Mitochondrial uptake and processing of ALAS2

Stable Identifier
R-GGA-421457
Type
Reaction [uncertain]
Species
Gallus gallus
Compartment
ReviewStatus
5/5
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Comparison of ALAS2 protein translated in vitro with that recovered from mitochondria has shown that in the course of becoming localized to the mitochondrion, the nascent ALAS2 polypeptide is shortened (Watanabe et al. 1983), though the annotated loss of 18 aminoterminal residues is an inference from analysis of the predicted ALAS2 amino acid sequence. By analogy to a bacterial ALAS protein whose three-dimensional structure is known (Astner et al. 2005), the active form of chicken ALAS2 is inferred to be a complex of two ALAS1 protein molecules, each bound to a molecule of pyridoxal phosphate. The order of proteolytic processing, cofactor binding, and protein-protein binding to form the active enzyme complex is unknown.
Literature References
PubMed ID Title Journal Year
6870861 delta-Aminolevulinate synthase isozymes in the liver and erythroid cells of chicken

Kikuchi, G, Hayashi, N, Watanabe, N

Biochem Biophys Res Commun 1983
16121195 Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans

Heinz, DW, Jahn, D, Schubert, WD, van den Heuvel, J, Schulze, JO, Astner, I

EMBO J 2005
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