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Literature summary for 2.5.1.54 extracted from

  • Sobota, J.M.; Gu, M.; Imlay, J.A.
    Intracellular hydrogen peroxide and superoxide poison 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase, the first committed enzyme in the aromatic biosynthetic pathway of Escherichia coli (2014), J. Bacteriol., 196, 1980-1991.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
gene aroG, recombinant expression of His10-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain DH5alpha Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
H2O2 DAHP synthase enzymes are inactivated by H2O2 in vitro and in vivo, H2O2 displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide Escherichia coli
additional information isozyme AroG is not inhibited by L-Phe. In peroxide-stressed cells, the enzyme accumulates as an apoprotein, potentially with an oxidized cysteine residue. In superoxide-stressed cells, the enzyme acquires a nonactivating zinc ion in its active site, an apparent consequence of the repeated ejection of iron. Manganese supplementation protects the activity in both cases, which matches the ability of manganese to metallate the enzyme and to provide substantial oxidant-resistant activity. The damage to DAHP synthase can be completely restored in vivo, while in vitro, restoration is only partly, overview. Escherichia coli attempts to compensate for diminished DAHP synthase activity by increasing expression Escherichia coli
superoxide displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide. Superoxide stress promotes the mismetallation of DAHP synthase Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a mononuclear iron enzyme, the enzyme required divalent metal cations, Fe2+ activates best, iron is the prosthetic metal in vivo Escherichia coli
Mn2+ can substitute for Fe2+, activates DAHP synthase to about 70% of the iron-activated sample Escherichia coli
Zn2+ cannot well substitute for Fe2+, activates DAHP synthase to about 20% of the iron-activated sample Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AB91 gene aroG
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His10-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography, followed by tag cleavage with factor Xa and again affinity chromatography and dialysis to remove the tag Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
3-deoxy-D-arabinoheptulosonate 7-phosphate synthase
-
 Escherichia coli
DAHP synthase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4
-
 assay at Escherichia coli

Expression

Organism Comment Expression
Escherichia coli enzyme damage by reactive oxidants, H2O2 and superoxide, induces the enzyme expression in Escherichia coli, which attempts to compensate for diminished DAHP synthase activity by increasing expression up

General Information

General Information Comment Organism
evolution DAHP synthase belongs to a family of mononuclear iron-containing enzymes that are disabled by oxidative stress Escherichia coli
metabolism first committed enzyme in the aromatic biosynthetic pathway of Escherichia coli, shikimate biosynthesis pathway overview Escherichia coli