Adenosine deaminase in the marine mussel, Mytilus edulis: Purification, characterization and inhibition by a substrate analog, coformycin (cas 11033-22-0)

Add time:08/21/2019    Source:sciencedirect.com

1.1. The purified mussel adenosine deaminase (mol. wt: 140,000) was stable in the pH range of 4.0–6.0 at 17°C. The optimum pH was 6.0 for adenosine and 6.5 for deoxyadenosine.2.2. Adenine, 2′- and 5′-AMP, 5′-ADP and 5′-ATP were not deaminated.3.3. The α (Vmax/Km) and β (Vmax) parameters changed with temperature and pH, respectively. RSS (relative substrate specificity) values with deoxyadenosine were 0.88 for α and 1 for β.4.4. PCMB and MgCl2 were competitive inhibitors.5.5. The enzyme was strongly inhibited when preincubated with coformycin and the Ki was 2 gmM. The association and dissociation rate constants for the EI complex were 1.22 × 103 M−1 sec−1 and 2.44 × 10−3 sec−1, respectively. The half time (t12) of EI dissociation was 284 sec.

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