Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily: Pathways for the catabolism of L-gulonate and L-idonate

Biochemistry

Volumn 53, Issue 35, 2014, Pages 5692-5699

  Wichelecki, Daniel J ^a   Vendiola, Jean Alyxa Ferolin ^a   Jones, Amy M ^a   Al Obaidi, Nawar ^b   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

D-GLUCONATES; ENOLASE; PHYSIOLOGICAL ROLES;

BACTERIAL ENZYME; D GLUCONATE DEHYDRATASE; D MANNONATE; ENOLASE; LEVO GULONATE; LEVO IDONATE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; GLUCONATE DEHYDRATASE; GULONIC ACID; HYDROLYASE; IDONIC ACID; MANNONATE DEHYDRATASE; SUGAR ACID;

ARTICLE; BACTERIAL GENOME; CHROMOHALOBACTER; CHROMOHALOBACTER SALEXIGENS; ENZYME ACTIVITY; ENZYME DEGRADATION; ESCHERICHIA COLI; IN VITRO STUDY; NONHUMAN; PHYSIOLOGICAL PROCESS; SALMONELLA ENTERITIDIS; ENZYME SPECIFICITY; ENZYMOLOGY; GENE INACTIVATION; GENETICS; HALOMONAS; KINETICS; METABOLISM; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR ENTERITIDIS;

BACTERIAL PROTEINS; CHROMOHALOBACTER; ESCHERICHIA COLI PROTEINS; GENE KNOCKOUT TECHNIQUES; HALOMONAS; HYDRO-LYASES; KINETICS; METABOLIC NETWORKS AND PATHWAYS; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; SALMONELLA ENTERITIDIS; SUBSTRATE SPECIFICITY; SUGAR ACIDS;

EID: 84907520580     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500837w     Document Type: Article

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