Substrate-bound crystal structures reveal features unique to Mycobacterium tuberculosis N-Acetyl-glucosamine 1-phosphate uridyltransferase and a catalytic mechanism for acetyl transfer

Journal of Biological Chemistry

Volumn 287, Issue 47, 2012, Pages 39524-39537

  Jagtap, Pravin Kumar Ankush ^a   Soni, Vijay ^b   Vithani, Neha ^a   Jhingan, Gagan Deep ^b   Bais, Vaibhav Singh ^a   Nandicoori, Vinay Kumar ^b   Prakash, Balaji ^a,c  

^a INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

^b NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

^c INDIAN COUNCIL OF MEDICAL RESEARCH   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS;

ACETYLTRANSFERASE ACTIVITY; CATALYTIC MECHANISMS; M. TUBERCULOSIS; MYCOBACTERIUM TUBERCULOSIS; SELECTIVE INHIBITORS; SUBSTRATE BINDING; SUBSTRATE-BOUND; UNIQUE FEATURES;

CATALYST ACTIVITY;

ACETYL COENZYME A; ACYLTRANSFERASE; ASPARAGINE; BACTERIAL ENZYME; HEXOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; MEPYRAMINE MALEATE; N ACETYL GLUCOSAMINE 1 PHOSPHATE URIDYLTRANSFERASE; PROTEIN KINASE B; SERINE; THREONINE; TRYPTOPHAN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; GLMU PROTEIN, MYCOBACTERIUM TUBERCULOSIS; MULTIENZYME COMPLEX;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DOWN REGULATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; MOLECULAR RECOGNITION; MYCOBACTERIUM TUBERCULOSIS; NUCLEOPHILICITY; PRIORITY JOURNAL; RESIDUE ANALYSIS; STRUCTURE ANALYSIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ACETYL COENZYME A; ACETYLTRANSFERASES; BACTERIAL PROTEINS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; MULTIENZYME COMPLEXES; MYCOBACTERIUM TUBERCULOSIS; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 84873971691     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.390765     Document Type: Article

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