Fumarase
From Proteopedia
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'''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. | '''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. | ||
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==Other interesting information== | ==Other interesting information== | ||
| - | '''Fumarase''' is dominant in fetal and adult tissues and largely expressed in the skin, parathyroid, lymph, and colon | + | '''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. | 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. | ||
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 of infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of Fumarase. | 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 of infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of Fumarase. | ||
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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 /> | ||
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==3D structures of fumarase== | ==3D structures of fumarase== | ||
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[[3no9]] – MtFUM II – ''Mycobacterium tuberculosis''<br /> | [[3no9]] – MtFUM II – ''Mycobacterium tuberculosis''<br /> | ||
[[4apa]] - MtFUM II (mutant)<br /> | [[4apa]] - MtFUM II (mutant)<br /> | ||
| + | [[3rd8]] – FUM II – ''Mycobacterium smegmatis''<br /> | ||
[[3gtd]] – FUM II – ''Rickettsia prowazekii''<br /> | [[3gtd]] – FUM II – ''Rickettsia prowazekii''<br /> | ||
[[3e04]] – FUM residues 44-510 – human<br /> | [[3e04]] – FUM residues 44-510 – human<br /> | ||
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[[2yfe]], [[1yfm]] – EcFUM II – ''Escherichia coli''<br /> | [[2yfe]], [[1yfm]] – EcFUM II – ''Escherichia coli''<br /> | ||
[[1vdk]], [[1kq7]], [[1yfe]] - EcFUM II (mutant)<br /> | [[1vdk]], [[1kq7]], [[1yfe]] - EcFUM II (mutant)<br /> | ||
| - | [[4hgv]] – FUM II – ''Sinorhizobium meliloti'' | + | [[4hgv]] – FUM II – ''Sinorhizobium meliloti''<br /> |
| + | [[3tv2]] – FUM II – ''Burkholderia pseudomallei''<br /> | ||
===Fumarase binary complexes=== | ===Fumarase binary complexes=== | ||
Revision as of 07:04, 13 August 2014
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.
Contents |
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. 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 of infants with neurologic abnormalities and its potential causes include cytosolic and mitochondrial forms of Fumarase.
Fumarase Scenes
3D structures of fumarase
Updated on 13-August-2014
Fumarase
3qbp – FUM – Mycobacterium marinum
3no9 – MtFUM II – Mycobacterium tuberculosis
4apa - MtFUM II (mutant)
3rd8 – FUM II – Mycobacterium smegmatis
3gtd – FUM II – Rickettsia prowazekii
3e04 – FUM residues 44-510 – human
2isb – FUM I – Archaeoglobus fulgidus
2yfe, 1yfm – EcFUM II – Escherichia coli
1vdk, 1kq7, 1yfe - EcFUM II (mutant)
4hgv – FUM II – Sinorhizobium meliloti
3tv2 – FUM II – Burkholderia pseudomallei
Fumarase binary complexes
1fur - EcFUM II (mutant) + malate
2fus - EcFUM II (mutant) + citrate
4adl - MtFUM II + malate
4adm - MtFUM II + tartrate
4apb - MtFUM II (mutant) + fumarate
Fumarase ternary complexes
1fup - EcFUM II + pyromellitic acid + malate
1fuq - EcFUM II + pyromellitic acid + citrate
1fuo - EcFUM II + citrate + malate
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>
Author
Originally Completed by Sydney Park
