Properties of adenosine deaminase in extracts of Asperigillus terricola.
Article Details
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Abu-Shady MR, Elshafei AM, el-Beih FM, Mohamed LA
Properties of adenosine deaminase in extracts of Asperigillus terricola.
Acta Microbiol Pol. 1994;43(3-4):305-11.
- PubMed ID
- 7740980 [ View in PubMed]
- Abstract
Cell-free extracts of nitrate-grown Aspergillus terricola catalyze the hydrolytic deamination of adenosine to inosine at maximum rate at pH 6.5 and 50 degrees C. Incubation of the extracts at 60 degrees C for 30 minutes caused about 66.7% loss in activity. Results indicated the involvement of SH groups in the catalytic site of adenosine deaminase. Frequent freezing and thawing of the enzyme preparation for three days (3 times) resulted in about 47% loss in activity. The enzyme is also inhibited by EDTA indicating that adenosine deaminase is a metaloenzyme. MgCl2 and CoSO4 had a remarkable activating effect, whereas MnCl2 showed a slight inhibitory effect on enzyme activity. The apparent Km value was calculated for adenosine and found to be 6.66 x 10(-3) M, which indicates the greater affinity of adenosine deaminase for adenosine.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Edetate calcium disodium anhydrous Adenosine deaminase Protein Humans UnknownInhibitorDetails Edetate disodium anhydrous Adenosine deaminase Protein Humans UnknownInhibitorDetails Edetic acid Adenosine deaminase Protein Humans UnknownInhibitorDetails