Document Detail


Enhancing the latent nucleotide triphosphate flexibility of the glucose-1-phosphate thymidylyltransferase RmlA.
MedLine Citation:
PMID:  17434871     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nucleotidyltransferases are central to nearly all glycosylation-dependent processes and have been used extensively for the chemoenzymatic synthesis of sugar nucleotides. The determination of the NTP specificity of the model thymidylyltransferase RmlA revealed RmlA to utilize all eight naturally occurring NTPs with varying levels of catalytic efficiency, even in the presence of nonnative sugar-1-phosphates. Guided by structural models, active site engineering of RmlA led to alterations of the inherent pyrimidine/purine bias by up to three orders of magnitude. This study sets the stage for engineering single universal nucleotidyltransferases and also provides new catalysts for the synthesis of novel nucleotide diphosphosugars.
Authors:
Rocco Moretti; Jon S Thorson
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2007-04-12
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  282     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-06-04     Completed Date:  2007-07-10     Revised Date:  2007-12-03    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  16942-7     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
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MeSH Terms
Descriptor/Qualifier:
Base Sequence
Binding Sites
DNA Primers
Models, Molecular
Mutagenesis
Nucleotides / metabolism*
Nucleotidyltransferases / chemistry,  genetics,  isolation & purification,  metabolism*
Protein Conformation
Grant Support
ID/Acronym/Agency:
AI552218/AI/NIAID NIH HHS; CA84374/CA/NCI NIH HHS; GM07215/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Nucleotides; EC 2.7.7.-/Nucleotidyltransferases; EC 2.7.7.24/glucose-1-phosphate thymidylyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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