Arg305 of streptomyces l-glutamate oxidase plays a crucial role for substrate recognition

Biochemical and Biophysical Research Communications

Volumn 417, Issue 3, 2012, Pages 951-955

  Utsumi, Tomohiro ^a   Arima, Jiro ^b   Sakaguchi, Chika ^a   Tamura, Takashi ^a   Sasaki, Chiduko ^c   Kusakabe, Hitoshi ^d   Sugio, Shigetoshi ^c   Inagaki, Kenji ^a  

^a OKAYAMA UNIVERSITY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

^c MITSUBISHI CHEMICAL CORPORATION   (Japan)

^d UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

L Glutamate oxidase; Streptomyces; Substrate recognition; Substrate specificity

Indexed keywords

ALANINE; ARGININE; HISTIDINE; LEVO GLUTAMATE OXIDASE; OXIDOREDUCTASE; PROTEIN VARIANT; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; GENE MUTATION; HYDROGEN BOND; MOLECULAR DOCKING; MOLECULAR RECOGNITION; NONHUMAN; OXIDATION; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STREPTOMYCES;

AMINO ACID OXIDOREDUCTASES; ARGININE; CATALYSIS; CATALYTIC DOMAIN; HYDROGEN-ION CONCENTRATION; KINETICS; MUTATION; PROTEIN CONFORMATION; STREPTOMYCES; SUBSTRATE SPECIFICITY;

STREPTOMYCES; STREPTOMYCES SP. X-119-6;

EID: 84856012530     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.12.033     Document Type: Article

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