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

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

Samples of whole saliva and dental plaque were collected from initially 10-year old subjects who participated in a 40-month cohort study investigating the effect of chewing gum usage on caries rates. The subjects represented nine cohorts of which one did not receive gum, while in eight cohorts the subjects received gum containing either xylitol, sorbitol, their mixtures, or sucrose as bulk sweeteners, the maximum sweetener consumption in the form of gums being up to 10.7 g/day, used in 3-5 daily chewing episodes. Gum usage had no significant effect on the levels of salivary protein, IgA, alpha-amylase, peroxidase, lysozyme, SCN and buffer capacity. At the endpoint, the group that received 100% xylitol pellet-shaped gum five times/day, had significantly lower levels of sucrase (p <0.05) and free sialic acid (p < 0.001) in whole saliva than at baseline. This group showed significantly (p <0.05) smaller plaque index scores at two cross-sectional measurements, and exhibited the lowest log(10) counts of salivary lactobacilli at endpoint than most other groups. The salivary levels of peptidase(s) (oligopeptidase B-like enzymes) hydrolyzing N-alpha-benzoyl-DL-arginyl-p-nitroaniline were significantly (p<0.05) or almost significantly lower in groups which received 100% xylitol pellet gums. All groups exhibited obviously an aging-related increase of salivary mutans streptococcus scores, except the above xylitol group in which the mean scores did not change.
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PMID:Properties of whole saliva and dental plaque in relation to 40-month consumption of chewing gums containing xylitol, sorbitol of sucrose. 886 27

Aspergillus oryzae has numerous protease genes that might cause proteolytic degradation of heterologously-produced proteins. The productivity of the heterologous protein can be improved by protease gene disruption, but it is difficult to select disruption targets efficiently. In this study, we monitored the expression of 132 protease genes by DNA microarray. A group of protease genes up-regulated during cultivation was identified by clustering analysis. In this protease group, the nptB gene encoding neutral protease II was included as well as the alpA, tppA, and pepA genes, disruption of which has improved human lysozyme (HLY) production. The nptB gene was disrupted to investigate its involvement in HLY production, and nptB disruptants showed an improvement in the production. These observations suggest that monitoring the expression of protease genes is an efficient strategy in screening potential disruption targets for heterologous protein production in A. oryzae.
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PMID:Monitoring global gene expression of proteases and improvement of human lysozyme production in the nptB gene disruptant of Aspergillus oryzae. 1825 87