Structure and Function of 2,3-Dimethylmalate Lyase, a PEP Mutase/Isocitrate Lyase Superfamily Member

Journal of Molecular Biology

Volumn 386, Issue 2, 2009, Pages 486-503

  Narayanan, Buvaneswari ^a   Niu, Weiling ^b   Joosten, Henk Jan ^c   Li, Zhimin ^b   Kuipers, Remko K P ^d   Schaap, Peter J ^c   Dunaway Mariano, Debra ^b   Herzberg, Osnat ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b UNIVERSITY OF NEW MEXICO   (United States)

^c WAGENINGEN UNIVERSITY   (Netherlands)

^d RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

2,3 dimethylmalate lyase; citramalate lyase; function annotation; nicotinate pathway; PEP mutase isocitrate lyase superfamily

Indexed keywords

2,3 DIMETHYLMALATE LYASE; 3,3 DIFLUOROOXALOACETATE; HYDROLASE; ISOCITRATE LYASE; NICOTINAMIDE; NICOTINIC ACID; OXALOACETATE ACETYLHYDROLASE; OXALOACETIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS NIGER; BACTERIAL METABOLISM; CARBON SOURCE; CATABOLITE REPRESSION; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA MICROARRAY; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; FUNGAL GENE; GENOME; NONHUMAN; NUCLEOTIDE SEQUENCE; OAH GENE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

ASPERGILLUS NIGER; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 59149094101     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.12.037     Document Type: Article

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