type	Journal Article
authors	Ferreira, G. C.; Cheltsov, A. V.
title	Circular permutation of 5-aminolevulinate synthase as a tool to evaluate folding, structure and function
journal	Cell Mol Biol (Noisy-le-grand)
Activity	2.3.1.37
ui	21925949
year	(2002)
volume	48
number	1
pages	11-6.
abstract	5-Aminolevulinate synthase, a pyridoxal 5'-phosphate-dependent enzyme, catalyzes the condensation of glycine with succinyl-coenzyme A to yield aminolevulinate, carbon dioxide and CoA. This reaction corresponds to the first and regulatory step of the mammalian heme biosynthetic pathway. Mutations in the erythroid aminolevulinate synthase gene are associated with X-linked sideroblastic anemia, an erythropoietic disorder characterized by the presence of hypochromic-microcytic erythrocytes in peripheral blood and ring sideroblasts in bone marrow. In the past five years, transient kinetic studies in conjunction with three-dimensional structure models and engineered variants of aminolevulinate synthase have been instrumental in understanding the individual steps of the catalytic mechanism of aminolevulinate synthase. The mechanism of folding, assembly of the two subunits into a functional, dimeric holoenzyme has been recently explored in this laboratory using circular permutation of aminolevulinate synthase.
last changed	2002/11/04 17:41