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Literature summary for 5.2.1.2 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

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

Inhibitors

Inhibitors Comment Organism Structure
GSSG
-
Vibrio sp.
S-Methylglutathione
-
Vibrio sp.

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Vibrio sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Vibrio sp.

Reaction

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

Substrates and Products (Substrate)

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