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   <subfield code="a">Characterization of a recombinant (+)-γ-lactamase from Microbacterium hydrocarbonoxydans which provides evidence that two enantiocomplementary γ-lactamases are in the strain</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Jianjun Wang, Yaxin Zhu, Guogang Zhao, Junge Zhu, Sheng Wu]</subfield>
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   <subfield code="a">A two-step method, i.e., the transfer acyl analysis and then the chiral HPLC analysis, was employed in the screening of the cosmid library of Microbacterium hydrocarbonoxydans genome. Two enantiocomplementary γ-lactamase clones were found. A 40-kb cosmid showed (−)-γ-lactamase activity, and the activity was from Mhg which was reported previously according to the results of PCR identifying experiment. The 37-kb (+)-γ-lactamase cosmid was further constructed into a pUC18 plasmid library and screened by the same two-step method. A plasmid clone harboring a 1.6-kb fragment showed (+)-γ-lactamase activity. A 555-bp ORF in the 1.6-kb fragment showed high (+)-γ-lactamase activity when it was expressed under the control of T7 promoter. The coding protein showed significant homology with bacterial isochorismatase. The (+)-γ-lactamase was characterized and compared with the (−)-γ-lactamase Mhg. This is another report that two enantiocomplementary γ-lactamases are present in the same strain.</subfield>
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