The role of residue S139 of mandelate racemase: Synergistic effect of S139 and E317 on transition state stabilization

Journal of Biomolecular Structure and Dynamics

Volumn 30, Issue 5, 2012, Pages 585-593

  Gu, Jiali ^a   Yu, Hongwei ^a  

^a ZHEJIANG UNIVERSITY   (China)

Author keywords

Enzyme catalysis; Hydrogen bonds; Molecular dynamics; Mutagenesis; Proton transport

Indexed keywords

MANDELATE RACEMASE; SERINE;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN FUNCTION; PROTON TRANSPORT; PSEUDOMONAS PUTIDA; RACEMIZATION; SITE DIRECTED MUTAGENESIS; SOLVATION; STATIC ELECTRICITY;

BINDING SITES; BIOCATALYSIS; HYDROGEN BONDING; KINETICS; MOLECULAR DYNAMICS SIMULATION; MUTAGENESIS, SITE-DIRECTED; OXYGEN; PSEUDOMONAS PUTIDA; RACEMASES AND EPIMERASES;

PSEUDOMONAS PUTIDA;

EID: 84865645644     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2012.687524     Document Type: Article

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