6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
== 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. HPPK is inhibited by a variety of antimicrobial agents like trimethoprim and sulfonamides.
+
6-hydroxymethyl-7,8-dihydropteridine pyrophosphate.
== Disease ==
== Disease ==
== Relevance ==
== Relevance ==
 +
 +
HPPK is a potential target for antimicrobial drugs like trimethoprim and sulfonamides.
== Structural highlights ==
== Structural highlights ==
 +
 +
Three loop regions surround the HPPK active site. Upon binding of ATP, the loop region changes its conformation and enables the binding of HMDP.
 +
</StructureSection>
</StructureSection>

Revision as of 09:45, 21 October 2015

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

Drag the structure with the mouse to rotate

3D structures of HPPK

Updated on 21-October-2015

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools