Identification and regulation of the catalytic promiscuity of (−)-γ-lactamase from Microbacterium hydrocarbonoxydans

Applied Microbiology and Biotechnology

Volumn 99, Issue 18, 2015, Pages 7559-7568

  Sun, Yu ^a,b   Zhao, Hongtao ^c   Wang, Jianjun ^a   Zhu, Junge ^a   Wu, Sheng ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Enzyme promiscuity; Microbacterium hydrocarbonoxydans; Perhydrolase; Protein engineering; Lactamase

Indexed keywords

ENZYMES; PROTEINS;

COMPUTATIONAL ANALYSIS; EXPERIMENTAL EVIDENCE; LACTAMASES; MICROBACTERIUM HYDROCARBONOXYDANS; PERHYDROLASE; PERHYDROLASE ACTIVITY; PROTEIN ENGINEERING; STRUCTURE SIMILARITY;

BIOCHEMICAL ENGINEERING;

ALANINE; BACTERIAL ENZYME; GAMMA LACTAMASE; HYDROLASE; UNCLASSIFIED DRUG; AMIDASE; GAMMA-LACTAMASE; MUTANT PROTEIN;

BACTERIUM; BIOENGINEERING; CATALYSIS; ENZYME ACTIVITY; HYDROLYSIS; IDENTIFICATION METHOD; MICROBIAL ACTIVITY; PROTEIN; TEMPERATURE EFFECT;

ARTICLE; BIOCHEMICAL ANALYSIS; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; MICROBACTERIUM; MICROBACTERIUM HYDROCARBONOXYDANS; MOLECULAR DOCKING; MUTAGENESIS; PROTEIN EXPRESSION; TEMPERATURE; ACTINOBACTERIA; BIOLOGY; CHEMICAL STRUCTURE; DNA MUTATIONAL ANALYSIS; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS;

MICROBACTERIUM HYDROCARBONOXYDANS;

ACTINOBACTERIA; AMIDOHYDROLASES; CATALYTIC DOMAIN; COMPUTATIONAL BIOLOGY; DNA MUTATIONAL ANALYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN CONFORMATION; PROTEIN ENGINEERING;

EID: 84939562901     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-6503-7     Document Type: Article

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