Matsumura N, Mitsuhashi S
Episome Institute, Gunma, Japan.
Antimicrob Agents Chemother. 1995 Sep;39(9):2132-4. doi: 10.1128/AAC.39.9.2132.
A beta-lactamase was purified from Serratia marcescens GN16694; it hydrolyzed T-5575 and oxime-type cephalosporins, i.e., cefuroxime and ceftazidime. Its isoelectric point and molecular weight were 8.6 and 42,000, respectively. This enzyme was not inhibited by EDTA and clavulanic acid. This enzyme is an unusual beta-lactamase and has been classified as a group 1 cephalosporinase.
从粘质沙雷氏菌GN16694中纯化出一种β-内酰胺酶;它能水解T-5575和肟型头孢菌素,即头孢呋辛和头孢他啶。其等电点和分子量分别为8.6和42,000。该酶不受EDTA和克拉维酸的抑制。这种酶是一种不寻常的β-内酰胺酶,已被归类为1组头孢菌素酶。