6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
From Proteopedia
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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-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> | ||
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| + | The'' Plasmodium'' parasites encode a protein fused of '''HPPK''' and '''dihydroperoate synthase''' (HPPK-DHPS) which catalyse reaction in the folate biosynthesis pathway<ref>PMID:30104413</ref>. | ||
== Relevance == | == Relevance == | ||
Revision as of 09:04, 28 February 2021
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References
- ↑ 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
- ↑ Yogavel M, Nettleship JE, Sharma A, Harlos K, Jamwal A, Chaturvedi R, Sharma M, Jain V, Chhibber-Goel J, Sharma A. Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance. J Biol Chem. 2018 Aug 13. pii: RA118.004558. doi: 10.1074/jbc.RA118.004558. PMID:30104413 doi:http://dx.doi.org/10.1074/jbc.RA118.004558
