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Literature summary for 5.3.2.6 extracted from

  • Stivers, J.; Abeygunawardana, C.; Mildvan, A.; Hajipour, G.; Whitman, C.; Chen, L.
    Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies (1996), Biochemistry, 35, 803-813.
    View publication on PubMed
Search for more literature for 5.3.2.6

Inhibitors

Inhibitors Comment Organism Structure
3-Bromopyruvate a active-site-directed irreversible inhibitor, modification of three active sites per hexamer abolishes essentially all activity of the hexamer, pH dependence of inactivation Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp. CF 600
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 4-oxalocrotonate tautomerase catalyzes the isomerization of unsaturated 2-oxo acids, converting unconjugated ketones to the conjugated isomers via a dienolic intermediate Pseudomonas sp. ?
-
 ?
additional information 4-oxalocrotonate tautomerase catalyzes the isomerization of unsaturated 2-oxo acids, converting unconjugated ketones to the conjugated isomers via a dienolic intermediate Pseudomonas sp. CF 600 ?
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Pseudomonas sp.

Synonyms

Synonyms Comment Organism
4-OT
-
 Pseudomonas sp.
4-oxalocrotonate tautomerase
-
 Pseudomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 assay at Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.75
-
 assay at Pseudomonas sp.

General Information

General Information Comment Organism
malfunction modification by 3-bromopyruvate of three active sites per hexamer abolishes essentially all activity of the hexamer, spectrocopic and sequence analysis of labeled peptides, overview Pseudomonas sp.