Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mitomycin C induced a pyocinogenic Pseudomonas aeruginosa P15 to produce a bacteriolytic enzyme, PR1-lysozyme, together with pyocin R1. No significant accumulation of the enzyme was observed inside the induced cells. The enzyme was partially purified by acrinol treatment and Amberlie CG-50 column chromatography. The mode of action of the enzyme on the host bacterial cells as well as on Micrococcus lysodeikticus cells or peptidoglycan isolated from Salmonella typhimurium, was compared with that of hen egg-white lysozyme or phage lambda-lysozyme. It is suggested that PR1-lysozyme should be classified as a glycosidase, rather than an amidase or an endopeptidase.
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PMID:Induction of bacteriolytic enzyme from pyocinogenic Pseudomonas aeruginosa and its enzymatic properties. 11 82

A bacteriolytic enzyme was found to be produced, concomitantly with the progeny phage, in Pseudomonas aeruginosa P14 infected with phage PS17. The enzyme, named PS17-lysozyme, was purified by acrinol treatment, two cycles of Amberlite CG-50 chromatography, and SP-Sephadex C-50 chromatography. Homogeneity of the preparation was demonstrated by three electrophoretic techniques. PS17-lysozyme behaved like a basic protein (pI, 9-10) consisting of a single polypeptide chain (molecular weight, 24,500) and showed the substrate specificity as hen egg-white lysozyme. The enzyme exhibited much higher specific activity than the egg-white enzyme when assayed with chloroform-killed P. aeruginosa P14 as a substrate. These characteristics, as well as the amino acid composition, were very similar to those of PR1-lysozyme; a bacteriolytic enzyme produced in mitomycin C-induced P. aeruginosa P15 concomitantly with a phage-tail-like bacteriocin, pyocin R1 (Ochi et al. (1978) J. Biochem. 83, 727-736). However, the behavior of these two lysozymes from P. aeruginosa in Amberlite CG-50 chromatography and some other properties indicated that they were not identical, though they were similar. The results are in accord with the view that pyocin R1 may be a defective form of a bacteriophage closely related to but not identical with phage PS17.
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PMID:Lytic enzyme produced by Pseudomonas aeruginosa concomitantly with bacteriophage PS17. Purification, characterization, and comparison with PR1-lysozyme. 678 37

Bacteriophage PRD1 is a lipid-containing virus that infects a variety of Gram-negative bacteria, including Escherichia coli. The phage lyses its host by virtue of a virally-encoded lytic enzyme, the synthesis of which has been assigned to gene XV on the basis of complementation analysis and experiments with mutant phages. We report here the cloning of gene XV into an expression plasmid and the purification of its product, protein P15, to near homogeneity. The purified protein P15, identified by N-terminal sequence analysis, showed a strong lytic activity against chloroform-treated Gram-negative cells. No activity against Gram-positive bacterial species could be detected. The pH optimum of the enzyme was between 7.0-8.0. Protein P15 was readily inactivated at temperatures above 4 degrees C, as well as by increasing the ionic strength of the buffers. The analysis of cell wall digests indicated that P15 is a glycosidase that cleaves the beta (1-4) linkage between N-acetylmuramic acid and N-acetylglucosamine, thus displaying muramidase activity.
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PMID:Gene XV of bacteriophage PRD1 encodes a lytic enzyme with muramidase activity. 792 54

Bacteriophage PRD1 encodes two proteins (P7 and P15) that are associated with a muralytic activity. Protein P15 is a soluble beta-1,4-N-acetylmuramidase that causes phage-induced host cell lysis. We demonstrate here that P15 is also a structural component of the PRD1 virion and that it is connected to the phage membrane. Small viral membrane proteins P20 and P22 modulate incorporation of P15 into the virion and may connect it to the phage membrane. The principal muralytic protein involved in PRD1 DNA entry seems to be the putative lytic transglycosylase protein P7, as the absence of protein P15 did not delay initiation of phage DNA replication in the virus-host system used. The incorporation of two different lytic enzymes into virions may reflect the broad host range of bacteriophage PRD1.
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PMID:The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane. 1174 49