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Adenylosuccinate lyase C-terminal
This domain is found at the C-terminus of adenylosuccinate lyase(ASL; PurB in E. coli). It has been identified in bacteria, eukaryotes and archaea and is found together with the lyase domain Pfam:PF00206. ASL catalyses the cleavage of succinylaminoimidazole carboxamide ribotide to aminoimidazole carboxamide ribotide and fumarate and the cleavage of adenylosuccinate to adenylate and fumarate [1]. [1]. 8530047. Characterization of the cDNA and the gene encoding murine adenylosuccinate lyase. Wong LJ, O'Brien WE;. Genomics 1995;28:341-343. (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.
adenylosuccinate lyase
adenylosuccinate lyase catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate
This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP.
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