Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis

Journal of Biological Chemistry

Volumn 280, Issue 24, 2005, Pages 23000-23008

  Williams, Gareth J ^a   Breazeale, Steven D ^b   Raetz, Christian R H ^b   Naismith, James H ^a  

^a UNIVERSITY OF ST ANDREWS   (United Kingdom)

^b DUKE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; CARBOXYLATION; CARBOXYLIC ACIDS; CATALYSIS; CHEMICAL MODIFICATION; CRYSTAL STRUCTURE; IMMUNOLOGY; MOLECULAR BIOLOGY; OXIDATION; POLYPEPTIDES;

CATIONIC ANTIMICROBIAL PEPTIDES; IMMUNE SYSTEM; LIPOPOLYSACCHARIDE; OXIDATIVE DECARBOXYLATION;

ENZYMES;

4 AMINO 4 DEOXY LEVO ARABINOSE; AMINO ACID; ARABINOSE; ASPARAGINE; ASPARTIC ACID; CARBOXYLYASE; FOLINIC ACID; FORMYLTRANSFERASE; GLUTAMINE; HISTIDINE; LIPID A; LIPOPOLYSACCHARIDE; N10 FORMYLTETRAHYDROFOLATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PENTOSE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN ARNA; SERINE; TRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE; URIDINE DIPHOSPHATE GLUCURONIC ACID; URIDINE PHOSPHATE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOHYDRATE SYNTHESIS; CATALYSIS; CATALYST; DECARBOXYLATION; ENZYME ACTIVE SITE; INNATE IMMUNITY; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; REACTION ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; AMINO SUGARS; ANTIMICROBIAL CATIONIC PEPTIDES; BINDING SITES; CARBOXY-LYASES; CHROMATOGRAPHY, GEL; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GLUTAMIC ACID; KINETICS; LEUCOVORIN; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION; OXYGEN; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SELENOMETHIONINE; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; URIDINE DIPHOSPHATE; URIDINE DIPHOSPHATE GLUCURONIC ACID;

NEGIBACTERIA;

EID: 20744455042     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M501534200     Document Type: Article

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