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

BRENDA support

Literature summary for 5.99.1.4 extracted from

  • Thompson, L.C.; Ladner, J.E.; Codreanu, S.G.; Harp, J.; Gilliland, G.L.; Armstrong, R.N.
    2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida (2007), Biochemistry, 46, 6710-6722.
    View publication on PubMed
Search for more literature for 5.99.1.4

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the enzyme at 1.7 A resolution Pseudomonas putida

General Stability

General Stability Organism
unstable in absence of GSH Pseudomonas putida

Inhibitors

Inhibitors Comment Organism Structure
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate i.e. (E)-2'-hydroxybenzylidenepyruvate Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.084
-
 2-hydroxychromene-2-carboxylate pH 7.0, 25°C Pseudomonas putida
0.138
-
 (E)-2'-hydroxybenzylidenepyruvate pH 7.0, 25°C Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida Q51948
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxy-2H-chromene-2-carboxylate glutathione (GSH)-dependent interconversion. The isomerization reaction involves a short-lived covalent adduct between the sulfur of GSH and C7 of the substrate Pseudomonas putida (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate i.e. (E)-2'-hydroxybenzylidenepyruvate, i.e. trans-o-hydroxybenzylidenepyruvate ?

Subunits

Subunits Comment Organism
dimer
-
 Pseudomonas putida

Synonyms

Synonyms Comment Organism
2-hydroxychromene-2-carboxylic acid isomerase
-
 Pseudomonas putida
HCCA isomerase
-
 Pseudomonas putida

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
19
-
 (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate pH 7.0, 25°C Pseudomonas putida
47
-
 2-hydroxy-2H-chromene-2-carboxylate pH 7.0, 25°C Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
glutathione the dimeric protein binds one molecule of GSH very tightly and a second molecule of GSH with much lower affinity. The enzyme is unstable in the absence of GSH. The turnover number in the forward direction greatly exceeds off rates for GSH, suggesting that GSH acts as a tightly bound cofactor in the reaction. Km: 0.017 mM Pseudomonas putida

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.136
-
 (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate pH 7.0, 25°C Pseudomonas putida