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Adenylate kinase of Mycobacterium marinum. Amino acid composition, secondary structure and other aspects
P P Batra1, K Yamamoto, K Takeda
1Department of Biochemistry, Wright State University, Dayton, OH 45435.
The International Journal of Biochemistry
|January 1, 1989
Abstract:
1. Adenylate kinase purified from Mycobacterium marinum shares homology with the enzyme from mammalian muscle and from other bacteria with respect to amino acid composition, total residues and Mr. 2. However, it differs from others in not containing a free sulfhydryl or disulfide group. 3. It is much more sensitive to inhibition by adenosine (5')pentaphospho(5')adenosine than is the enzyme from other sources. 4. The enzyme contains 24% alpha-helix, 30% beta-structure and 46% random coil.