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Curr Opin Struct Biol. 1994 Dec;4(6):810-3.

'Holy' proteins. II: The soluble lytic transglycosylase.

Author information

1
Laboratory of Biophysical Chemistry, University of Groningen, The Netherlands.

Abstract

Enzymes involved in the metabolism of the bacterial cell wall peptidoglycan are excellent targets for antibiotics. Penicillins and related beta-lactam antibiotics inhibit the enzymes that act on the peptide cross-links of the peptidoglycan. The X-ray structure of the transglycosylase revealed a two-layered ring of alpha-helices in a right-handed superhelical arrangement with a separate catalytic domain on top, which resembles the fold of goose-type lysozyme. Three sequence motifs were found that characterize the catalytic and substrate-binding sites in the enzyme. These motifs are present in a broad family of muramidases and chitinases.

PMID:
7712284
DOI:
10.1016/0959-440x(94)90261-5
[Indexed for MEDLINE]

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