PMID:10378268
| Citation |
Xiao, B, Shi, G, Chen, X, Yan, H and Ji, X (1999) Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents. Structure 7:489-96 |
|---|---|
| Abstract |
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 pyrophosphokinase (HPPK) catalyzes the transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate biosynthetic pathway. |
| Links | |
| Keywords |
Adenosine Triphosphate/metabolism; Amino Acid Sequence; Anti-Bacterial Agents/metabolism; Binding Sites; Diphosphotransferases/chemistry; Diphosphotransferases/metabolism; Escherichia coli/enzymology; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Substrate Specificity |
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