6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase

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== Function ==
== Function ==
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'''6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase''' (HPPK) is a prokaryotic enzyme which is part of the folate synthesis pathway. HPPK catalyzes the attachment of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HMDP) to form
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'''6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase''' (HPPK) or '''2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase''' is a prokaryotic enzyme which is part of the folate synthesis pathway. HPPK catalyzes the attachment of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HMDP) to form
6-hydroxymethyl-7,8-dihydropteridine pyrophosphate. Mg+2 ion is important for binding ATP and HMDP.<ref>PMID:10378268</ref>
6-hydroxymethyl-7,8-dihydropteridine pyrophosphate. Mg+2 ion is important for binding ATP and HMDP.<ref>PMID:10378268</ref>

Revision as of 08:34, 28 February 2021

Structure of E. coli HPPK complex with inhibitor (green) (PDB code 3udv).

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References

  1. Xiao B, Shi G, Chen X, Yan H, Ji X. Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents. Structure. 1999 May;7(5):489-96. PMID:10378268

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