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SubtilisinSubtilisinsProprotein ConvertasesSerine EndopeptidasesBacillusSerine Proteinase InhibitorsAmino Acid SequenceChymotrypsinBacillus subtilisMolecular Sequence DataEnzyme StabilityKineticsStreptomycesProtease InhibitorsEndopeptidasesDimethylformamideProtein ConformationSubstrate SpecificityBinding SitesModels, MolecularProtein Refoldingalpha-AmylasesPeptide FragmentsEnzyme PrecursorsHydrogen-Ion ConcentrationFurinTrypsinBacterial ProteinsPeptide HydrolasesElectrophoresis, Polyacrylamide GelHydrolysisProprotein Convertase 2Proprotein Convertase 5Amino AcidsTrypsin Inhibitor, Kazal PancreaticTrypsin Inhibitor, Kunitz SoybeanDirected Molecular EvolutionAutolysisStreptomyces griseusReceptors, LDLMutagenesis, Site-DirectedArenaviruses, Old WorldProtein EngineeringMolecular WeightTrypsin InhibitorsAcetonitrilesStreptomycetaceaeEndopeptidase KBase SequenceCatalysisSequence Homology, Amino AcidDisulfidesThermococcusCloning, MolecularProtein Structure, SecondaryHordeumProtein DenaturationTemperaturePhenylmethylsulfonyl FluorideGlyoxalProtein PrecursorsProtein FoldingMutationSerpinsCircular DichroismX-Ray DiffractionProprotein Convertase 1SolventsEscherichia coliPancreatic ElastaseChromatography, High Pressure LiquidPleurotusSpectrophotometry, UltravioletProtein BindingHydrogen BondingHyperlipoproteinemia Type IIChemistry, OrganicProteolysisCholesterol, LDLLeechesProtein RenaturationArenavirusStructure-Activity RelationshipThermodynamicsProtein Structure, TertiarySterol Regulatory Element Binding Protein 2ChemistryEnzymes, ImmobilizedPeptidesChemical PhenomenaSpectrometry, FluorescenceRecombinant ProteinsSequence AlignmentThermolysinProtein Processing, Post-TranslationalTryptophanMolecular ChaperonesRibonuclease, PancreaticAspartokinase Homoserine DehydrogenaseHot Temperature
ProproteinBacillusProteaseContains SubtilisinSerine proteasesAmino-acid seqEnzymesEnzymeCarlsbergPeptidaseHomologyResiduesChymotrypsinGenePropeptideCatalyticStructureSiteSimilarCrystalRolePCSK9Proprotein convertase familyProteasesEnzymesInhibitorsAquatic toxicityTypeProteinPace4DetergentConcentrationsExposureStudyProductionLevelsAmount
Proprotein12
  • This gene encodes a member of the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking through regulated or constitutive branches of the secretory pathway. (nih.gov)
  • Association of proprotein convertase subtilisin/kexin type 9 (PCSK9) levels with abnormally high ankle-brachial index in atrial fibrillation. (nih.gov)
  • Proprotein convertase subtilisin kexin 9 (PCSK9), also named neural apoptosis-regulated convertase 1 (NARC-1), is a member of the proteinase K subfamily of subtilisin-related serine endoproteases. (nexelis.com)
  • PCSK9 (proprotein convertase subtilisin/kexin 9) increases low-density lipoprotein (LDL)-cholesterol levels via LDL receptor (LDLR) degradation. (elsevierpure.com)
  • CIENCIASMEDICASNEWS: Expert consensus on the rational clinical use of proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors. (blogspot.com)
  • Two proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors, evolocumab and alirocumab, have recently been approved by both the Food and Drug Administration (FDA) and the European Medicines Agency (EMA) for the treatment of hypercholesterolemia. (blogspot.com)
  • Efficacy and Safety of Alirocumab and Evolocumab as Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) Inhibitors in Familial Hypercholesterolemia: A Systematic Review and Meta-Analysis. (bvsalud.org)
  • PURPOSE:Proprotein convertase subtilisin-kexin type 9 (PCSK9) promotes low density lipoprotein (LDL) receptor degradation, thereby providing a key pathway for LDL metabolism. (shengsci.com)
  • Proprotein convertase subtilisin kexin t. (gazi.edu.tr)
  • Patients receiving proprotein convertase subtilisin kexin 9 (PCSK9) inhibitors 6. (nih.gov)
  • Furin is a ubiquitous subtilisin-like proprotein convertase. (neb.com)
  • Melanocortin-4 receptor agonists are approved for weight management in patients with rare genetic conditions (ie, proopiomelanocortin, proprotein convertase subtilisin/kexin type 1, and leptin receptor deficiencies). (medscape.com)
Bacillus6
  • Subtilisin is a protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis. (wikipedia.org)
  • People who are sensitive to Subtilisin (Alcalase) usually are also allergic to the bacterium Bacillus subtilis. (wikipedia.org)
  • This innovative research discovered the fibrinolytic characteristic, the mechanism of Subtilisin that was extracted from Bacillus Subtilis G8, and it has also displayed a strong interaction between Subtilisin and Fibrin. (sph.ac.id)
  • Subtilisin, a serine proteinase from Bacillus subtilis (natto), is an important enzyme for the taste and flavor of natto [10]. (sph.ac.id)
  • Moreover, previous studies by Pinotoan et al (2021) and Dikson et al (2022) also show that one of the enzymes from Bacillus subtilis G8 is responsible for its fibrinolytic activity is Subtilisin (Figure 1). (sph.ac.id)
  • The main model of subtilisin in this study was generated from the subtilisin amino acid sequence of Bacillus subtilis G8 which was reported as a Natto starter culture in the previous study by Dikson et al (2022). (sph.ac.id)
Protease4
  • When they sequenced the amino acid of the peptide, they found that it is derived from a member of the subtilisin-like protease (subtilase) family, which are characterized by a catalytic triad of amino acids-aspartate, histidine, and serine. (isaaa.org)
  • In order to address this issue we have concentrated on the subtilisin-like serine protease encoding gene ABNORMAL LEAF-SHAPE1 . (biologists.com)
  • Subtilisin, an enzyme, is also a protease similar to Nattokinase. (sph.ac.id)
  • Subtilisin is a serine protease in prokaryotes . (bionity.com)
Contains Subtilisin1
Serine proteases2
  • Insect-pathogenic fungi use subtilisin-like serine proteases (SLSPs) to degrade chitin-associated proteins in the insect procuticle. (doe.gov)
  • In this study, subtilisin-like serine proteases (subtilases) were examined for their putative role in cell viability. (pacific.edu)
Amino-acid seq1
  • The larger polypeptide (M(r) ~77 kDa) yielded an N-terminal amino-acid sequence that was homologous with a range of plant subtilisin-like serine proteinases. (who.int)
Enzymes1
  • The chief feature of a serine peptidase is that they have a alone Ser residue of exceeding responsiveness that forms a covalent bond with some of the substrates or inhibitors ( Creighton J ) . In both Trypsin and subtilisin shows many similarity and both contains the peculiarly extremely reaction serine residue which can be specifically phosphorylated by other substrate such as isoprophylfluorophosphate ( Alden and Wright, 1970 ) , sulphonated and acylated utilizing different enzymes. (graduateway.com)
Enzyme2
  • This ASA research Project with the UPH university focuses on discovering the fibrinolysis activity and its mechanism of action from Subtilisin, the enzyme that gives natto its unique characteristic in degrading blood clot lysis. (sph.ac.id)
  • Subtilisin BPN is an extracellular peptidase enzyme of a spore organizing being Bacullus Amyloliquelaniens. (graduateway.com)
Carlsberg1
  • Subtilisin is found in assorted signifiers such as Carlsberg and 'BNP. (graduateway.com)
Peptidase2
  • The major clans found in humans include the chymotrypsin -like, the subtilisin -like, the alpha/beta hydrolase, and signal peptidase clans. (bionity.com)
  • In this essay I will be reexamining the construction and map of a serine peptidase known as subtilisin and I will analyse the different techniques used by different research workers to specify the construction or maps of Subtilisin. (graduateway.com)
Homology1
  • The N-terminal propeptide region shows homology with bacterial subtilisin. (sigmaaldrich.com)
Residues1
  • subtilisin bpn' prosegment (77 residues) complexed with a mutant subtilisin bpn' (266 residues). (wikipedia.org)
Chymotrypsin1
  • Subtilisin is evolutionary unrelated to the chymotrypsin-clan, but shares the same catalytic mechanism utilising a catalytic triad , to create a nucleophilic serine . (bionity.com)
Gene1
  • In molecular biology using B. subtilis as a model organism, the gene encoding subtilisin (aprE) is often the second gene of choice after amyE for integrating reporter constructs into, due to its dispensability. (wikipedia.org)
Propeptide1
  • The N-terminal contains an I9 propeptide domain (InterPro: IPR010259) that assists the folding of subtilisin. (wikipedia.org)
Catalytic1
  • Nattokinase and Subtilisin have similar features, including the action mechanism and the catalytic triad: they are identical to each other, except for their structure. (sph.ac.id)
Structure2
  • The structure of subtilisin has been determined by X-ray crystallography. (wikipedia.org)
  • The 3D structure of Subtilisin was constructed through the SWISS-MODEL workspace [4], using the Nattokinase structure as the template. (sph.ac.id)
Site1
  • This is possible due to the nature of the charge-relay site of subtilisin. (wikipedia.org)
Similar1
  • The Trypsin and the subtilisin are believed to hold evolved as they have similar mechanism of action even though they are non detectably related. (graduateway.com)
Crystal1
  • The crystal structures of 4 variants of subtilisin, each one containing an engineered disulfide crosslink have been determined. (helmholtz-hzi.de)
Role1
  • The reference's important amino acids that have the role of catalysis were aligned with Subtilisin at the same pattern and therefore concluded as conserved. (sph.ac.id)
PCSK98
  • Recent microarray studies and database searches identified a novel member of the proprotein convertase family called proprotein convertase subtilisin kexin 9 (PCSK9). (nih.gov)
  • The inhibition of proprotein convertase subtilisin/kexin type 9 (PCSK9) serine protease represents a novel lipid-lowering tool. (medscape.com)
  • PCSK9 ( proprotein convertase subtilisin /kexin type 9) is an enzyme that helps to reduce cardiovascular events. (bvsalud.org)
  • Patients receiving proprotein convertase subtilisin kexin 9 (PCSK9) inhibitors 6. (nih.gov)
  • Over the last decade, inhibition of proprotein convertase subtilisin/kexin type 9 (PCSK9) has emerged as a promising target to reduce residual cardiovascular disease risk. (medscape.com)
  • Abstracts include data evaluating Repatha ® (evolocumab), a proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitor for the treatment of patients with high cholesterol, across ESC/European Atherosclerosis Society (EAS) cardiovascular risk subgroups, as well as the long-term efficacy and safety of Repatha treatment in patients with the genetic condition heterozygous familial hypercholesterolemia (HeFH). (prnewswire.com)
  • Evolocumab is an investigational fully human monoclonal antibody that inhibits proprotein convertase subtilisin/kexin type 9 (PCSK9), a protein that reduces the liver's ability to remove LDL-C from the blood. (prnewswire.com)
  • In recent years, two new drugs were approved for patients who are unable to reduce circulating LDL-C with the current therapies: evolocumab and alirocumab (proprotein convertase subtilisin/kexin type nine [PCSK9] inhibitors). (springer.com)
Proprotein convertase family2
  • The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. (antikoerper-online.de)
  • From NCBI Gene: This gene encodes a member of the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking through regulated or constitutive branches of the secretory pathway. (nih.gov)
Proteases3
  • The prepatellamide is heterocyclized to form thiazole and oxazoline rings and the peptide is cleaved to form the two cyclic patellamides A and C. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). (nih.gov)
  • Induction of IDO1 and Kynurenine by Serine Proteases Subtilisin, Prostate Specific Antigen, CD26 and HtrA: A New Form of Immunosuppression? (ox.ac.uk)
  • We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin. (ox.ac.uk)
Enzymes2
  • Enzymes such as subtilisin-like proteinase, glutamyl endopeptidase, and metalloproteinase have been described in detail in the dissertations of Ye. (eurekalert.org)
  • Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes. (cathdb.info)
Inhibitors1
  • Natural Proprotein Convertase Subtilisin/Kexin Type 9 Inhibitors: A Review. (bvsalud.org)
Aquatic toxicity3
  • Aquatic toxicity studies with subtilisin revealed that the species most sensitive to the test substance was the invertebrate Daphnia magna for acute effects and fish for chronic effects. (europa.eu)
  • Based on the aquatic toxicity data subtilisin is classified as acute toxic to aquatic organism category 1 and chronic toxicity to aquatic organisms category 2. (europa.eu)
  • Subtilisin is unstable in aquatic media and it is thus crucial when performing a longterm aquatic toxicity study with subtilisin to optimize and adjust the test design in order to avoid degradation/inactivation during exposure. (europa.eu)
Type3
  • 13. Processing of wild-type and mutant proinsulin-like growth factor-IA by subtilisin-related proprotein convertases. (nih.gov)
  • The FOURIER-OLE studies are the longest trials with a proprotein convertase subtilisin/kexin type 9 inhibitor (PCSK9i) to date, with patients receiving Repatha for a median of 5 years and some patients receiving Repatha continuously for up to 8.5 years across the FOURIER and OLE study period. (amgen.com)
  • The key health concern identified for Subtilisin is respiratory (Type 1) allergy. (heraproject.com)
Protein2
  • Furthermore, as subtilisin is a protein it is expected to be degraded in the gastrointestinal tract. (europa.eu)
  • In this work, immobilization of a fullerene derivative with a mutant subtilisin is demonstrated, and the effect of the fullerene on the protein activity is determined. (nih.gov)
Pace41
Detergent4
  • This study specifically evaluated the use of an SKC Button inhalable aerosol sampler with a Grimm Aerosol Monitor for monitoring low concentrations of subtilisin particulates in air within a laundry detergent production facility. (cdc.gov)
  • Methods: Air samples of detergent with subtilisin were collected using a Button sampler containing a glass fiber filter concurrently with a Grimm model 1.109 Aerosol Spectrometer. (cdc.gov)
  • Sampling locations included a detergent containing subtilisin (DCS) production area and a specially constructed enclosure where DCS was introduced in a controlled manner. (cdc.gov)
  • Consumers may be exposed by skin contact during laundry hand wash (exposure up to a Subtilisin concentration of 0.0009%), by laundry pre-treatment using liquid detergent (0.09%), by hand dish wash (0.0001%) and by fabric wear with skin in contact with Subtilisin deposited during the wash (0.0035 g/cm2). (heraproject.com)
Concentrations3
  • Evaluation of the use of an SKC button inhalable aerosol sampler with a Grimm aerosol monitor to determine air concentrations of subtilisin. (cdc.gov)
  • The linear regression for the average concentrations of DCS aerosol measured on the Button filter media compared to the average subtilisin detected from the aerosol in the enclosure produced an R2 value of 0.66 (p = 0.004). (cdc.gov)
  • Conclusion: The results of the statistical evaluation from the aerosol monitoring results in the enclosure indicate the Button inhalable sampler compared with the results from the Grimm aerosol monitor may be a valid method for determining airborne subtilisin concentrations for aerosols with diameters less than or equal to the 25 µm particle size. (cdc.gov)
Exposure4
  • PNEC values for sediment exposure have not been derived because subtilisin is readily biodegradable, highly water soluble and has a very low potential for adsorption to sediments. (europa.eu)
  • The effect of long-term aquatic exposure to subtilisin has been assessed in the early life stage test (ELS), daphnia reproduction assay and in algae. (europa.eu)
  • The ACGIH ceiling limit and NIOSH short term exposure limit (STEL) for subtilisin is 0.06 µg/m3 making it the lowest exposure limit established for any exposure by the organizations. (cdc.gov)
  • Based on the HERA detergents exposure scenario, the environmental risk characterisation of Subtilisin revealed risk characterisation ratios below 1 in all environmental compartments. (heraproject.com)
Study3
  • Take our patient case study quiz specially curated for you by our Faculty Member, Prof. Chern-En Chiang. (wiley.com)
  • Study purpose: Currently, there is no OSHA or NIOSH monitoring method for subtilisin. (cdc.gov)
  • This study evaluated a personal aerosol monitoring method for detection and quantification of subtilisin. (cdc.gov)
Production1
  • Discussion: The amount of subtilisin in all air samples in the DCS production area were below the limit of quantitation due to the subtilisin encapsulation at the DCS production area. (cdc.gov)
Levels1
  • The PNEC value for STP is based on actual measurements of subtilisin levels in STP connected to manufacturing site. (europa.eu)
Amount1
  • Sample analysis was conducted with a Konelab Arena 20 analyzer to quantify the amount of subtilisin collected on the filter of each air sample. (cdc.gov)