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[Beta-lactamase and its molecular evolution].
Sawai T, Nukaga M, Haruta S. Sawai T, et al. Tanpakushitsu Kakusan Koso. 1995 Oct;40(13):1887-99. Tanpakushitsu Kakusan Koso. 1995. PMID: 8524994 Review. Japanese. No abstract available.
The effect of amino acid substitution at position 219 of Citrobacter freundii cephalosporinase on extension of its substrate spectrum.
Tsukamoto K, Ohno R, Nukaga M, Sawai T. Tsukamoto K, et al. Among authors: sawai t. Eur J Biochem. 1992 Aug 1;207(3):1123-7. doi: 10.1111/j.1432-1033.1992.tb17150.x. Eur J Biochem. 1992. PMID: 1499556 Free article.
The substitution of the glutamic acid at position 219 in the enzyme by lysine was previously shown to broaden its substrate specificity to unfavorable substrates such as oxyimino cephalosporins [Tsukamoto, K., Ohno, R. & Sawai, T. (1990) J. Bacteriol. 172, 4348- …
The substitution of the glutamic acid at position 219 in the enzyme by lysine was previously shown to broaden its substrate specificity to u …
Interaction of oxyimino beta-lactams with a class C beta-lactamase and a mutant with a spectrum extended to beta-lactams.
Nukaga M, Tsukamoto K, Yamaguchi H, Sawai T. Nukaga M, et al. Among authors: sawai t. Antimicrob Agents Chemother. 1994 Jun;38(6):1374-7. doi: 10.1128/AAC.38.6.1374. Antimicrob Agents Chemother. 1994. PMID: 8092840 Free PMC article.
The class C beta-lactamase of Citrobacter freundii GN346 is a typical cephalosporinase comprising 361 amino acids, and substitution of the glutamic acid at position 219 in the enzyme by lysine was previously shown to broaden its substrate spectrum to oxyimino beta-lactams (K. Tsu …
The class C beta-lactamase of Citrobacter freundii GN346 is a typical cephalosporinase comprising 361 amino acids, and substitution of the g …
1,068 results