title: Adenylate kinase of Mycobacterium marinum. Amino acid composition, secondary structure and other aspects.
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.
authors.affiliation: Department of Biochemistry, Wright State University, Dayton, OH 45435.
authors.forename: P P
authors.initials: PP
authors.lastname: Batra
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: K
authors.initials: K
authors.lastname: Takeda
mesh_terms: D000263:Adenylate Kinase / Q000032:analysis* / Q000037:antagonists & inhibitors; D000596:Amino Acids / Q000032:analysis*; D002942:Circular Dichroism; D015226:Dinucleoside Phosphates / Q000494:pharmacology; D009161:Mycobacterium / Q000201:enzymology*; D010770:Phosphotransferases / Q000032:analysis*; D011487:Protein Conformation
chemical_list: D000596:Amino Acids; D015226:Dinucleoside Phosphates; C012275:P(1),P(5)-di(adenosine-5'-)pentaphosphate; D010770:Phosphotransferases; D000263:Adenylate Kinase