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The structural peptidoglycan hydrolase gp181 of bacteriophage φKZ
Biochemical and Biophysical Research Communications, 2008Gp181 (2237 amino acids) of Pseudomonas aeruginosa bacteriophage phiKZ (Myoviridae) is a structural virion protein, which bears a peptidoglycan hydrolase domain near its C-terminus. This protein is supposed to degrade the peptidoglycan locally during the infection process.
Alexei Nekrasov +2 more
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Biochemical analysis of NlpC/p60 peptidoglycan hydrolase activity
Methods in Enzymology, 2020The NlpC/p60-family of peptidoglycan hydrolases are key enzymes that facilitate bacterial cell division and also modulate microbe-host interactions. These endopeptidases utilize conserved Cys-His residues in their active site and are expressed in most bacterial species as well as some eukaryotes.
Byung Chul Kim +2 more
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Regulation of peptidoglycan hydrolases: localization, abundance, and activity
Current Opinion in Microbiology, 2023Most bacteria are surrounded by a cell wall composed of peptidoglycan (PG) that specifies shape and protects the cell from osmotic rupture. Growth, division, and morphogenesis are intimately linked to the synthesis of this exoskeleton but also its hydrolysis. The enzymes that cleave the PG meshwork require careful control to prevent aberrant hydrolysis
Anna P, Brogan, David Z, Rudner
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Detection and Localization of a Peptidoglycan Hydrolase in Lactobacillus delbrueckiisubsp. bulgaricus [PDF]
Journal of Dairy Science, 2003 Peptidoglycan hydrolase activities in Lactobacillus delbrueckii subsp. bulgaricus were detected by analysis of bacterial extracts on denaturing polyacrylamide gel electrophoresis containing lyophilized Micrococcus lysodeikticus cells as substrate. A hydrolase with an estimated molecular mass of 80 kDa was found to cross-react on Western blot with ...
R E Simard, R E Simard
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Peptidoglycan hydrolases, bacterial shape, and pathogenesis
Current Opinion in Microbiology, 2013Bacterial shape has always been hypothesized to play an important role in the biology of a species and in the ability of certain bacteria to influence human health. The recent discovery of peptidoglycan hydrolases that modulate shape has now allowed this hypothesis to be addressed directly.
Emilisa, Frirdich, Erin C, Gaynor
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The autolytic peptidoglycan hydrolases of Streptococcus faecium
Annales de l'Institut Pasteur / Microbiologie, 1985Streptococcus faecium ATCC 9790 possesses two peptidoglycan hydrolase activities. The first enzyme, an N-acetylmuramoylhydrolase, has been purified and has been shown to be a glucoenzyme. Studies of hydrolysis of soluble, linear uncross-linked peptidoglycan chains showed that the enzyme bound strongly to the non-reducing ends of the chains and then ...
G D, Shockman +3 more
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Bacterial Walls, Peptidoglycan Hydrolases, Autolysins, and Autolysis
Microbial Drug Resistance, 1996ABSTRACT Knowledge of the chemistry, ultrastructure, biosynthesis, assembly, and function of bacterial cell walls has expanded enormously since the opening of this field of research approximately 40 years ago, primarily by the early work of Milton Salton.
SHOCKMAN G. D. +3 more
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Carbohydrate recognition and lysis by bacterial peptidoglycan hydrolases
Current Opinion in Structural Biology, 2017The major component of bacterial cell wall is peptidoglycan (PG), a complex polymer formed by long glycan chains cross-linked by peptide stems. PG is in constant equilibrium requiring well-orchestrated coordination between synthesis and degradation. The resulting cell-wall fragments can be recycled, act as messengers for bacterial communication, as ...
Alcorlo, Martín +3 more
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Measure of Peptidoglycan Hydrolase Activity
2017Most gene clusters encoding multiprotein complexes of the bacterial cell envelope, such as conjugation and secretion systems, Type IV pili, and flagella, bear a gene encoding an enzyme with peptidoglycan hydrolase activity. These enzymes are usually glycoside hydrolases that cleave the glycan chains of the peptidoglycan.
Yoann G, Santin, Eric, Cascales
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Crystal structure of the glycosidase family 73 peptidoglycan hydrolase FlgJ
Biochemical and Biophysical Research Communications, 2009Glycoside hydrolase (GH) categorized into family 73 plays an important role in degrading bacterial cell wall peptidoglycan. The flagellar protein FlgJ contains N- and C-terminal domains responsible for flagellar rod assembly and peptidoglycan hydrolysis, respectively. A member of family GH-73, the C-terminal domain (SPH1045-C) of FlgJ from Sphingomonas
Wataru Hashimoto +2 more
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