A strong carboxylate-arginine interaction is important in substrate orientation and recognition in lactate dehydrogenase

Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

Volumn 914, Issue 3, 1987, Pages 294-298

  Hart, Keith W ^a   Clarke, Anthony R ^a   Wigley, Dale B ^a   Waldman, Adam D B ^a   Chia, William N ^a   Barstow, David A ^b   Atkinson, Tony ^b   Jones, J Bryan ^c   Holbrook, J John ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b PUBLIC HEALTH ENGLAND   (United Kingdom)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

(B. stearothermophilus); Lactate dehydrogenase; Site directed mutagenesis; Substrate binding energy; Substrate specificity

Indexed keywords

ARGININE; CARBOXYLIC ACID; LACTATE DEHYDROGENASE; LYSINE;

ARTICLE; BACILLUS STEAROTHERMOPHILUS; BINDING SITE; CALORIMETRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MUTATION; PROTEIN BINDING;

ARGININE; BACILLUS STEAROTHERMOPHILUS; BINDING SITES; CALORIMETRY; CARBOXYLIC ACIDS; KINETICS; LACTATE DEHYDROGENASE; LYSINE; MUTATION; PROTEIN BINDING; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T;

EID: 0023661826     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/0167-4838(87)90289-5     Document Type: Article

References (8)