Human UDP-α- d -xylose synthase and escherichia coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced

Biochemistry

Volumn 51, Issue 44, 2012, Pages 8844-8855

  Polizzi, Samuel J ^a   Walsh, Richard M ^a   Peeples, William B ^a   Lim, Jae Min ^c   Wells, Lance ^a,b   Wood, Zachary A ^a  

^a University of Georgia ^*  (United States)

^b UNIVERSITY OF GEORGIA   (United States)

^c Changwon National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; COFACTORS; CONFORMATIONAL CHANGE; D-GLUCURONIC ACID; D-XYLOSE; DECARBOXYLASES; RATE EQUATIONS; SIDE PRODUCTS; SLOW RELEASE; STIMULATORY EFFECTS; STRUCTURAL ELEMENTS; SYNTHASES;

ENZYMES; ESCHERICHIA COLI; GLUCOSE; MACHINERY;

XYLOSE;

4 KETO XYLOSE; BACTERIAL ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SYNTHETASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE ALPHA DEXTRO GLUCURONIC ACID DECARBOXYLASE; URIDINE DIPHOSPHATE ALPHA DEXTRO XYLOSE SYNTHASE; XYLOSE;

ARTICLE; CARBOHYDRATE SYNTHESIS; CATALYSIS; CHEMICAL BINDING; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN UNFOLDING;

CARBOXY-LYASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HUMANS; KINETICS; METABOLIC NETWORKS AND PATHWAYS; MODELS, MOLECULAR; NAD; URIDINE DIPHOSPHATE SUGARS; XYLOSE;

ESCHERICHIA COLI;

EID: 84868574639     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301135b     Document Type: Article

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