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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.6.3 expressed in Escherichia coli BL21 cells Francisella tularensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.15 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
2.7.6.3 apoenzyme and in complex with substrate 6-hydroxymethyl-7,8-dihydropteridine or 2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydorpyrimido[4,5-c]pyridazin-3-yl)propanoic acid, sitting drop vapor diffusion method, using 90 mM Tris (pH 8.0), 190 mM sodium acetate, 24% (w/v) polyethylene glycol (PEG) 4000, and 17% (v/v) glycerol, at 18°C Francisella tularensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.15 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
2.5.1.15 additional information simultaneously targeting of the two modules of the bifunctional enzyme with pterin binding inhibitors Francisella tularensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.6.3 Mg2+ contains two Mg2+ ions Francisella tularensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.15 50509
-
 1 * 50509, sequence calculation Francisella tularensis
2.5.1.15 53000
-
 gel filtration, analytical sedimentation centrifugation Francisella tularensis
2.7.6.3 50509
-
 1 * 50509, the bifunctional enzyme HPPK-DHPS exists mainly as a monomer in solution, calculated from amino acid sequence Francisella tularensis
2.7.6.3 53000
-
 1 * 53000, the bifunctional enzyme HPPK-DHPS exists mainly as a monomer in solution, sedimentation velocity and equilibrium analysis Francisella tularensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.15 (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate Francisella tularensis
-
 diphosphate + 7,8-dihydropteroate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.15 Francisella tularensis
-
-
-
2.7.6.3 Francisella tularensis A0A6B2JKF9
-
-
2.7.6.3 Francisella tularensis LVS A0A6B2JKF9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.6.3 Ni-NTA column chromatography and Superdex 75 gel filtration Francisella tularensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.15 (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
-
 Francisella tularensis diphosphate + 7,8-dihydropteroate
-
 ?
2.5.1.15 additional information the enzyme is bifunctional exhibiting 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK, and dihydropteroate synthase, DHPS, activities Francisella tularensis ?
-
 ?
2.7.6.3 ATP + 6-hydroxymethyl-7,8-dihydropteridine
-
 Francisella tularensis AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
 ir
2.7.6.3 ATP + 6-hydroxymethyl-7,8-dihydropteridine
-
 Francisella tularensis LVS AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
 ir
2.7.6.3 additional information the enzyme does not hydrolyze alpha,beta-methyleneadenosine 5’-triphosphate Francisella tularensis ?
-
 ?
2.7.6.3 additional information the enzyme does not hydrolyze alpha,beta-methyleneadenosine 5’-triphosphate Francisella tularensis LVS ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.15 monomer 1 * 50509, sequence calculation Francisella tularensis
2.5.1.15 More primary and secondary structures of the HPPK-DHPS bifunctional enzyme, structure comparisons, three-dimensional structure, overview Francisella tularensis
2.7.6.3 monomer 1 * 50509, the bifunctional enzyme HPPK-DHPS exists mainly as a monomer in solution, calculated from amino acid sequence Francisella tularensis
2.7.6.3 monomer 1 * 53000, the bifunctional enzyme HPPK-DHPS exists mainly as a monomer in solution, sedimentation velocity and equilibrium analysis Francisella tularensis

Synonyms

EC Number Synonyms Comment Organism
2.5.1.15 DHPS
-
 Francisella tularensis
2.7.6.3 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase HPPK-DHPS, bifunctional enzyme Francisella tularensis
2.7.6.3 HPPK
-
 Francisella tularensis

General Information

EC Number General Information Comment Organism
2.5.1.15 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