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Literature summary for 2.5.1.15 extracted from

  • Pemble, C.W.; Mehta, P.K.; Mehra, S.; Li, Z.; Nourse, A.; Lee, R.E.; White, S.W.
    Crystal structure of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase bifunctional enzyme from Francisella tularensis (2010), PLoS ONE, 5, e14165.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.15

Crystallization (Commentary)

Crystallization (Comment) Organism
apo-enzyme, and enzyme in complex with HPPK substrate 6-hydroxymethyl-7,8-dihydropterin or inhibitor 2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydorpyrimido[4,5-c]pyridazin-3-yl)propanoic acid, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution Francisella tularensis

Inhibitors

Inhibitors Comment Organism Structure
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoate binding structure, interactions with the DHPS module and the HPPK module, modeling, ovverview Francisella tularensis
additional information simultaneously targeting of the two modules of the bifunctional enzyme with pterin binding inhibitors Francisella tularensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50509
-
 1 * 50509, sequence calculation Francisella tularensis
53000
-
 gel filtration, analytical sedimentation centrifugation Francisella tularensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate Francisella tularensis
-
 diphosphate + 7,8-dihydropteroate
-
 ?

Organism

Organism UniProt Comment Textmining
Francisella tularensis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
-
 Francisella tularensis diphosphate + 7,8-dihydropteroate
-
 ?
additional information the enzyme is bifunctional exhibiting 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK, and dihydropteroate synthase, DHPS, activities Francisella tularensis ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 50509, sequence calculation Francisella tularensis
More primary and secondary structures of the HPPK-DHPS bifunctional enzyme, structure comparisons, three-dimensional structure, overview Francisella tularensis

Synonyms

Synonyms Comment Organism
DHPS
-
 Francisella tularensis

General Information

General Information Comment Organism
additional information the enzyme is bifunctional exhibiting 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK, EC 2.7.6.3, and dihydropteroate synthase, DHPS, activities, that catalyze sequential metabolic reactions in the folate biosynthetic pathway of bacteria and lower eukaryotes, structural organization between FtHPPK and FtDHPS which are tethered together by a short linker, overview. Each active site binds substrate in the same manner observed in the monofunctional forms. Structures of the active site loops in the DHPS module Francisella tularensis