The role of conserved arginine residue in loop 4 of glycoside hydrolase family 10 xylanases

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 5, 2005, Pages 904-910

  Nishimoto, Mamoru ^a   Kitaoka, Motomitsu ^a   Fushinobu, Shinya ^b   Hayashi, Kiyoshi ^a  

^a NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

Arginine; Glycoside hydrolase family 10 (GH10); pH activity; Xylanase

Indexed keywords

AMINO ACIDS; BACTERIA; DERIVATIVES; MUTAGENESIS; PROTONS; SUBSTRATES;

ARGININE RESIDUE; GLYCOSIDE HYDROLASE FAMILY 10 (GH10); MUTANT ENZYMES; PROTON DONORS;

ENZYMES;

ARGININE; ENDO 1,4 BETA XYLANASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; CHEMISTRY; CLOSTRIDIUM; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PH; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ARGININE; BACILLUS; BASE SEQUENCE; CLOSTRIDIUM; CONSERVED SEQUENCE; ENDO-1,4-BETA XYLANASES; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

BACILLUS HALODURANS C-125; CLOSTRIDIUM; CLOSTRIDIUM STERCORARIUM;

EID: 22444445434     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.69.904     Document Type: Article

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