Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris

Biochemistry

Volumn 45, Issue 49, 2006, Pages 14582-14597

  Yew, Wen Shan ^a   Fedorov, Alexander A ^b   Fedorov, Elena V ^b   Rakus, John F ^a   Pierce, Richard W ^a   Almo, Steven C ^b   Gerlt, John A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CATALYSIS; DEHYDRATION; MOLECULAR STRUCTURE; ORGANIC ACIDS; SUGARS;

ACID SUGARS; EUKARYOTES; KETONIZATION; XANTHOMONAS CAMPESTRIS;

ENZYME IMMOBILIZATION;

2 KETO 3 DEOXY LEVO FUCONATE; ACID SUGAR; ALCOHOL DERIVATIVE; ASPARTIC ACID; CARBOHYDRATE; CARBOXYLIC ACID; DEXTRO ALTRONATE; DEXTRO ARABINONATE; DEXTRO RIBONATE; ENEDIOLATE; ENOL; ENOLASE; ESTER; FUNCTIONAL GROUP; GLUTAMIC ACID; HISTIDINE; HYDROLYASE; HYDROXYL GROUP; LEVO FUCONATE DEHYDRATASE; LEVO GALACTONATE; LEVO TALONATE; LIGAND; LYSINE; MAGNESIUM ION; MANDELATE RACEMASE; PROTEIN; PROTON; RTS BETA PROTEIN; THYMIDYLATE SYNTHASE;

ARTICLE; BACTERIAL GENOME; BETA SHEET; CATALYSIS; CHEMICAL MODIFICATION; CONTROLLED STUDY; ELIMINATION REACTION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; EVOLUTION; HYDRATION; KETONIZATION; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; ORTHOLOGY; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTON TRANSPORT; STEREOSPECIFICITY; XANTHOMONAS CAMPESTRIS;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CLONING, MOLECULAR; DNA PRIMERS; GENOME, BACTERIAL; HYDRO-LYASES; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PHOSPHOPYRUVATE HYDRATASE; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; SUGAR ACIDS; XANTHOMONAS CAMPESTRIS;

EUKARYOTA; HOMO SAPIENS; XANTHOMONAS CAMPESTRIS; XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS STR. ATCC 33913;

EID: 33845401627     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061687o     Document Type: Article

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