6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | '''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 to 6-hydroxymethyl-7,8-dihydropterin 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. | + | 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate. |
== Disease == | == Disease == | ||
== Relevance == | == Relevance == | ||
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| + | HPPK is a potential target for antimicrobial drugs like trimethoprim and sulfonamides. | ||
== Structural highlights == | == Structural highlights == | ||
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| + | Three loop regions surround the HPPK active site. Upon binding of ATP, the loop region changes its conformation and enables the binding of HMDP. | ||
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</StructureSection> | </StructureSection> | ||
Revision as of 09:45, 21 October 2015
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3D structures of HPPK
Updated on 21-October-2015
