Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily

Biochemistry

Volumn 47, Issue 1, 2008, Pages 167-182

  Narayanan, Buvaneswari C ^a   Niu, Weiling ^a   Han, Ying ^b   Zou, Jiwen ^b   Mariano, Patrick S ^b   Dunaway Mariano, Debra ^b   Herzberg, Osnat ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b UNIVERSITY OF NEW MEXICO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DECARBOXYLASE ACTIVITY; ISOCITRATE LYASE; PSEUDOMONAS AERUGINOSA; SUPERFAMILY MEMBERS;

CARBOXYLATION; CONFORMATIONS; CRYSTAL STRUCTURE; DIMERS; ENZYME ACTIVITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

BACTERIA;

ALPHA OXOCARBOXYLATE; BACTERIAL ENZYME PA4872; BICARBONATE; CARBOXYLIC ACID; DEUTERIUM; ISOCITRATE LYASE; MAGNESIUM; MANGANESE; OXALOACETATE DECARBOXYLASE; OXALOACETIC ACID DERIVATIVE; PYRUVIC ACID; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CARBOXYLATION; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ASSAY; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; GRAM NEGATIVE BACTERIUM; NONHUMAN; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FAMILY; PROTON NUCLEAR MAGNETIC RESONANCE; PSEUDOMONAS AERUGINOSA; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BICARBONATES; BINDING SITES; CARBOXY-LYASES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ISOCITRATE LYASE; MAGNESIUM; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; OXALATES; OXALOACETATE; PHOSPHOTRANSFERASES (PHOSPHOMUTASES); PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PSEUDOMONAS AERUGINOSA; PYRUVATES; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; PSEUDOMONAS AERUGINOSA;

EID: 37849018387     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701954p     Document Type: Article

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