User:Adéla Fejfarová/Sandbox 1
From Proteopedia
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| - | == | + | =ALAS2 in erythroid heme biosynthesis disorders= |
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| + | Enzyme 5’-aminolevulinic acid synthase (ALAS, EC 2.3.1.37) catalyzes the first step in the biosynthesis of heme molecule in alpha-proteobacteria and mitochondria of nonplant eukaryotes. In vertebrates there are two isoforms of the ALAS enzyme. The erythroid-specific ALAS2 located on chromosome X is expressed during erythropoiesis and mediates the biosynthesis of heme that carries oxygen in hemoglobin. Different mutations thorough the sequence of the enzyme lead to two ALAS2-associated blood disorders. Namely X-linked sideroblastic anemia (XLSA, MIM 300751) and X-linked protoporphyria (XLP, MIM 300752) caused typically by loss-of-function (enzyme deficiency) and gain-of-function (enzyme hyperactivity), respectively. | ||
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a default text for your page '''Adéla Fejfarová/Sandbox 1'''. 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. | ||
| - | == | + | == Physiological function of enzyme ALAS2 == |
| - | == | + | === ALAS role in heme biosynthesis === |
| - | == | + | === Structure of human ALAS2 === |
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| + | == Mutations causing blood diseases == | ||
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| + | === X-linked sideroblastic anemia === | ||
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| + | === X-linked protoporphyria === | ||
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| + | 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 == | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 18:58, 27 April 2022
ALAS2 in erythroid heme biosynthesis disorders
Enzyme 5’-aminolevulinic acid synthase (ALAS, EC 2.3.1.37) catalyzes the first step in the biosynthesis of heme molecule in alpha-proteobacteria and mitochondria of nonplant eukaryotes. In vertebrates there are two isoforms of the ALAS enzyme. The erythroid-specific ALAS2 located on chromosome X is expressed during erythropoiesis and mediates the biosynthesis of heme that carries oxygen in hemoglobin. Different mutations thorough the sequence of the enzyme lead to two ALAS2-associated blood disorders. Namely X-linked sideroblastic anemia (XLSA, MIM 300751) and X-linked protoporphyria (XLP, MIM 300752) caused typically by loss-of-function (enzyme deficiency) and gain-of-function (enzyme hyperactivity), respectively.
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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
