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7776128 
Journal Article 
Streptomycin biosynthesis. Enzymatic synthesis of O-phosphorylstreptidine from streptidine and adenosinetriphosphate 
Walker, JB; Walker, MS 
1967 
1 
Biochimica et Biophysica Acta
ISSN: 0006-3002
EISSN: 1878-2434 
148 
2 
335-341 
English 
6075410 
1. 1. An enzyme has been found in dialyzed extracts of streptomycin-producing strains of Streptomyces which catalyzes the formation of an O-phosphorylstreptidine from streptidine and ATP. Although streptidine kinase activity was detected in vivo in many Streptomyces strains, activity in cell-free preparations could be detected only in extracts from mature mycelia of streptomycin-producing strains; extracts from log-phase mycelia were inactive. 2. 2. A partially purified enzyme preparation phosphorylates streptidine and 2-deoxystreptidine, but not N-amidinostreptamine, N′-amidinostreptamine, or N-amidinoinosamines. The closely-related N-amidinostreptamine kinase from streptomycin producers is inhibited by the sulfhydryl reagents formamidine disulfide and p-chloromercuribenzoate, but streptidine kinase is not. Streptidine kinase activity is inhibited by streptomycin. 3. 3. The ATP requirement can be met by dATP, but not by GTP, CTP, UTP, or dTTP; Mn2+ can replace Mg2+. 4. 4. A sensitive radiochemical assay for the streptidine in biological materials can be devised by coupling streptidine kinase with amidinotransferase. 5. 5. A scheme is presented which summarizes current concepts of streptidine metabolism. 1967.