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Literature summary for 2.5.1.54 extracted from

  • Cross, P.J.; Parker, E.J.
    Allosteric inhibitor specificity of Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (2013), FEBS Lett., 587, 3063-3068.
    View publication on PubMed
Search for more literature for 2.5.1.54

Cloned(Commentary)

Cloned (Comment) Organism
gene aroG, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain (DE3) Star Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
H29A site-directed mutagenesis, the mutant is inhibited by both L-Tyr and L-Phe Thermotoga maritima
H29S/S31H site-directed mutagenesis, the mutant is inhibited to a greater extent by L-Phe than L-Tyr Thermotoga maritima
S31G site-directed mutagenesis, the mutation severely reduces inhibition by L-Tyr Thermotoga maritima

Inhibitors

Inhibitors Comment Organism Structure
L-phenylalanine involved in allosteric regulation of the enzyme, inhibits the wild-type enzyme, and enzyme mutants H29A and H29S/S31H Thermotoga maritima
L-tyrosine allosteric regulation of the enzyme is mediated by L-Tyr binding to a discrete ACT regulatory domain appended to a core catalytic (beta/alpha)8 barrel, highly reduced inhibition of enzyme mutant S31G. Comparison of the position of the regulatory ACT domain of TmaDAH7PS in the unbound and L-Tyr-bound conformations, overview Thermotoga maritima
additional information small angle X-ray (SAXS) scattering analysis Thermotoga maritima

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Thermotoga maritima
0.00485
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, wild-type enzyme Thermotoga maritima
0.0128
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant S31G Thermotoga maritima
0.013
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, wild-type enzyme Thermotoga maritima
0.021
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant H29A Thermotoga maritima
0.028
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant H29S/S31H Thermotoga maritima
0.03
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant H29A Thermotoga maritima
0.033
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant S31G Thermotoga maritima
0.039
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant H29S/S31H Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O Thermotoga maritima
-
 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9WYH8 gene aroF
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
-
 Thermotoga maritima 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
-
 Thermotoga maritima
DAH7PS
-
 Thermotoga maritima
phospho-2-dehydro-3-deoxyheptonate aldolase UniProt Thermotoga maritima
TmaDAH7PS
-
 Thermotoga maritima

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11.7
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, wild-type enzyme Thermotoga maritima
11.7
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, wild-type enzyme Thermotoga maritima
14.1
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant H29S/S31H Thermotoga maritima
14.1
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant H29S/S31H Thermotoga maritima
14.3
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant H29A Thermotoga maritima
14.3
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant S31G Thermotoga maritima
17.5
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant H29A Thermotoga maritima
17.5
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant S31G Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Thermotoga maritima

General Information

General Information Comment Organism
metabolism the enzyme catalyses the first step of the shikimate pathway for the biosynthesis of aromatic amino acids Thermotoga maritima
physiological function allosteric regulation of the enzyme is mediated by L-Tyr binding to a discrete ACT regulatory domain appended to a core catalytic (beta/alpha)8 barrel Thermotoga maritima

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
360
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant H29S/S31H Thermotoga maritima
430
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant S31G Thermotoga maritima
500
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant H29S/S31H Thermotoga maritima
580
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, mutant H29A Thermotoga maritima
700
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant H29A Thermotoga maritima
900
-
 D-erythrose 4-phosphate pH 7.3, temperature not specified in the publication, wild-type enzyme Thermotoga maritima
1400
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, mutant S31G Thermotoga maritima
2400
-
 phosphoenolpyruvate pH 7.3, temperature not specified in the publication, wild-type enzyme Thermotoga maritima