Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents

Background: Folate cofactors are essential for life. Mammals derive folates from their diet, whereas most microorganisms must synthesize folates de novo. Enzymes of the folate pathway therefore provide ideal targets for the development of antimicrobial agents. 6-Hydroxymethyl-7,8-dihydropterin pyrop...

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Veröffentlicht in:	Structure (London) 1999-05, Vol.7 (5), p.489-496
Hauptverfasser:	Xiao, Bing, Shi, Genbin, Chen, Xin, Yan, Honggao, Ji, Xinhua
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acid Sequence Anti-Bacterial Agents - metabolism antimicrobial agent Binding Sites Diphosphotransferases - chemistry Diphosphotransferases - metabolism drug design Escherichia coli - enzymology HPPK Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Protein Conformation protein fold pyrophosphoryl transfer Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sequence Homology, Amino Acid Substrate Specificity
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