Insights into ligand binding and catalysis of a central step in NAD + synthesis. Structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes

Journal of Biological Chemistry

Volumn 276, Issue 10, 2001, Pages 7225-7232

  Saridakis, Vivian ^a,b   Christendat, Dinesh ^a,b,c   Kimber, Matthew S ^b   Dharamsi, Akil ^d   Edwards, Aled M ^a,b,c,d   Pai, Emil F ^a,b  

^a PRINCESS MARGARET HOSPITAL   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

^d Integrative Proteomics Inc   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CATALYSTS; MUTAGENESIS; SYNTHESIS (CHEMICAL);

BIOSYNTHETIC PATHWAYS;

ENZYMES;

ADENOSINE TRIPHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE NUCLEOTIDE; NICOTINAMIDE NUCLEOTIDE ADENYLYLTRANSFERASE; NICOTINIC ACID NUCLEOTIDE; SULFATE; UNCLASSIFIED DRUG; LIGAND;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME STRUCTURE; LIGAND BINDING; METHANOBACTERIUM THERMOAUTOTROPHICUM; NONHUMAN; NUCLEOTIDE METABOLISM; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN MOTIF; X RAY DIFFRACTION; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GEL CHROMATOGRAPHY; GENETICS; METHANOBACTERIUM; MOLECULAR CLONING; MOLECULAR GENETICS; MUTAGENESIS; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); METHANOBACTERIUM; METHANOTHERMOBACTER THERMAUTOTROPHICUS;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; LIGANDS; METHANOBACTERIUM; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; MUTATION; NAD; NICOTINAMIDE-NUCLEOTIDE ADENYLYLTRANSFERASE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0035831542     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M008810200     Document Type: Article

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