The crystal structure of the adenylation enzyme VinN reveals a unique β-amino acid recognition mechanism

Journal of Biological Chemistry

Volumn 289, Issue 45, 2014, Pages 31448-31457

  Miyanaga, Akimasa ^a   Cies̈lak, Jolanta ^a   Shinohara, Yuji ^a   Kudo, Fumitaka ^a   Eguchi, Tadashi ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; ENZYMES; METABOLITES; SUBSTRATES;

ALPHA-AMINO ACIDS; BETA-AMINO ACIDS; MUTATIONAL ANALYSIS; RECOGNITION MECHANISM; SECONDARY METABOLITES; SELECTIVE RECOGNITION; STRUCTURAL COMPARISON; SUBSTRATE-BINDING;

CRYSTAL STRUCTURE;

ALPHA AMINO ACID; BETA AMINO ACID; ENZYME; N METHYLASPARTIC ACID; UNCLASSIFIED DRUG; VICENISTATIN; VINN ENZYME; AMINOGLYCOSIDE; BACTERIAL PROTEIN; LACTAM; MACROLIDE; NUCLEOTIDYLTRANSFERASE; PROTEIN BINDING; RECOMBINANT PROTEIN;

ADENYLATION; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; MOLECULAR RECOGNITION; MUTATIONAL ANALYSIS; NONHUMAN; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; HYDROGEN BOND; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYLOGENY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STREPTOMYCES; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; AMINOGLYCOSIDES; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DNA MUTATIONAL ANALYSIS; ESCHERICHIA COLI; HYDROGEN BONDING; LACTAMS; MACROLIDES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; N-METHYLASPARTATE; NUCLEOTIDYLTRANSFERASES; PHYLOGENY; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOMYCES; SUBSTRATE SPECIFICITY;

EID: 84909606184     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.602326     Document Type: Article

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