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-dihydropteridine pyrophosphate. HPPK is inhibited by a variety of antimicrobial agents like trimethoprim and sulfonamides.
Disease
Relevance
Structural highlights
3D structures of HPPK
Updated on 02-July-2014
1hka, 1eq0 – EcHPPK – Escherichia coli
1g4c, 1im6, 1kbr, 1rtz, 1tmj, 3hcx, 3hsd, 3hsj, 3hsz, 3ili, 3ill, 3kue, 3kug – EcHPPK (mutant)
2f63, 2f65 – EcHPPK - NMR
HPPK binary complex
1cbk – HPPK + dihydro-dimethyl-6-hydroxypterin – Haemophilus influenza
1eqm – EcHPPK + ADP
1ex8 – EcHPPK + adenosine-tetraphosphate-methyl-dihydropterin
1rb0 – EcHPPK + 6-hydroxymethylpterin-diphosphate
3hd1, 3hsg, 3ht0, 3ilj, 3kuh – EcHPPK (mutant) + methyleneadenosine-triphosphate
3ud5, 3ude, 3udv, 4f7v – EcHPPK + inhibitor
3qbc – HPPK + inhibitor – Staphylococcus aureus
HPPK ternary complex
1ru2, 1tmm – EcHPPK (mutant) + methyleneadenosine-triphosphate + 6-hydroxymethylpterin
1dy3 – EcHPPK (mutant) + ATP + pteridine derivative
3ip0 – EcHPPK + methyleneadenosine-triphosphate + pteridine derivative
1f9h, 1hq2, 1q0n, 1ru1, 3ilo – EcHPPK (mutant) + methyleneadenosine-triphosphate + pteridine derivative
3hd2 – EcHPPK (mutant) + methyleneadenosine-triphosphate + pterine
4m5g, 4m5h, 4m5i, 4m5j, 4m5k, 4m5l, 4m5m, 4m5n – EcHPPK + methyleneadenosine-triphosphate + inhibitor
1rao – EcHPPK (mutant) + AMP + 6-hydroxymethylpterin-diphosphate
2qx0 – HPPK + methyleneadenosine-triphosphate + pteridine derivative – Yersinia pestis
References
