Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysis

Journal of Biochemistry

Volumn 122, Issue 4, 1997, Pages 802-809

  Taguchi, Hayao ^a   Ohta, Takahisa ^b   Matsuzawa, Hiroshi ^c  

^a TOKYO UNIVERSITY OF SCIENCE   (Japan)

^b KOGAKUIN UNIVERSITY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

Active center; D lactate dehydrogenase; Lactobacillus; Stereospecificity

Indexed keywords

2 OXOACID; ACETIC ACID; ARGININE; ASPARTIC ACID; DEXTRO LACTATE DEHYDROGENASE; FORMIC ACID; GLUTAMIC ACID; IMIDAZOLE; LYSINE; OXAMIC ACID; PROPIONIC ACID;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; GENETIC CONSERVATION; LACTOBACILLUS; MOLECULAR INTERACTION; NONHUMAN; PH;

LACTOBACILLUS; LACTOBACILLUS PENTOSUS;

EID: 0030666842     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021826     Document Type: Article

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