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)

High molecular genomic DNAs were isolated by using the lysozyme plus achromopeptidase system from Frankia strains At4, Ccol and Hr16, the root nodule endophytes of Alnus, Casuarina and Hippophae respectively, and used to construct genomic libraries in pLAFR1, a broad host range cosmid vector within many gram-negative hosts. The genomic libraries were screened by in situ colony hybridization to identify clones homologous to common nodulation genes of Rhizobium leguminosarum, based on the sequence homology of EcoRI-digested Frankia total DNA to nodABC from Rhizobium meliloti. Several clones showing relatively strong hybridization were found, the recombinant plasmid was isolated, and their homology with Rhizobium nodulation genes was confirmed by spot hybridization. Further work on these positive clones is now underway.
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PMID:[Construction of Frankia genomic libraries and isolation of clones homologous to nodulation genes from Rhizobium leguminosarum]. 226 50

The lysozyme (rabbit kidney lysozyme) from the homogenate of rabbit kidney (Japanese white) was purified by repeated cation-exchange chromatography on Bio-Rex 70. The amino acid sequence was determined by automated gas-phase Edman degradation of the peptides obtained from the digestion of reduced and S-carboxymethylated rabbit lysozyme with Achromobacter protease I (lysyl endopeptidase). The sequence thus determined was KIYERCELARTLKKLGLDGYKGVSLANWMCLAKWESSYNTRATNYNPGDKSTDYGIFQ INSRYWCNDGKTPRAVNACHIPCSDLLKDDITQAVACAKRVVSDPQGIRAWVAWRNHCQ NQDLTPYIRGCGV, indicating 25 amino acid substitutions from human lysozyme. The lytic activity of rabbit lysozyme against Micrococcus lysodeikticus at pH 7, ionic strength of 0.1, and 30 degrees C was found to be 190 and 60% of those of hen and human lysozymes, respectively. The lytic activity-pH profile of rabbit lysozyme was slightly different from those of hen and human lysozymes. While hen and human lysozymes had wide optimum activities at around pH 5.5-8.5, the optimum activity of rabbit lysozyme was at around pH 5.5-7.0. The high proline content (five residues per molecule compared with two prolines per molecule in hen or human lysozyme) is one of the interesting features of rabbit lysozyme. The transition temperatures for the unfolding of rabbit, human, and hen lysozymes in 3 M guanidine hydrochloride at pH 5.5 were 51.2, 45.5, and 45.4 degrees C, respectively, indicating that rabbit lysozyme is stabler than the other two lysozymes. The high proline content may be responsible for the increased stability of rabbit lysozyme.
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PMID:Purification, amino acid sequence, and some properties of rabbit kidney lysozyme. 236 54

DNA could not be quickly extracted from members of the genus Actinomyces by the usual methods of lysis. Treatment of 7 different actinomyces cells with lysozyme and achromopeptidase, both 5 mg/g wet cells, for 2 h, followed by SDS (0.2%), proteinase K (5 mg/g wet cells) and EDTA (lmM) for 1 h, lysed the cells. The yield obtained in one day was 337 micrograms per 200 mg of bacterial cells. The treatment was also found to work effectively on strains belonging to Veillonella, Staphylococcus, Fusobacterium and Bifidobacterium genera.
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PMID:Rapid isolation of DNA from Actinomyces. 312 48

A rapid and simple method for preparation of chromosomal DNA from Gram-positive bacteria is reported. Susceptibility to lysis with Sodium Dodecyl Sulfate (SDS) increases when undergoing treatment with acetone before being digested by bacteriolytic enzymes. Rapid lysis of Staphylococcus and Listeria cells is obtained through a respective treatment by lysozyme with lysostaphine and by lysozyme with achromopeptidase, adding to that the effect of SDS in Tris-Hcl buffer. This procedure of preparing chromosomal DNA provides 1 to 4 mg of DNA out of 1 g of bacterial cells in a day.
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PMID:[Extraction of chromosomal DNA from Staphylococcus and Listeria by a rapid method using achromopeptidase]. 315 Jun 53

A second extracellular protease from myxobacter strain AL-1 has been purified to homogeneity and named protease II; the enzyme crystallizes as fine needles. The extracellular, cell wall lytic protease reported previously from the same organism is now designated protease I. Protease II exhibits a pH optimum of 8.5 to 9.0 and is stable from pH 3.0 to 9.0. The enzyme is heat stable at 50 C for 18 hr. Results of sedimentation equilibrium studies yielded a molecular weight of 17,000, and amino acid analysis revealed 157 residues with a minimal molecular weight of 16,660. Cleavage of peptide bonds in the oxidized B-chain of insulin, cytochrome c (horse heart). lysozyme, and vasopressin is restricted to the amino side of lysine. Dilysine and trilysine were not hydrolyzed. Products from digestions of polylysine were lysine and dilysine.
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PMID:Myxobacter AL-1 protease II: specific peptide bond cleavage on the amino side of lysine. 434 25

Achromopeptidase, which has potent bacteriolytic activity for most of the gram-positive aerobic bacteria, was for the first time used for the lysis of anaerobic cocci. Most of the lysozyme-resistant gram-positive anaerobic cocci were lysed with this new enzyme. Peptococcus magnus was the only organism tested resistant to achromopeptidase. P. saccharolyticus was quite unusual because it was very sensitive to both achromopeptidase and lysozyme.
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PMID:Achromopeptidase for lysis of anaerobic gram-positive cocci. 675 29

Recently, it has become more important to establish rapid and reliable methods for identifying bacterial species and their drug resistances because of the high incidence of nosocomial infection caused by multi-drug resistant bacteria. At first, several enzymes were tested to evaluate the efficacy of DNA extraction. N-acetylmuramidase, lysozyme and achromopeptidase were most effective to extract DNA from E. faecalis, E. faecium and S. aureus, respectively. After achromopeptidase extraction, the mecA gene was amplified by polymerase chain reaction (PCR) in clinically isolated MRSA (95 strains), MSSA (66), MRSE (methicillin-resistant S. epidermidis, 37), MSSE (methicillin-sensitive S. epidermidis, 1), S haemolyticus(5), S.hominis(1) and others (Enterococcus, Pseudomonas, and Streptococcus, total 45). PCR products were analyzed by agarose gel electrophoresis. The positive rates were 95% (MRSA), 1.5% (MSSA), and 97% (MRSE). The mecA gene was also positive in 2/2 of methicillin-resistant S.haemolyticus and 2/3 of methicillin-sensitive S.haemolyticus and 1/1 of methicillin-resistant S.hominis. The mecA gene was not detected in 45 non-Staphylococcal strains. MecA and femA gene by PCR and PBP 2' by IRMA were further detected in newly isolated MRSA (20 strains), MSSA(20), MRSE(14), MSSE(1) and S.simulans(2). Complete correlation between MPIPC susceptibility and mecA were found. The femA gene was positive in 39/40 of S. aureus, and 0/14 of S.epidermidis, 2/3 of S.simulans. PBP2' were positive in 20/20 of MRSA, 0/20 of MSSA, 14/14 of MRSE, 0/1 of MSSE, 1/1 of methicillin-resistant S.simulans, and 0/2 of methicillin-sensitive S.simulans. In conclusion, diagnoses of MRSA by simultaneous detection of mecA and femA gene as well as PBP2' are similarly useful because of their specificity and rapidity.
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PMID:[Method of DNA extraction and mecA, femA and PBP2' in multi-drug resistant bacterial strains]. 806 30

The complete amino acid sequence of cassowary (Casuarius casuarius) goose type lysozyme was analyzed by direct protein sequencing of peptides obtained by cleavage with trypsin, V8 protease, chymotrypsin, lysyl endopeptidase, and cyanogen bromide. The N-terminal residue of the enzyme was deduced to be a pyroglutamate group by analysis with a LC/MS/MS system equipped with the oMALDI ionization source, and then confirmed by a glutamate aminopeptidase enzyme. The blocked N-terminal is the first reported in this enzyme group. The positions of disulfide bonds in this enzyme were chemically identified as Cys4-Cys60 and Cys18-Cys29. Cassowary lysozyme was proved to consist of 185 amino acid residues and had a molecular mass of 20408 Da calculated from the amino acid sequence. The amino acid sequence of cassowary lysozyme compared to that of reported G-type lysozymes had identities of 90%, 83%, and 81%, for ostrich, goose, and black swan lysozymes, respectively. The amino acid substitutions at PyroGlu1, Glu19, Gly40, Asp82, Thr102, Thr156, and Asn167 were newly detected in this enzyme group. The substituted amino acids that might contribute to substrate binding were found at subsite B (Asn122Ser, Phe123Met). The amino acid sequences that formed three alpha-helices and three beta-sheets were completely conserved. The disulfide bond locations and catalytic amino acid were also strictly conserved. The conservation of the three alpha-helices structures and the location of disulfide bonds were considered to be important for the formation of the hydrophobic core structure of the catalytic site and for maintaining a similar three-dimensional structure in this enzyme group.
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PMID:The primary structure of cassowary (Casuarius casuarius) goose type lysozyme. 1186 97

We tested a previously described protocol for fluorescence in situ hybridization of marine bacterioplankton with horseradish peroxidase-labeled rRNA-targeted oligonucleotide probes and catalyzed reporter deposition (CARD-FISH) in plankton samples from different lakes. The fraction of Bacteria detected by CARD-FISH was significantly lower than after FISH with fluorescently monolabeled probes. In particular, the abundances of aquatic Actinobacteria were significantly underestimated. We thus developed a combined fixation and permeabilization protocol for CARD-FISH of freshwater samples. Enzymatic pretreatment of fixed cells was optimized for the controlled digestion of gram-positive cell walls without causing overall cell loss. Incubations with high concentrations of lysozyme (10 mg ml(-1)) followed by achromopeptidase (60 U ml(-1)) successfully permeabilized cell walls of Actinobacteria for subsequent CARD-FISH both in enrichment cultures and environmental samples. Between 72 and >99% (mean, 86%) of all Bacteria could be visualized with the improved assay in surface waters of four lakes. For freshwater samples, our method is thus superior to the CARD-FISH protocol for marine Bacteria (mean, 55%) and to FISH with directly fluorochrome labeled probes (mean, 67%). Actinobacterial abundances in the studied systems, as detected by the optimized protocol, ranged from 32 to >55% (mean, 45%). Our findings confirm that members of this lineage are among the numerically most important Bacteria of freshwater picoplankton.
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PMID:An improved protocol for quantification of freshwater Actinobacteria by fluorescence in situ hybridization. 1273 68

Lysobacter sp. IB-9374, which was isolated from soil as a high lysyl endopeptidase-producing strain (Chohnanet al., FEMS Microbiol. Lett., 213, 13-20, 2002), was found to produce a beta-lytic protease capable of lysing gram-positive bacteria such as Staphylococcus aureus, Microccocuseus, and Bacillus subtilis. The Lysobacter strain secreted the beta-lytic protease into the culture medium at a 2.4-fold higher level than Achromobacter lyticus. The enzyme was highly purified through a series of six steps with a high yield. The enzyme was strongly inhibited by tetraethylene-pentamine and 1,10-phenanthroline. The purified enzyme lysed more efficiently almost all the gram-positive bacteria tested than lysozyme, lysostaphin, and mutanolysin. The enzyme was very similar to Achromobacter beta-lytic protease containing one zinc atom in terms of amino acid composition and N-terminal sequence. The nucleotide sequence revealed that the mature enzyme was composed of 179 amino acid residues with additional 198 amino acids at the amino-terminal end of the enzyme. The deduced amino acid sequence of the mature enzyme coincided with that of the Achromobacter enzyme, although the prepro-region showed a 41% sequence identity with the counterpart. These results indicate that Lysobacter sp. is a useful strain for an efficient large-scale preparation of beta-lytic protease capable of lysing bacteria.
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PMID:Purification, bacteriolytic activity, and specificity of beta-lytic protease from Lysobacter sp. IB-9374. 1623 62


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