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Literature summary for 2.7.6.3 extracted from

  • Blaszczyk, J.; Li, Y.; Cherry, S.; Alexandratos, J.; Wu, Y.; Shaw, G.; Tropea, J.E.; Waugh, D.S.; Yan, H.; Ji, X.
    Structure and activity of Yersinia pestis 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as a novel target for the development of anti-plague therapeutics (2007), Acta Crystallogr. Sect. D, D63, 1169-1177.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His6-tagged maltose-binding-protein fusion HPPK in Escherichia coli strain BL21(DE3) Yersinia pestis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant HPPK in complex with 6-hydroxymethyl-7,8-dihydropterin and an ATP analogue AMPCPP, 8.0 mg/ml HPPK in 15 mM HP, 25 mM AMPCPP, 50 mM MgCl2 and 10 mM Tris-HCl, pH 8.0 s mixed with well solution containing 0.18 M ammonium acetate, 30% w/v PEG 4000, 20 mM imidazole, and 0.1 M sodium acetate, pH 4.6, 1-3 weeks, X-ray diffraction structure determination and analysis, molecular replacement Yersinia pestis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic mechanism and thermodynamics, overview Yersinia pestis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Yersinia pestis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 6-hydroxymethyl-7,8-dihydropterin Yersinia pestis
-
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
-
?
additional information Yersinia pestis HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals ?
-
?

Organism

Organism UniProt Comment Textmining
Yersinia pestis Q7CKD7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 6-hydroxymethyl-7,8-dihydropterin
-
Yersinia pestis AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
-
?
additional information HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals Yersinia pestis ?
-
?

Subunits

Subunits Comment Organism
homodimer Arg79 and Gln88 may help to stabilize the homodimer. The long side chain of Arg79 in YpHPPK forms many hydrophobic interactions with Trp90 and Gln49 from the partner subunit and a weak hydrogen bond with the side chain of Gln49, which may help to stabilize the dimeric molecule Yersinia pestis

Synonyms

Synonyms Comment Organism
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
-
Yersinia pestis
HPPK
-
Yersinia pestis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
assay at Yersinia pestis

Cofactor

Cofactor Comment Organism Structure
ATP
-
Yersinia pestis