Crystal structures of Trypanosoma cruzi UDP-galactopyranose mutase implicate flexibility of the histidine loop in enzyme activation

Biochemistry

Volumn 51, Issue 24, 2012, Pages 4968-4979

  Dhatwalia, Richa ^a   Singh, Harkewal ^a   Oppenheimer, Michelle ^b   Sobrado, Pablo ^b   Tanner, John J ^a,c  

^a UNIVERSITY OF MISSOURI   (United States)

^b VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^c University of Missouri   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPERGILLUS FUMIGATUS; BIOSYNTHETIC ENZYMES; CATALYTIC EFFICIENCIES; CHAGAS DISEASE; CHEMICAL EQUATIONS; CONFORMATIONAL CHANGE; COOPERATIVE MOVEMENT; DRUG DESIGN; ENZYMATIC ACTIVITIES; ENZYME ACTIVATION; ESSENTIAL COMPONENT; GALACTOFURANOSE; GLYCOLIPIDS; INHIBITOR DESIGN; MUTANT ENZYMES; NON-COVALENT INTERACTION; PROTOZOAN PARASITES; SEQUENCE ALIGNMENTS; SEQUENCE DATA; SUBSTRATE RECOGNITION; TROPICAL DISEASE; TRYPANOSOMA CRUZI; TRYPANOSOMATIDS; UDP-GALACTOPYRANOSE;

AMINO ACIDS; ASPERGILLUS; PATHOGENS;

ENZYME ACTIVITY;

FLAVINE ADENINE NUCLEOTIDE; GLYCINE; GLYCOLIPID; GLYCOPROTEIN; HISTIDINE; IMIDAZOLE; MUTASE; UDP GALACTOPYRANOSE MUTASE; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS FUMIGATUS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME SUBSTRATE; KINETOPLASTIDA; MUTATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; SEQUENCE ALIGNMENT; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; ENZYME ACTIVATION; ENZYME INHIBITORS; HISTIDINE; INTRAMOLECULAR TRANSFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; TRYPANOSOMA CRUZI; URIDINE DIPHOSPHATE;

EID: 84862529810     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300498c     Document Type: Article

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