Lysozyme phage

Myoglobin, hemoglobin Thermolysin domain 2 T4 phage lysozyme domain 2 Papain domain 1... 

Tyrosyl-tRNA synthetase dl, d2 Thermolysin dl, d2 T4 phage lysozyme dl, d2 Glucosephosphate isomerase dl, d2 Pyruvate kinase dl, d2 Pyruvate kinase d2, d3 Lactate dehydrogenase dl, d2 Alcohol dehydrogenase dl, d2 Glyceraldehyde-phosphate dehydrogenase dl,d2... 

Phage Lysozymes and Other Lytic Enzymes Akira Tsugita... 

Weaver, L.H. T.M. Gray, M.G. Gruetter, D.E. Anderson, J.A. Wozniak, F.W. Dahlquist, B.W. Matthews, (1989) High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96 -> His. 

Matthews, B. W. (1975). Comparison of the predicted and observed secondary structure of T4 phage lysozyme. Biochim Biophys Acta 405,442-51. 

B. W. Matthews, Biochim. Biophys. Acta, 405, 442 (1975). Comparison of Predicted and Observed Secondary Structure of T4 Phage Lysozyme. 

Lysozymes derived from sources other than bird egg-whites were also tested for their susceptibility to inactivation by the epoxypropyl /8-gly-cosides. Among these, human leukemic urine lysozyme was inactivated by (GlcNAc)3-Ep at pH 5.5, whereas the lysozymes from papaya latex and the bacteriophage T4 were not inactivated at all. Similar results were also obtained at pH 4.6, at which the papaya lysozyme acts on chitin most efficiently. These results show that the active sites of human and the hen lysozymes are similar, whereas the active sites of the T4 phage and the papaya lysozymes differ from them. Indeed, the hen and the human lysozymes are similar in their amino acid sequences" and three-dimensional structures, whereas the papaya and the T4 phage lysozymes differ from the hen egg-w hite lysozyme in their amino acid composition, molecular weight, and substrate specificity."" ... 

Singla et al. [19] examined the adsorption kinetics of wild type and two synthetic stability mutants of T4 phage lysozyme at silanized silica surfaces. Substitution of the isoleucine at amino acid position three with cysteine (13 C) and tryptophan (13W) rendered such mutants with a higher and lower thermal stability, respectively. It was found that the I3W mutant, characterized by a lower structural stability, would more readily undergo a stmctural change at the interface. Moreover, such a mutant showed more resistance to elution by DTAB than either the wild type or 13 C mutant, simply by forming a more tightly bound conformation (adsorbed state) with the adsorbent. 

T7 lysozyme T7 phage lysozyme, a zinc amidase (118 amino acids) which cuts the amide bond between N-acetylmuramic acid (MurNAc) and L-Ala rather than the glycosidic bond between MurNAc and N-acetylglucosamine (GlcNAc),... 

The above properties have enabled us to investigate the biochemical properties of the two forms of the lipoprotein and their quantitative relationship. Figure 8 shows a gel pattern of the E. coli envelope proteins after T4 phage lysozyme treatment. The only change caused by the treatment is the appearance of a new peak at the arrow in Fig. 8. Without lysozyme treatment, no such peak appears, as shown in Figs. 2 and 4. All murami-dases tested so far (hen egg-white lysozyme, goose egg-white lysozyme, and T4 phage lysozyme) cause the same peak to appear. ... 

Fig. 8. Gel electrophoresis of an envelope protein fraction double labeled with pHJarginine and [ CJhistidihe. The envelope fraction was treated with T4 phage lysozyme before electrophoresis.

Fig. 10. Pulse-chase experiment of the envelope fraction. (A) A culture was pulse labeled for 4 min with [ C]arginine. Another culture was pulse labeled for 4 min with PH]arginine and chased with nonradioactive arginine for another 50 min. The envelope fraction was prepared from the mixture of both cultures, digested with T4 phage lysozyme, and subjected to SDS gel electrophoresis on a 7.5% acrylamide gel. (B) The radioisotopes were used in the reverse way...

Fig. 11. Gel electrophoresis of the envelope fractions of an E. coli histidine auxotroph ( . coli CP78) labeled with [ C]arginine in the presence and absence of histidine. (A) Labeled in the presence of histidine for 1 h. (B) Labeled during a 1-h histidine starvation. (C) Labeled for 2 h after 2 h of histidine starvation. The patterns of the envelope fractions with and without the lysozyme treatment were superimposed with the aid of the internal standards. Envelope fractions treated with T4 phage lysozyme ------- without T4 phage treatment . In the case of...

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