Identification and characterization of a tyramine-glutamate ligase (MfnD) involved in methanofuran biosynthesis

Biochemistry

Volumn 53, Issue 39, 2014, Pages 6220-6230

  Wang, Yu ^a   Xu, Huimin ^a   Harich, Kim C ^a   White, Robert H ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AROMATIC COMPOUNDS; BIOCHEMISTRY; BIOSYNTHESIS; CARBON DIOXIDE; CARBOXYLATION; CATALYSIS; ENZYMES; ESCHERICHIA COLI; MANGANESE; METHANE; ORGANIC POLLUTANTS; SUBSTRATES;

ARCHAEOGLOBUS FULGIDUS; GLUTATHIONE SYNTHETASE; METAL-BINDING MOTIF; RECOMBINANT ENZYMES; SITE DIRECTED MUTAGENESIS; SOLVED CRYSTAL STRUCTURES; STEADY-STATE KINETICS; STRUCTURAL DOMAINS;

CRYSTAL STRUCTURE;

ADENOSINE TRIPHOSPHATE; AMINO ACID; CARBOXYLIC ACID; CELL EXTRACT; FURAN DERIVATIVE; GLUTAMIC ACID; GLUTATHIONE SYNTHASE; LIGASE; METHANOFURAN; RECOMBINANT ENZYME; TYRAMINE; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; CARBON DIOXIDE REDUCTION FACTOR; PROTEIN BINDING; RECOMBINANT PROTEIN;

ARCHAEOGLOBUS FULGIDUS; ARTICLE; BIOSYNTHESIS; CATALYSIS; CELL INCLUSION; CHEMICAL STRUCTURE; COENZYME; CRYSTAL STRUCTURE; ENZYMATIC ASSAY; ENZYME ACTIVITY; ENZYMOLOGY; ESCHERICHIA COLI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; METAL BINDING; METHANOCALDOCOCCUS; METHANOCALDOCOCCUS FERVENS; METHANOCALDOCOCCUS JANNASCHII; MOLECULAR CLONING; MOLECULAR DOCKING; NONHUMAN; SITE DIRECTED MUTAGENESIS; STEADY STATE; SYNTHESIS; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; BIOSYNTHETIC PATHWAYS; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; FURANS; GLUTAMIC ACID; KINETICS; LIGASES; METHANOCALDOCOCCUS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TYRAMINE;

EID: 84907812774     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500879h     Document Type: Article

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