EVOLUTIONARY CONSIDERATION ON 5-AMINOLEVULINATE SYNTHASE IN NATURE
β Scribed by TAMIKO OH-HAMA
- Book ID
- 110238249
- Publisher
- Springer Netherlands
- Year
- 1997
- Tongue
- English
- Weight
- 54 KB
- Volume
- 27
- Category
- Article
- ISSN
- 1573-0875
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5-Aminolevulinate synthase (EC 2.3.1.37) is the first enzyme in the heme biosynthesis in nonplant eukaryotes and some prokaryotes. It functions as a homodimer and requires pyridoxal 5'-phosphate as an essential cofactor. Tyr-121 is a conserved residue in all known sequences of 5-aminolevulinate synt
To examine the role of 5-aminolevulinate synthase (ALAS) in the pathogenesis of sideroblastic anemias, levels of mRNAs for erythroid and housekeeping ALAS isozymes were examined, and total ALAS activity was assessed in bone marrow cells. In two patients with X-linked sideroblastic anemia the levels
The serum protein hemopexin is considered to have a major role in the mechanism of the uptake of heme by hepatocytes by means of a heme-hemopexin receptor. Therefore, we examined in primary cultures of adult rat and embryonic chick hepatocytes whether the presence of hemopexin would affect the heme-