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Argininosuccinate lyase C-terminal
This domain is found at the C-terminus of argininosuccinate lyase [1-2]. [1]. 11698398. Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase. Sampaleanu LM, Yu B, Howell PL;. J Biol Chem. 2002;277:4166-4175. [2]. 9256435. Human argininosuccinate lyase: a structural basis for intragenic complementation. Turner MA, Simpson A, McInnes RR, Howell PL;. Proc Natl Acad Sci U S A. 1997;94:9063-9068. (from Pfam)
lyase family protein
Members of this family include fumarate hydratase, L-aspartate ammonia-lyase, argininosuccinate lyase, and adenylosuccinate lyase. All are classified as lyases, meaning these enzymes break a bond by an eliminating reaction that does not involve hydrolysis or oxidation.
argininosuccinate lyase
argininosuccinate lyase catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis
Catalyzes the formation of arginine from (N-L-arginino)succinate and the formation of N-acetylglutamate from glutamate and acetyl-CoA
This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens.
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