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- W2010073189 abstract "1. Adenylosuccinate lyase (S-AMP lyase) (E.C. 4.3.2.2) has been purified 10,000-fold from human erythrocyte lysates. 2. The enzyme catalyzes the conversion of S-AMP to AMP and fumarate, and the conversion of JV-(5-amino-l-ribosyl-4-imidazole carbonyl)-l-aspartic acid 5'-phosphate (S-AICA ribonucleotide) to 5-amino-l-ribosyl-4-imidazole carboxamide 5'-phosphate (AICA ribonucleotide) and fumarate. 3. The apparent Kms for S-AMP and S-AICA ribonucleotide were 2.3 μM and 3.5 μM respectively, in tricine buffer (pH 7.8). 4. AMP, AICA ribonucleotide and6-N succinoadenine were strong competitive inhibitors, fumarate was a comparatively weak non-competitive inhibitor, and orthophosphate was a weak competitive inhibitor." @default.
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- W2010073189 date "1975-07-01" @default.
- W2010073189 modified "2023-09-25" @default.
- W2010073189 title "Adenylosuccinate lyase from human erythrocytes" @default.
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- W2010073189 doi "https://doi.org/10.1016/0020-711x(75)90030-0" @default.
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