期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1988
卷号：85
期号：8
页码：2563-2567
DOI：10.1073/pnas.85.8.2563
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Escherichia coli optA1, a mutant unable to support the growth of T7 phage containing mutations in gene 1.2, contains reduced amounts of dGTP. Extracts of E. coli optA1 catalyze the hydrolysis of dGTP at a rate 50-fold greater than do extracts of E. coli optA+. The dGTPase responsible for the increased hydrolysis has been purified to apparent homogeneity. Purification of the protein is facilitated by its high affinity for single-stranded DNA. By using this purification scheme an identical dGTPase has been purified from E. coli optA+. The purified proteins catalyze the hydrolysis of dGTP to yield deoxyguanosine and tripolyphosphate. The products of hydrolysis, chromatographic properties, denatured molecular mass of 56 kDa, N-terminal amino acid sequence, substrate specificity, and heat inactivation indicate that the proteins purified from optA1 and from optA+ cells are identical and identify the enzyme as the deoxyguanosine 5'-triphosphate triphosphohydrolase purified to homogeneity from wild-type E. coli [Seto, D., Bhatnagar, S. K. & Bessman, M. J. (1988) J. Biol. Chem. 263, 1494-1499]. OptA1 cells contain approximately equal to 50-fold more active molecules of the 56-kDa dGTPase than do E. coli optA+ cells.
