Methylenetetrahydrofolate reductase
From Proteopedia
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==MTHFR== | ==MTHFR== | ||
<scene name='90/907473/Mthfr_protein/1'>first scene</scene> | <scene name='90/907473/Mthfr_protein/1'>first scene</scene> | ||
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| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a default text for your page '''Shaylie Albright/MTHFR'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
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| + | <StructureSection load='' size='340' side='right' scene='90/907473/Mthfr_protein/1'> | ||
| + | This is a default text for your page '''Shaylie Albright/MTHFR'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| + | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Structural highlights == | == Structural highlights == | ||
MTHFR<scene name='90/907473/Superposition/4'>ping pong mechanism</scene> | MTHFR<scene name='90/907473/Superposition/4'>ping pong mechanism</scene> | ||
Revision as of 15:09, 6 April 2022
Contents |
MTHFR
Function
Methylenetetrahydrofolate reductase (MTHFR) is a regulatory agent of one carbon folate metabolism. The enzyme catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate to be recycled back into the folate cycle, and for aiding folate uptake in the body. This reduction reaction requires the cofactor molecule flavin adenine dinucleotide (FAD) and the second substrate nicotinamide adenine dinucleotide phosphate (NADPH) as the electron donor in the reaction. MTHFR has a unique folding structure. Its N-terminal is abundant in serine and acts as a phosphorylation site, its situated in close proximity to it's C-terminal S-adenosyl methionine (SAM) binding site. A linker joins the catalytic domain (N-terminal) to the regulatory domain (C-terminal) for interaction and increases the sensitivity to SAM binding and feedback properties.
Disease
In addition to the folate cycle, MTHFR is also a major component of the homeostasis of homocysteine in the blood stream. When this homeostasis is disrupted, mutations are created that result in hyperhomocysteinemia with homocystinuria, or mild hyperhomocysteinemia. Hyperhomocysteinemia is an excess of the amino acid circulating in the body, and is a direct correlation of cardiovascular disease, Alzheimer's disease, depression, and neural tube defects within the fetus. Furthermore, homocystinuria is clinically described as the body's inability to adequately process homocysteine and the amino acid methionine. This dysfunction can be clinically presented with skeletal, vision, and blood clotting abnormalities coupled with learning disorders.
Relevance
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
Proteopedia Page Contributors and Editors (what is this?)
Shaylie Albright, Karsten Theis, Michal Harel, Michael O'Shaughnessy, Kia Yang, Anna Postnikova
