Sandbox Reserved 1547
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{{ Sandbox_Reserved_GGC_BHCM4100_1}} | {{ Sandbox_Reserved_GGC_BHCM4100_1}} | ||
==Enoyl-coa hydratase complexed with octanoyl-coa== | ==Enoyl-coa hydratase complexed with octanoyl-coa== | ||
| - | Alternative names: Enoyl hydrase, Unsaturated acyl-CoA hydratase.Cocrystallized with octanoyl-CoA.The structure of the hexameric rat mitochondrial enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA. | + | Alternative names: Crotonase, Enoyl hydrase, Unsaturated acyl-CoA hydratase.Cocrystallized with octanoyl-CoA.The structure of the hexameric rat mitochondrial enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA. |
<scene name='80/806433/Hetero_components_ligand3/1'>Octanoyl Coenzyme A, four Hetero Components : CO8a, CO8b, CO8c, CO8d</scene> | <scene name='80/806433/Hetero_components_ligand3/1'>Octanoyl Coenzyme A, four Hetero Components : CO8a, CO8b, CO8c, CO8d</scene> | ||
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== Function == | == Function == | ||
| - | Short-chain enoyl-CoA hydratase (ECHS1) is a multifunctional mitochondrial matrix enzyme that is involved in the oxidation of fatty acids and essential amino acids such as valine. | + | MTP catalyzes the last three steps of mitochondrial β-oxidation; LCHAD, long-chain enoyl-CoA hydratase, and long-chain thiolase are all part of the MTP. Short-chain enoyl-CoA hydratase (ECHS1) is a multifunctional mitochondrial matrix enzyme that is involved in the oxidation of fatty acids and essential amino acids such as valine. The MTP is a membrane bound complex and it has 4 alpha and 4 beta sub-unite the gene that codes for our enoyl CoA is found on alpha subunit and is coded by the HADHA gene on chromosome 2p23.3 |
The active sites of the N- and the C-terminal parts catalyse,respectively, the second (2E-enoyl-CoA hydration) and third (3-hydroxy-acyl-CoA dehydrogenation) reactions | The active sites of the N- and the C-terminal parts catalyse,respectively, the second (2E-enoyl-CoA hydration) and third (3-hydroxy-acyl-CoA dehydrogenation) reactions | ||
[2] of the b-oxidation pathway of fatty acid metabolism. Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. The chains homologous to 2DUB: 1DUB, 1EY3. | [2] of the b-oxidation pathway of fatty acid metabolism. Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. The chains homologous to 2DUB: 1DUB, 1EY3. | ||
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O | (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O | ||
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| + | [[Image:Enoly_CoA_Hyratase.png ]] | ||
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== Disease == | == Disease == | ||
| - | A catalytic water, bound | + | Mutation of any type like deletion,and or insertion on the HADHA will result in a rare autosomal recessive complete mitochondrial trifunctional protein deficiency, in which all three enzymatic processes do not function properly; more common is LCHAD deficiency, due to a less-encompassing HADHA missense mutation. This deficiency is rare satistics show that in the united States it rages from 1/75,00 to 1/250,000. more most common incidence is recorded in Finland. Clinically, LCHAD deficiency manifests early, typically in the first year of life, with episodes of hypoketotic hypoglycemia accompanied by variable other manifestations, including poor feeding, vomiting, lethargy, hypotonia, hepatic failure, skeletal myopathy and possibly rhabdomyolysis, early-onset cardiomyopathy, sensory polyneuropathy, and sudden death in infancy. |
| - | between the OE1-atoms of the two catalytic glutamates, Glu103 and | + | The diagnosis of LCHAD/MTP deficiency may be suspected by elevation of long-chain fatty acyl-CoAs (C14, C16, and C18), especially 16-carbon acyl-CoA (C16), along with elevated urinary dicarboxylic acids. |
| - | Glu123, plays an important role in the enoyl-CoA isomerase and the | + | A catalytic water, bound between the OE1-atoms of the two catalytic glutamates, Glu103 and Glu123, plays an important role in the enoyl-CoA isomerase and the enoyl-CoA hydratase reaction mechanism of MFE1. |
| - | enoyl-CoA hydratase reaction mechanism of MFE1. | + | |
Dysfunctional MFE2 is one of the most common reasons of peroxi- somal disorder in humans | Dysfunctional MFE2 is one of the most common reasons of peroxi- somal disorder in humans | ||
== Relevance == | == Relevance == | ||
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https://www.uniprot.org/uniprot/P14604#function | https://www.uniprot.org/uniprot/P14604#function | ||
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| + | https://www.sciencedirect.com/topics/medicine-and-dentistry/enoyl-coenzyme-a-hydratase | ||
| + | Huaning Zhang, Huaning Zhang, et al. “Fatty Acid Biosynthesis and Oxidation.” ScienceDirect, Elsevier, 17 Mar. 2010, www.sciencedirect.com/science/article/pii/B9780080453828006687. | ||
Current revision
| This Sandbox is Reserved from May 28 through July 01, 2019 for use in the course Advanced Biochemistry BCHM 4100 taught by Tom Gluick at the Georgia Gwinnett College. This reservation includes Sandbox Reserved 1544 through Sandbox Reserved 1555. |
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Enoyl-coa hydratase complexed with octanoyl-coa
Alternative names: Crotonase, Enoyl hydrase, Unsaturated acyl-CoA hydratase.Cocrystallized with octanoyl-CoA.The structure of the hexameric rat mitochondrial enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA.
The source of the sample from organism: is from mitochondrial Cell of iver of Norway rat, Rattus norvegicus. Organism_taxid: 10116.
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