PMID:11139297
| Citation |
Blackburn, NT and Clarke, AJ (2001) Identification of four families of peptidoglycan lytic transglycosylases. J. Mol. Evol. 52:78-84 |
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| Abstract |
The lytic transglycosylases are a class of autolysins which cleave the bacterial cell wall heteropolymer peptidoglycan (murein) to facilitate its biosynthesis and turnover. A search of the National Center for Biotechnology Information (NCBI) databases using the primary sequences of the six characterized lytic transglycosylases of Escherichia coli, a membrane-bound form of the enzyme from Pseudomonas aeruginosa, and the endolysins of lambda bacteriophage permitted the identification of a total of 127 known and hypothetical enzymes from a wide variety of bacteria and bacteriophage. These amino acid sequences have been arranged into four families based on alignments, and consensus motifs have been identified. Family 1 represents a superfamily comprising 86 sequences which are subdivided into five (1A--1E) subfamilies. |
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| Keywords |
Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacteriophage lambda/enzymology; Bacteriophage lambda/genetics; Databases, Factual; Endopeptidases/chemistry; Endopeptidases/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Evolution, Molecular; Glycosyltransferases/chemistry; Glycosyltransferases/classification; Glycosyltransferases/genetics; Hexosyltransferases/chemistry; Hexosyltransferases/classification; Hexosyltransferases/genetics; Molecular Sequence Data; Molecular Structure; Multigene Family; Phylogeny; Pseudomonas aeruginosa/enzymology; Pseudomonas aeruginosa/genetics |
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