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Volumn 12, Issue 12, 2011, Pages 1886-1896

Revisiting the Mechanism of the Triosephosphate Isomerase Reaction: The Role of the Fully Conserved Glutamic Acid 97 Residue

(4) Samanta, Moumita a Murthy, M R N a Balaram, Hemalatha b Balaram, Padmanabhan a

a INDIAN INSTITUTE OF SCIENCE (India)

b JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH (India)

Author keywords

Active sites; Enzyme mechanisms; Isomerases; Mutagenesis; Proton transfer

Indexed keywords

DIHYDROXYACETONE PHOSPHATE; DIMER; GLUTAMIC ACID; GLUTAMINE; IMIDAZOLE; MUTANT PROTEIN; TRIOSEPHOSPHATE ISOMERASE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL BOND; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN FOLDING; PROTON TRANSPORT; WILD TYPE;

BINDING SITES; BIOCATALYSIS; BIOCHEMISTRY; CIRCULAR DICHROISM; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; DIHYDROXYACETONE PHOSPHATE; GLUTAMIC ACID; GLUTAMINE; HYDROGEN BONDING; KINETICS; MALARIA, FALCIPARUM; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; PLASMODIUM FALCIPARUM; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTONS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; TRANSFORMATION, BACTERIAL; TRIOSE-PHOSPHATE ISOMERASE;

PLASMODIUM FALCIPARUM;

EID: 79961124367 PISSN: 14394227 EISSN: 14397633 Source Type: Journal
DOI: 10.1002/cbic.201100116 Document Type: Article

Times cited : (16)

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