Simultaneous release of penicilloic acid and phenylacetyl glycine by penicillin-binding proteins 5 and 6 of Escherichia coli.
نویسندگان
چکیده
Penicillin-binding proteins (PBPs) 5 and 6 of Escherichia coli released the bound penicilloyl moiety at an intermediate rate relative to, e.g., Staphylococcus aureus PBPs 4 (rapid) and 1 or 2 (slow). Each of these E. coli PBPs released the bound penicilloyl moiety as both penicilloic acid (hydrolysis) and phenylacetyl glycine (scission of the C-5--C-6 bond followed by hydrolysis).
منابع مشابه
Enzymatic Deacylation of S35-benzylpenicillin.
Pruess, David L. (University of Wisconsin, Madison), and Marvin J. Johnson. Enzymatic deacylation of S(35)-benzylpenicillin. J. Bacteriol. 90:380-383. 1965.-S(35)-benzylpenicillin, penicilloic acid, and penilloic acid were deacylated by cell suspensions of Escherichia coli and Micrococcus roseus. Both cultures deacylated penicillin most rapidly and penilloic acid least rapidly. The deacylase ac...
متن کاملBinding of (14C)penicillin G to the membrane-bound and the purified D-alanine carboxypeptidases from Bacillus stearothermophilus and Bacillus subtilis and its release.
[%]Penicillin G bound to the Bacillus subtilis and Bacillus stearothermophilus D-ala&e carboxypeptidases in either the membrane-bound or purified states. ‘Ihis binding was subsequently reversed with a half-time ranging from 10 min to several days, depending on the enzyme, the penicillin derivative, and the temperature. The released material was neither intact penicillin nor penicilloic acid but...
متن کاملEngineered single- and multi-cell chemotaxis pathways in E. coli
We have engineered the chemotaxis system of Escherichia coli to respond to molecules that are not attractants for wild-type cells. The system depends on an artificially introduced enzymatic activity that converts the target molecule into a ligand for an E. coli chemoreceptor, thereby enabling the cells to respond to the new attractant. Two systems were designed, and both showed robust chemotact...
متن کاملMutation in Pseudomonas aeruginosa causing simultaneous defects in penicillin-binding protein 5 and in enzyme activities of penicillin release and D-alanine carboxypeptidase.
Penicillin-binding protein 5 in Pseudomonas aeruginosa had moderately penicillin-sensitive D-alanine carboxypeptidase activity. As in Escherichia coli, a defect in this enzyme activity was not lethal.
متن کاملBinding of thienamycin and clavulanic acid to the penicillin-binding proteins of Escherichia coli K-12.
Thienamycin and clavulanic acid are new beta-lactam derivatives with structures markedly different from those of penicillins or cephalosporins. Both derivatives had the same general mode of action as typical beta-lactam antibiotics since they bound to precisely the same proteins as [(14)C]benzylpenicillin. Thienamycin showed high affinity for penicillin-binding proteins 1, 2, 4, 5, and 6 and a ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 160 2 شماره
صفحات -
تاریخ انتشار 1984