopeptides; D013438:Sulfhydryl Compounds; D014440:Tyrocidine; D004950:Esterases; C475899:tyrocidine thioesterase; D000111:Acetylcysteine