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Literature summary for 4.2.1.2 extracted from

  • Behal, R.H.; Oliver, D.J.
    Biochemical and molecular characterization of fumarase from plants: purification and characterization of the enzyme--cloning, sequencing, and expression of the gene (1997), Arch. Biochem. Biophys., 348, 65-74.
    View publication on PubMed
Search for more literature for 4.2.1.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate
-
 Arabidopsis thaliana
ADP
-
 Arabidopsis thaliana
AMP
-
 Arabidopsis thaliana
citrate
-
 Arabidopsis thaliana
pyruvate
-
 Arabidopsis thaliana
succinate
-
 Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.45
-
 (S)-malate
-
 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Arabidopsis thaliana 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
175000
-
 gel filtration Pisum sativum
190000
-
 gel filtration Pisum sativum

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P93033
-
-
Pisum sativum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
plant etiolated Arabidopsis thaliana
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
238
-
-
 Arabidopsis thaliana

Storage Stability

Storage Stability Organism
4°C or -20°C, stable for several days Pisum sativum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate
-
 Arabidopsis thaliana fumarate + H2O
-
 r

Subunits

Subunits Comment Organism
tetramer
-
 Pisum sativum