5-Aminolevulinate synthase and the first step of heme biosynthesis. J Bioenerg Biomembr 1995 . 27: 151 – 159 .Ferreira GC, Gong J (1995) 5-Aminolevulinate syn- thase and the first step of heme biosynthesis. J Bioen- erg Biomembr 27:151-159....
5-Aminolevulinate synthase (ALAS), the first enzyme of the heme biosynthetic pathway in non-plant eukaryotes and some bacteria, catalyzes the condensation of glycine and succinyl- CoA . Rapid scanning stopped flow experiments of murine erythroid ALAS demonstrate that reaction with glycine plus ...
The gene for 5-aminolevulinate synthase (ALAS) has been mapped to 3pter-3q13.2 by Southern blot hybridization analysis of a mouse/human hybrid cell panel. In situ hybridization maps the gene to 3p21, distal to the common fragile site at 3p14.2 (FRA3B). The mapping of this gene to an...
建议收到该5-Aminolevulinate Synthase, Nonspecific, Mitochondrial (ALAS-H) Antibody产品后,储存温度为-20°C。避免重复冻融其他 Abbexa总部位于英国剑桥的剑桥科学园,是一家专业的全球抗体供应商和蛋白质供应商,致力于为生命科学、药物开发和生物技术领域的科学家和研究者提供最佳的客户体验和高质量的产品。产品涵盖...
Pyridoxal-5'-phosphate (PLP) is an obligatory cofactor for the homodimeric mitochondrial enzyme 5-aminolevulinate synthase (ALAS), which controls metabolic flux into the porphyrin biosynthetic pathway in animals, fungi, and the alpha-subclass of proteobacteria. Recent work has provided an explanation...
建议收到该5-Aminolevulinate Synthase, Erythroid-Specific, Mitochondrial (ALAS2) Antibody产品后,储存温度为-20°C。避免重复冻融其他 Abbexa总部位于英国剑桥的剑桥科学园,是一家专业的全球抗体供应商和蛋白质供应商,致力于为生命科学、药物开发和生物技术领域的科学家和研究者提供最佳的客户体验和高质量的产品。产...
However, while maintaining a wild type-like three-dimensional structure, active, circularly permuted 5-aminolevulinate synthase variants possess different topologies. To assess whether the aminolevulinate synthase overall structure can be reached through alternative or multiple folding pathways, we ...
The first enzyme in the pathway, 5-aminolevulinate synthase (ALA-synthase; also known asd-aminolevulinate synthase; E.C. 2.3.1.37), catalyzes the condensation of glycine (activated by pyridoxal phosphate) and succinyl coenzyme A to form ALA. Distinct human housekeeping and erythroid-specific ALA...
Regulation of 5-aminolevulinate synthase (ALAS) is at the origin of balanced heme production in mammals. Mutations in the C-terminal region of human erythroid-specific ALAS (hALAS2) are associated with X-linked protoporphyria (XLPP), a disease characterized by extreme photosensitivity, with elevat...
5-Aminolevulinate synthase (ALAS) catalyzes the initial step of mammalian heme biosynthesis, the condensation between glycine and succinyl-CoA to produce CoA, CO2, and 5-aminolevulinate. The crystal structure ofRhodobacter capsulatusALAS indicates that the adenosyl moiety of succinyl-CoA is positioned...