Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.31.1 (micrococcal nuclease)
 2,818 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mechanism by which changes in diet mediate levels of exportable enzymes and proenzymes in pancreatic tissue were studied in rats. The relative levels of mRNA coding for pancreatic amylase, lipase, procarboxypeptidases A and B, and the family of serine protease zymogens have been determined by the ability of isolated RNA to direct the synthesis of these products in a high-fidelity micrococcal nuclease-treated reticulocyte-lysate translation system. Translation products synthesized in vitro correlated directly with products synthesized in vivo in pancreatic lobules. Dietary adaptation was observed when dietary carbohydrate was increased from 0 to 58% at the expense of protein (81-23%). The increase in dietary carbohydrate over this range resulted in a 2-fold increase in amylase synthesis in pancreatic lobules and a 1.8-fold increase in mRNA-directed synthesis of amylase in the translation system in vitro. Concomitant with the decrease in dietary protein, synthesis of serine protease zymogens in pancreatic lobules and in the system in vitro decreased by approximately 50%. Over this range of dietary manipulation, ratios of amylase to serine proteases showed a 3.6-fold change. When dietary carbohydrate was further increased to 81% and protein reduced to 0, non-adaptive changes were observed since there was a decrease in amylase synthesis under conditions both in vivo and in vitro. mRNAs coding for pancreatic lipase and procarboxypeptidases A and B were unaffected by the dietary changes. These findings indicate that nutritional regulation in the tissue levels of pancreatic enzymes and proenzymes is mediated by changes in the content of active cytoplasmic mRNAs.
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PMID:Dietary regulation of levels of active mRNA coding for amylase and serine protease zymogens in the rat pancreas. 619 2

Helichrysum italicum G. Don (Compositae) is a shrub commonly found in dry, sandy and stony areas of Mediterranean regions. This plant is known for its anti-inflammatory, anti-allergic and antimicrobial activity. The aim of this study was to evaluate the effect of the diethyl ether extract on growth of Staphylococcus aureus (ATCC 6538P, MRSA and MSSA isolates) and the influence of subminimum inhibitory concentrations (subMICs) on some enzymes which are considered virulence factors. The results indicate that the H. italicum extract had an inhibitory effect on S. aureus strains reducing both their growth and some of the enzymes such as coagulase, DNAse, thermonuclease and lipase. Helichrysum italicum extract could be a novel antimicrobial agent, less toxic to human skin and tissues, worthy of further studies.
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PMID:Effects of Helichrysum italicum extract on growth and enzymatic activity of Staphylococcus aureus. 1139 24

Staphylococcus aureus synthesizes a large number of extracellular proteins that have been postulated to play a role in bacterial virulence. The proteomic approach was used to analyse the pattern of extracellular proteins of two different S. aureus strains, RN6390 and COL. Thirty-nine protein spots were identified by N-terminal sequencing or MALDI-TOF-MS. The differences of the extracellular protein patterns between both strains are striking. Among the 18 proteins identified in S. aureus COL there are nine proteins not yet discovered in S. aureus RN6390. These are enterotoxin B, leukotoxin D, enterotoxin, serin proteases (SplA and SplC), thermonuclease, an IgG binding protein and two so far unknown proteins in S. aureus with similarities to SceD precursor in Staphylococcus carnosus and to synergohymenotropic toxin precursor in Streptococcus intermedius. In contrast, lipase as well as staphylokinase identified in S. aureus RN6390 were not detectable in S. aureus COL under the same conditions. By using a regulatory mutant of sarA (ALC136) isogenic to strain RN6390 we identified five proteins positively regulated by SarA and 12 proteins negatively regulated by SarA. Besides V8 protease (StsP) and Hlb already described to be regulated by the sar locus new putatively sarA-dependent proteins were identified, e.g. glycerolester hydrolase and autolysin both down-regulated in the sarA mutant, and aureolysin, staphylokinase, staphopain and format tetrahydrofolate lyase up-regulated in the mutant. Moreover, the role of sigma B in expression of extracellular proteins was studied. Interestingly, we found 11 proteins at an enhanced level in a sigB mutant of S. aureus COL, among them enterotoxin B, alpha and beta hemolysin, serine proteases SplA and SplB, leukotoxin D, and staphopain homologues. The sigma B-dependent repression of gene expression occurs at the transcriptional level. Only one protein, SceD, was identified whose synthesis was down-regulated in the mutant indicating that its gene belongs to the sigma B-dependent general stress regulon.
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PMID:Extracellular proteins of Staphylococcus aureus and the role of SarA and sigma B. 1168 Dec 2

Nepeta cataria L., commonly known as catnip, is a perennial herb with a considerable folkloric reputation. A diethyl ether extract of this plant has been shown to have antimicrobial activity against fungi and Gram-positive bacteria. The aim of this work was to study the activity of N. cataria extract on 44 Staphylococcus aureus strains, some resistant to methicillin, and S. aureus 6538P (American Type Culture Collection) by evaluating the effect of subminimum inhibitory concentrations on coagulase, DNAse, thermonuclease and lipase production, and on in-vitro adherence. DNAse, thermonuclease and lipase were inhibited by concentrations equal to 1/2 and 1/4 MIC. A reduction of adherence was also observed.
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PMID:The effect of Nepeta cataria extract on adherence and enzyme production of Staphylococcus aureus. 1173 50

The use of Lactococcus lactis (the most extensively characterized lactic acid bacterium) as a delivery organism for heterologous proteins is, in some cases, limited by low production levels and poor-quality products due to surface proteolysis. In this study, we combined in one L. lactis strain use of the nisin-inducible promoter P(nisA) and inactivation of the extracellular housekeeping protease HtrA. The ability of the mutant strain, designated htrA-NZ9000, to produce high levels of stable proteins was confirmed by using the staphylococcal nuclease (Nuc) and the following four heterologous proteins fused or not fused to Nuc that were initially unstable in wild-type L. lactis strains: (i) Staphylococcus hyicus lipase, (ii) the bovine rotavirus antigen nonstructural protein 4, (iii) human papillomavirus antigen E7, and (iv) Brucella abortus antigen L7/L12. In all cases, protein degradation was significantly lower in strain htrA-NZ9000, demonstrating the usefulness of this strain for stable heterologous protein production.
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PMID:Controlled production of stable heterologous proteins in Lactococcus lactis. 1203 80

The vacuum-ultraviolet circular dichroism (VUVCD) spectra of 16 globular proteins (insulin, lactate dehydrogenase, glucose isomerase, lipase, conalbumin, transferrin, catalase, subtilisin A, alpha-amylase, staphylococcal nuclease, papain, thioredoxin, carbonic anhydrase, elastase, avidin, and xylanase) were successfully measured in aqueous solutions at 25 degrees C from 260 to 160 nm under a high vacuum using a synchrotron-radiation VUVCD spectrophotometer. These proteins exhibited characteristic CD spectra below 190 nm that were related to their different secondary structures, which could not be detected with a conventional CD spectrophotometer. The component spectra of alpha-helices, beta-strands, turns, and unordered structures were obtained by deconvolution analysis of the VUVCD spectra of 31 reference proteins including the 15 proteins reported in our previous paper [Matsuo, K. et al. (2004) J. Biochem. 135, 405-411]. Prediction of the secondary-structure contents using the SELCON3 program was greatly improved, especially for alpha-helices, by extending the short-wavelength limit of CD spectra to 160 nm and by increasing the number of reference proteins. The numbers of alpha-helix and beta-strand segments, which were calculated from the distorted alpha-helix and beta-strand contents, were close to those obtained on X-ray crystallography. These results demonstrate the usefulness of synchrotron-radiation VUVCD spectroscopy for the secondary structure analysis of proteins.
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PMID:Improved estimation of the secondary structures of proteins by vacuum-ultraviolet circular dichroism spectroscopy. 1604 51

Coagulase-negative staphylococci (CNS) have been identified as the etiological agent in various infections and are currently the microorganisms most frequently isolated in nosocomial infections. However, little is known about the virulence factors produced by CNS that contribute to the pathogenesis of infections caused by these microorganisms. The study of CNS isolated from infectious processes of newborns hospitalized in the Neonatal Unit of the Hospital of the Botucatu Medical School, UNESP, indicated Staphylococcus epidermidis as the most frequently isolated species (77.8%), which was also associated with clinically significant situations. The analysis of virulence factors revealed the production of slime in 20 (17.1%) of all CNS samples isolated and the synthesis of a broad spectrum of enzymes and toxins, including hemolysins (19.6%), lipase (17.1%), lecithinase (3.4%), DNAse (15.4%), thermonuclease (7.7%), and enterotoxin A, B or C (37.6%). Taking into consideration that the etiological importance of CNS has often been neglected, the present investigation confirmed that these microorganisms should not be ignored or classified as mere contaminants.
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PMID:Study of virulence factors in coagulase-negative staphylococci isolated from newborns. 1707 80

Capsid-targeted viral inactivation (CTVI), a conceptually powerful new antiviral strategy, is attracting increasing attention from researchers. Specifically, this strategy is based on fusion between the capsid protein of a virus and a crucial effector molecule, such as a nuclease (e.g., staphylococcal nuclease, Barrase, RNase HI), lipase, protease, or single-chain antibody (scAb). In general, capsid proteins have a major role in viral integration and assembly, and the effector molecule used in CTVI functions to degrade viral DNA/RNA or interfere with proper folding of viral key proteins, thereby affecting the infectivity of progeny viruses. Interestingly, such a capsid-enzyme fusion protein is incorporated into virions during packaging. CTVI is more efficient compared to other antiviral methods, and this approach is promising for antiviral prophylaxis and therapy. This review summarizes the mechanism and utility of CTVI and provides some successful applications of this strategy, with the ultimate goal of widely implementing CTVI in antiviral research.
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PMID:Capsid-Targeted Viral Inactivation: A Novel Tactic for Inhibiting Replication in Viral Infections. 2765 14