Evidence from Raman spectroscopy that InhA, the mycobacterial enoyl reductase, modulates the conformation of the NADH cofactor to promote catalysis

Journal of the American Chemical Society

Volumn 129, Issue 20, 2007, Pages 6425-6431

  Bell, Alasdair F ^a,b   Stratton, Christopher F ^a,c   Zhang, Xujie ^a   Novichenok, Polina ^a   Jaye, Andrew A ^a   Nair, Pravin A ^a,d   Parikh, Sapan ^a   Rawat, Richa ^a   Tonge, Peter J ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b Medarex Inc   (United States)

^c Department of Molecular Biology and Genetics   (United States)

^d MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENOYL REDUCTASE; HYDRIDE TRANSFER; MYCOBACTERIUM TUBERCULOSIS; NICOTINAMIDE RING;

CATALYSIS; CONFORMATIONS; MUTAGENESIS; RAMAN SPECTROSCOPY;

ENZYMES;

2 ENOYL ACYL CARRIER PROTEIN; ACYL CARRIER PROTEIN; NICOTINAMIDE; OXIDOREDUCTASE; PHENYLALANINE; PROTEIN INHA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DENSITY FUNCTIONAL THEORY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; MUTAGENESIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; RAMAN SPECTROMETRY; REDUCTION;

CATALYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MYCOBACTERIUM TUBERCULOSIS; NAD; OXIDOREDUCTASES; PHENYLALANINE; SPECTRUM ANALYSIS, RAMAN; VIBRATION;

EID: 34249053274     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja068219m     Document Type: Article

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