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Literature summary extracted from

  • Alberty, R.A.
    Fumarase (1961), The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. ), 5, 531-544.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.2
-
 Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.2 meso-tartrate
-
 Sus scrofa
4.2.1.2 sulfhydryl reagents
-
 Saccharomyces cerevisiae
4.2.1.2 sulfhydryl reagents no inhibition Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.2 additional information Sus scrofa enzyme of the tricarboxylic acid cycle ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.2 Azotobacter vinelandii
-
-
-
4.2.1.2 Saccharomyces cerevisiae
-
-
-
4.2.1.2 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.2 (S)-malate = fumarate + H2O mechanism Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.2 heart
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.2 (S)-malate
-
 Sus scrofa fumarate + H2O
-
 r
4.2.1.2 (S)-malate
-
 Saccharomyces cerevisiae fumarate + H2O
-
 r
4.2.1.2 fumarate + H2O
-
 Sus scrofa L-malate
-
 r
4.2.1.2 fumarate + H2O
-
 Saccharomyces cerevisiae L-malate
-
 r
4.2.1.2 additional information enzyme of the tricarboxylic acid cycle Sus scrofa ?
-
 ?