Fumarase

spinqualitylabelsall models Fumarase tetramer complex with malate , 4adl Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Fumarase or fumarase hydratase is used in the citric acid cycle to conduct a transition step in the production of energy to make NADH. It metabolizes fumarate in the cytosol, which becomes a byproduct of the urea cycle and amino acid catabolism. It catalyzes the addition of water to fumarate to make L-malate. This is a reversible reaction. See also: Krebs cycle carbons Krebs cycle importance Krebs cycle overview Krebs cycle reactions Citric Acid Cycle Krebs cycle step 7 Fumarase 2 Glyoxylate cycle Other interesting information Fumarase or fumarate hydratase is dominant in fetal and adult tissues and largely expressed in the skin, parathyroid, lymph, and colon There are two classes of fumarases, which depend on the arrangement of their relative subunit, their metal requirement, and their thermal stability. Class I fumarases can change their state or become inactive when exposed to heat or radiation. They are sensitive to superoxide anions and Fe2+ dependent. Class II fumarases are found in eukaryotes and prokaryotes. They are iron-independent and thermal-stable. Disease Fumarase deficiency is an autosomal recessive metabolic disorder distinguished by a deficiency of the enzyme fumarate hydratase and indicated by an excess of fumaric acid in the urine. It is common in infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of fumarase. Fumarase Scenes Overview Secondary Structure Hydrophilic

3D structures of fumarase

Updated on 07-July-2025

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• Fumarase
  • Krebs cycle carbons – hFUM (mutant) – human
    
  • Krebs cycle importance, Krebs cycle overview, Krebs cycle reactions – hFUM residues 44-510 - human
    
  • Citric Acid Cycle, Krebs cycle step 7, Fumarase 2 – hFUM (mutant)
    
  • Glyoxylate cycle, 6ku6 – FUM (mutant) – yeast
    
  • 3qbp – FUM – Mycobacterium marinum
    
  • 3no9 – MtFUM II – Mycobacterium tuberculosis
    
  • 4apa - MtFUM II (mutant)
    
  • 3rd8 – FUM II – Mycobacterium smegmatis
    
  • 3gtd – FUM II – Rickettsia prowazekii
    
  • 2isb – FUM I – Archaeoglobus fulgidus
    
  • 1kq7, 1yfe, 6os7, 8sbs - EcFUM II (mutant) – Escherichia coli
    
  • 4hgv – FUM II – Sinorhizobium meliloti
    
  • 3tv2 – FUM II – Burkholderia pseudomallei
    
  • 1vdk – FUM II (mutant) – Thermus thermophilus
    
  • 6n1m – FUM II – Legionella pneumophila
    
  • 7miw – FUM II – Elizabethakingia anophelis
    
  • 6u4o – FUM II – Schistosoma mansoni
    
  • 7c1c – MsFUM II – Mannheimia succiniciproducens
    
  • 6unz – LmFUM II – Leishmania major
    
  • 9bpw – FUM C – Staphylococcus aureus
    
• Fumarase binary complexes
  • 7lub - hFUM II + phosphono-propionate
    
  • 1fur - EcFUM II (mutant) + malate
    
  • 6nz9 - EcFUM II + citrate
    
  • 2fus, 6nza, 6nzb, 6nzc, 6os7, 6p3c - EcFUM II (mutant) + citrate
    
  • 4adl - MtFUM II + malate
    
  • 4adm - MtFUM II + tartrate
    
  • 4apb - MtFUM II (mutant) + fumarate
    
  • 5f92 – MtFUM II + formate
    
  • 7c1a – MsFUM II + malate
    
  • 7c18 – MsFUM II + fumarate
    
  • 6uo0, 6upm, 6upo, 6uq9, 6uql, 6uqm – LmFUM II (mutant) + malate
    
  • 6uoi – LmFUM II + malonate
    
  • 6up9 – LmFUM II (mutant) + malonate
    
  • 6uoj – LmFUM II + succinate
    
  • 7t93 – FUM II + malate – Mycobacterium ulcerans
    
• Fumarase ternary complexes
  • 1fup - EcFUM II + pyromellitic acid + malate
    
  • 1fuq - EcFUM II + pyromellitic acid + citrate
    
  • 1fuo - EcFUM II + citrate + malate
    
  • 5f91, 6s43, 6s7k, 6s7s, 6s7u, 6s7w, 6s7z, 6s88 – MtFUM II + modulator + formate
    
  • 6uqn – LmFUM II (mutant) + malate + fumarate
    
  • 6uq8, 6uqb – LmFUM II (mutant) + malate + malonate
    

References

Wikipedia. <https://en.wikipedia.org/wiki/Fumarase>, Wikipedia. <https://en.wikipedia.org/wiki/Enolase>, University of Wisconsin- Eau Claire. <https://www.chem.uwec.edu/Webpapers_F99/Pages/Webpapers_F99/golnercm/Pages/descrip.html>, Virtual Chembook. Elmhurst College. <https://www.elmhurst.edu/~chm/vchembook/601glycolysisrx.html>

Author

Originally Completed by Sydney Park

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Jaime Prilusky, Alexander Berchansky