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Literature summary extracted from

  • Morrison, W.S.; Wong, G.; Seltzer, S.
    Maleylacetone cis-trans-isomerase: affinity chromatography on glutathione-bound Sepharose. Two-substrate-binding sequence from inhibition patterns (1976), Biochemistry, 15, 4228-4233.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.2.1.2 GSH the enzyme binds glutathione through the backbone of the tripeptide Vibrio sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.2.1.2 GSSG
-
Vibrio sp.
5.2.1.2 S-Methylglutathione
-
Vibrio sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.2.1.2 0.14
-
GSH
-
Vibrio sp.

Organism

EC Number Organism UniProt Comment Textmining
5.2.1.2 Vibrio sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.2.1.2
-
Vibrio sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
5.2.1.2 4-Maleylacetoacetate = 4-fumarylacetoacetate ordered sequence of binding: maleylacetone first followed by glutathione Vibrio sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.2.1.2 (+/-)-2-bromo-3-(4-nitrophenyl)propionic acid + glutathione
-
Vibrio sp. 2-(glutathion-S-yl)-3-(4-nitrophenyl)propanoic acid
-
?
5.2.1.2 Maleylacetoacetate
-
Vibrio sp. Fumarylacetoacetate
-
?