6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
From Proteopedia
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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 | '''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 | ||
| - | 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate. Mg+2 ion is important for binding ATP and HMDP. | + | 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate. Mg+2 ion is important for binding ATP and HMDP.<ref>PMID:10378268</ref> |
== Relevance == | == Relevance == | ||
Revision as of 07:27, 6 December 2015
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3D structures of HPPK
Updated on 06-December-2015
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
