Fumarase: Difference between revisions

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{{STRUCTURE_4adl|  PDB=4adl | SIZE=350| SCENE= |right|CAPTION=Fumarase tetramer complex with malate   , [[4adl]] }}
<StructureSection load='4adl' size='350' side='right' caption='Fumarase tetramer complex with malate , [[4adl]]' scene=''>
== Function ==
== Function ==


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<scene name='User:Sydney_Park/Secondary_structure/1'>Secondary Structure</scene><br />
<scene name='User:Sydney_Park/Secondary_structure/1'>Secondary Structure</scene><br />
<scene name='User:Sydney_Park/Leuthydro/1'>Hydrophilic</scene><br />
<scene name='User:Sydney_Park/Leuthydro/1'>Hydrophilic</scene><br />
</StructureSection>


==3D structures of fumarase==   
==3D structures of fumarase==   

Revision as of 20:10, 10 May 2016

Function

Fumarase 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 make S-malate. This is a reversible reaction[1]. See also:

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




Fumarase tetramer complex with malate , 4adl

Drag the structure with the mouse to rotate

3D structures of fumarase3D structures of fumarase

Updated on 10-May-2016

ReferencesReferences

  1. Weaver T. Structure of free fumarase C from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub, 2005 Sep 28. PMID:16204892 doi:http://dx.doi.org/10.1107/S0907444905024194

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

AuthorAuthor

Originally Completed by Sydney Park

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Jaime Prilusky, Alexander Berchansky