Fumarase: Difference between revisions
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<StructureSection load='4adl' size='350' side='right' caption='Fumarase tetramer complex with malate , [[4adl]]' scene=''> | |||
== 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<ref>PMID:16204892</ref>. See also:<br /> | |||
*[[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== | ==Fumarase Scenes== | ||
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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== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
{{#tree:id=OrganizedByTopic|openlevels=0| | |||
*Fumarase | |||
[[3qbp]] – FUM – ''Mycobacterium marinum''<br /> | **[[6ebt]] – hFUM (mutant) – human<br /> | ||
[[3no9]] – | **[[3e04]], [[5d6b]], [[5upp]] – hFUM residues 44-510 - human<br /> | ||
[[ | **[[6ebt]], [[6v8f]], [[6vbe]] – hFUM (mutant)<br /> | ||
[[ | **[[1yfm]], [[6ku6]] – FUM (mutant) – yeast<br /> | ||
[[2isb]] – FUM I – ''Archaeoglobus fulgidus''<br /> | **[[3qbp]] – FUM – ''Mycobacterium marinum''<br /> | ||
[[ | **[[3no9]] – MtFUM II – ''Mycobacterium tuberculosis''<br /> | ||
[[ | **[[4apa]] - MtFUM II (mutant)<br /> | ||
**[[3rd8]] – FUM II – ''Mycobacterium smegmatis''<br /> | |||
**[[3gtd]] – FUM II – ''Rickettsia prowazekii''<br /> | |||
**[[2isb]] – FUM I – ''Archaeoglobus fulgidus''<br /> | |||
**[[1kq7]], [[1yfe]], [[6os7]] - EcFUM II (mutant) – ''Escherichia coli''<br /> | |||
**[[4hgv]] – FUM II – ''Sinorhizobium meliloti''<br /> | |||
**[[3tv2]] – FUM II – ''Burkholderia pseudomallei''<br /> | |||
**[[1vdk]] – FUM II (mutant) – ''Thermus thermophilus''<br /> | |||
**[[6n1m]] – FUM II – ''Legionella pneumophila''<br /> | |||
**[[7miw]] – FUM II – ''Elizabethakingia anophelis''<br /> | |||
**[[6u4o]] – FUM II – ''Schistosoma mansoni''<br /> | |||
**[[7c1c]] – MsFUM II – ''Mannheimia succiniciproducens''<br /> | |||
**[[6unz]] – LmFUM II – ''Leishmania major''<br /> | |||
*Fumarase binary complexes | |||
[[1fur]] - EcFUM II (mutant) + malate<br /> | **[[1fur]] - EcFUM II (mutant) + malate<br /> | ||
[[2fus]] - EcFUM II (mutant) + citrate | **[[6nz9]] - EcFUM II + citrate<br /> | ||
**[[2fus]], [[6nza]], [[6nzb]], [[6nzc]], [[6os7]], [[6p3c]] - EcFUM II (mutant) + citrate<br /> | |||
**[[4adl]] - MtFUM II + malate<br /> | |||
**[[4adm]] - MtFUM II + tartrate<br /> | |||
**[[4apb]] - MtFUM II (mutant) + fumarate<br /> | |||
**[[5f92]] – MtFUM II + formate<br /> | |||
**[[7c1a]] – MsFUM II + malate <br /> | |||
**[[7c18]] – MsFUM II + fumarate <br /> | |||
**[[6uo0]], [[6upm]], [[6upo]], [[6uq9]], [[6uql]], [[6uqm]] – LmFUM II (mutant) + malate <br /> | |||
**[[6uoi]] – LmFUM II + malonate <br /> | |||
**[[6up9]] – LmFUM II (mutant) + malonate <br /> | |||
**[[6uoj]] – LmFUM II + succinate <br /> | |||
*Fumarase ternary complexes | |||
[[1fup]] - EcFUM II + pyromellitic acid + malate<br /> | **[[1fup]] - EcFUM II + pyromellitic acid + malate<br /> | ||
[[1fuq]] - EcFUM II + pyromellitic acid + citrate<br /> | **[[1fuq]] - EcFUM II + pyromellitic acid + citrate<br /> | ||
[[1fuo]] - EcFUM II + citrate + malate | **[[1fuo]] - EcFUM II + citrate + malate<br /> | ||
**[[5f91]], [[6s43]], [[6s7k]], [[6s7s]], [[6s7u]], [[6s7w]], [[6s7z]], [[6s88]] – MtFUM II + modulator + formate<br /> | |||
**[[6uqn]] – LmFUM II (mutant) + malate + fumarate <br /> | |||
**[[6uq8]], [[6uqb]] – LmFUM II (mutant) + malate + malonate <br /> | |||
}} | |||
==References== | ==References== | ||
<references/> | |||
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> | 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> | ||
Latest revision as of 12:01, 11 January 2023
FunctionFumarase 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[1]. See also:
Other interesting informationFumarase 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. DiseaseFumarase 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
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3D structures of fumarase3D structures of fumarase
Updated on 11-January-2023
ReferencesReferences
- ↑ 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