From Proteopedia
proteopedia linkproteopedia link 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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Physiological function of enzyme ALAS2
ALAS role in heme biosynthesis
Structure of human ALAS2
Mutations causing blood diseases
X-linked sideroblastic anemia
X-linked protoporphyria
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
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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
