Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12

Bioorganic and Medicinal Chemistry Letters

Volumn 19, Issue 22, 2009, Pages 6429-6432

  Fang, Junqiang ^a   Guan, Wanyi ^a,b   Cai, Li ^b   Gu, Guofeng ^a   Liu, Xianwei ^a   Wang, Peng George ^a,b  

^a SHANDONG UNIVERSITY   (China)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

Biosynthesis; N Acetylglucosamine 1 phosphate uridyltransferase; Pyrophosphorylase domain; Substrate specificity

Indexed keywords

BACTERIAL ENZYME; DEOXYADENOSINE TRIPHOSPHATE; N ACETYLGLUCOSAMINE 1 PHOSPHATE URIDYLTRANSFERASE; PHOSPHORYLASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE; URIDINE TRIPHOSPHATE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; ESCHERICHIA COLI; IN VITRO STUDY; NONHUMAN;

ACETYLGLUCOSAMINE; BINDING SITES; ESCHERICHIA COLI K12; MOLECULAR STRUCTURE; NUCLEOTIDES; NUCLEOTIDYLTRANSFERASES; PHOSPHATES; POLYPHOSPHATES; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; URIDINE TRIPHOSPHATE;

ESCHERICHIA COLI; PROKARYOTA;

EID: 71049138194     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2009.09.039     Document Type: Article

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