Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Cross, P.J.; Pietersma, A.L.; Allison, T.M.; Wilson-Coutts, S.M.; Cochrane, F.C.; Parker, E.J.
    Neisseria meningitidis expresses a single 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase that is inhibited primarily by phenylalanine (2013), Protein Sci., 22, 1087-1099.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.54 gene aroG, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Neisseria meningitidis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.54 purified enzyme mutant S213G with phosphoenolpyruvate and Mn2+, hanging drop vapor diffusion, mixing of 0.001 ml of 11 mg/mL in 10 mM BTP buffer, pH 7.3, in a 1:1 v/v with a reservoir solution containing 0.2 M trimethylamine N-oxide, 0.1 M Tris, pH 8.5, 15-20% w/v PEG 2000 MME, 0.4 mM MnSO4, and 0.4 mM phosphoenolpyruvate, equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffractin structure determination and analysis at 2.0-2.1 A resolution Neisseria meningitidis

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.54 S213G site-directed mutagenesis, a single Ser residue at the bottom of the inhibitor-binding cavity is substituted to Gly, which alters inhibitor specificity from L-Phe to L-Tyr Neisseria meningitidis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.54 L-Phe strong feedback inhibition Neisseria meningitidis
2.5.1.54 L-Trp feedback inhibition Neisseria meningitidis
2.5.1.54 L-Tyr feedback inhibition Neisseria meningitidis
2.5.1.54 additional information undergoes no significant conformational change on inhibitor binding, crystal structure analysis, overview. Allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme Neisseria meningitidis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.54 additional information
-
 additional information Michaelis-Menten kinetics, kinetics in presence of inhibitors L-phe and L-Tyr Neisseria meningitidis
2.5.1.54 0.0087
-
 phosphoenolpyruvate pH 6.8, 30°C, mutant S213G Neisseria meningitidis
2.5.1.54 0.011
-
 phosphoenolpyruvate pH 6.8, 30°C, wild-type enzyme Neisseria meningitidis
2.5.1.54 0.04
-
 D-erythrose 4-phosphate pH 6.8, 30°C, mutant R126S Neisseria meningitidis
2.5.1.54 0.043
-
 D-erythrose 4-phosphate pH 6.8, 30°C, wild-type enzyme Neisseria meningitidis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.54 Cd2+ activates Neisseria meningitidis
2.5.1.54 Co2+ activates Neisseria meningitidis
2.5.1.54 Cu2+ activates slightly Neisseria meningitidis
2.5.1.54 Fe2+ activates slightly Neisseria meningitidis
2.5.1.54 Mn2+ activates, best activating metal ion. The metal ion is coordinated by four protein ligands Cys63, His 270, Glu304, and Asp324 Neisseria meningitidis
2.5.1.54 additional information no effect by Mg2+, Ni2+, Ca2+, Ba2+, and Sr2+ Neisseria meningitidis
2.5.1.54 Zn2+ activates Neisseria meningitidis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O Neisseria meningitidis
-
 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O Neisseria meningitidis MC58
-
 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.54 Neisseria meningitidis Q9K169 serotype B, gene aroG
-
2.5.1.54 Neisseria meningitidis MC58 Q9K169 serotype B, gene aroG
-
2.5.1.54 no activity in Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.54 recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by anion exchange chromatography, ultrafiltration, and gel filtration Neisseria meningitidis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
-
 Neisseria meningitidis 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction Neisseria meningitidis 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
-
 Neisseria meningitidis MC58 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction Neisseria meningitidis MC58 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.54 homotetramer a dimer of tight dimers, crystal structure analysis Neisseria meningitidis
2.5.1.54 More the monomer of Nme-DAH7PS is a (beta/alpha)8 TIM-barrel Neisseria meningitidis

Synonyms

EC Number Synonyms Comment Organism
2.5.1.54 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
-
 Neisseria meningitidis
2.5.1.54 DAH7PS
-
 Neisseria meningitidis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.54 30
-
 assay at Neisseria meningitidis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.54 14.8
-
 D-erythrose 4-phosphate pH 6.8, 30°C, wild-type enzyme Neisseria meningitidis
2.5.1.54 14.8
-
 D-erythrose 4-phosphate pH 6.8, 30°C, mutant R126S Neisseria meningitidis
2.5.1.54 25
-
 phosphoenolpyruvate pH 6.8, 30°C, wild-type enzyme Neisseria meningitidis
2.5.1.54 25
-
 phosphoenolpyruvate pH 6.8, 30°C, mutant S213G Neisseria meningitidis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.54 6.8
-
 assay at Neisseria meningitidis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.54 additional information
-
 additional information inhibition kinetics of wld-type and mutant enzymes, overview Neisseria meningitidis

General Information

EC Number General Information Comment Organism
2.5.1.54 metabolism the enzyme catalyzes the first reaction in the shikimate pathway leading to the biosynthesis of aromatic metabolites including the aromatic acids L-Trp, L-Phe, and L-Tyr. As the entry point, feedback inhibition of DAH7PS by pathway end products is a key mechanism for the control of pathway flux Neisseria meningitidis
2.5.1.54 additional information allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme. The nature of the extra barrel extensions is directly implicated in the sensitivity of the DAH7PS enzymes to allosteric control Neisseria meningitidis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.54 370
-
 D-erythrose 4-phosphate pH 6.8, 30°C, mutant R126S Neisseria meningitidis
2.5.1.54 590
-
 D-erythrose 4-phosphate pH 6.8, 30°C, wild-type enzyme Neisseria meningitidis
2.5.1.54 1700
-
 phosphoenolpyruvate pH 6.8, 30°C, mutant S213G Neisseria meningitidis
2.5.1.54 2300
-
 phosphoenolpyruvate pH 6.8, 30°C, wild-type enzyme Neisseria meningitidis