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Preferential hydrolysis of cis configuration compounds at the 3,4 position of monobactams by beta-lactamase from Morganella morganii.

Authors
  • Matsuda, K
  • Sanada, M
  • Nakagawa, S
  • Inoue, M
  • Mitsuhashi, S
Type
Published Article
Journal
Antimicrobial agents and chemotherapy
Publication Date
Mar 01, 1991
Volume
35
Issue
3
Pages
458–461
Identifiers
PMID: 2039196
Source
Medline
License
Unknown

Abstract

Carumonam and BO-1166 (cis configuration) were inactivated by beta-lactamase of Morganella morganii more rapidly than were aztreonam and BO-1165 (trans configuration), as demonstrated by spectrophotometric analysis and microbiological assay. An active enzyme was recovered more rapidly from the inactivated enzyme-monobactam complex derived from the cis form of monobactams than from the complex derived from the trans form of monobactams. This result suggests that the configuration at the 3,4 position on the azetidinone ring of monobactams, together with the chemical structure of the side chains attached to the azetidinone ring, may play an important role in the stability of monobactams to the beta-lactamase of M. morganii.

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