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*  Papain - Wikipedia
Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and ... The enzyme is deacylated by a water molecule and releases the carboxy terminal portion of the peptide. In immunology, papain is ... including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity. ... Aspartate-158 was thought to play a role analogous to the role of aspartate in the serine protease catalytic triad, but that ...
  https://en.wikipedia.org/wiki/Papain
*  Protease and Phosphatase Inhibitor Tablets | Thermo Fisher Scientific - JP
... endopeptidases (serine, aspartic, cysteine and metalloproteinases) cleave the peptide distal to the terminus. Plants contain ... After evaluating many fluorescent substrates, we chose assay substrates for cysteine proteases (papain) and serine proteases ( ... Proteases are a ubiquitous class of enzymes that hydrolyze protein peptide bonds. Proteases are divided into two broad ... Cleavage of the cysteine protease substrate results in fluorescence at 460nm, and cleavage of the serine protease results in ...
  https://www.thermofisher.com/jp/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/protein-biology-application-notes/protease-phosphatase-inhibitor-tablets.html
*  Peptidase C12, ubiquitin carboxyl-terminal hydrolase (IPR001578) | InterPro | EMBL-EBI
A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ... Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine ... Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ... Families within the CA clan are loosely termed papain-like as protein fold of the peptidase unit resembles that of papain, the ...
  http://www.ebi.ac.uk/interpro/entry/IPR001578
*  Peptidase C10, streptopain (IPR000200) | InterPro | EMBL-EBI
A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ... Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine ... Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ... Clan CA includes proteins with a papain-like fold. There is a catalytic triad which occurs in the order: Cys/His/Asn (or Asp). ...
  http://www.ebi.ac.uk/interpro/entry/IPR000200
*  Peptidase C1B, bleomycin hydrolase (IPR004134) | InterPro | EMBL-EBI
A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ... Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine ... Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ... Other cysteine peptidases from the papain family have no effect on bleomycins [PMID: 8639621, PMID: 2477059]. Bleomycin ...
  http://www.ebi.ac.uk/interpro/entry/IPR004134
*  Endopeptidase, NLPC/P60 domain (IPR000064) | InterPro | EMBL-EBI
A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ... Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine ... This entry represents the NLPC/P60 domain, which is a primitive, papain-like peptidase in the CA clan of cysteine peptidases ... Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ...
  https://www.ebi.ac.uk/interpro/entry/IPR000064
*  Protease - Wikipedia
... others attack internal peptide bonds of a protein (endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). ... Proteases can be classified into seven broad groups: Serine proteases - using a serine alcohol Cysteine proteases - using a ... A seventh catalytic type of proteolytic enzymes, asparagine peptide lyase, was described in 2011. Its proteolytic mechanism is ... Serine, threonine and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ...
  https://en.wikipedia.org/wiki/Protease
*  Master Formulas take the body back to what it was intended to be.
Papain by far is the most widely studied of the cysteine enzymes because of its commercial value.. ... internal peptide bonds of a protein (endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase).. Proteases are ... Acid proteases secreted into the stomach (such as pepsin) and serine proteases present in duodenum (trypsin and chymotrypsin) ... Papain. Proteolytic enzymes are widely used in cell isolation. With some tissues papain has proved less damaging and more ...
  http://www.advancedhealthplan.com/masterformulas.html
*  Patent US20110045138 - Enzymatic Process - Google Patentsuche
EC 3.4 comprises enzymes acting on peptide bonds (peptidases/proteinases) and EC 3.5 comprises enzymes that act on carbon- ... cysteine-carboxypeptidase (3.4.18), omegapeptidase (3.4.19), serine-endopeptidase (3.4.21), cysteine-endopeptidase (3.4.22), ... Endopeptidases include, without limitation, trypsin, chymotrypsin, pepsin, papain, and elastase. ... Enzymes. * [0014] Useful enzyme classes include proteolytic enzymes that hydrolyze bonds in a protein, and optionally, a ...
  https://www.google.ch/patents/US20110045138
*  Hemoglobin digestion in Blood-Feeding Ticks: Mapping a Multi-Peptidase Pathway by Functional Proteomics
10 mM E-64 for papain-type cysteine peptidases (Barrett et al., 1982), 20 nM cystatin for cysteine peptidases (Turk et al., ... Aza-peptide Michael acceptors: a new class of inhibitors specific for caspases and other clan CD cysteine proteases. J. Med. ... The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays. Arch ... Previous studies have focused on individual enzymes in particular species and identified mainly cysteine peptidases (e.g. ...
  http://pubmedcentralcanada.ca/pmcc/articles/PMC2801564/
*  Digestion of Proteins by Proteases - Study Solutions
... hydrolyze the peptide bond between amino acid residues in a polypeptide chain. ... Cysteine proteases have a similar mechanism, but use cysteine rather than serine. These include the plant proteases (papain, ... Endopeptidases cleave the target protein internally. Exopeptidases remove single amino acids from the amino- or carboxy- ... Proteases (also known as proteinases or peptidases ) hydrolyze the peptide bond between amino acid residues in a polypeptide ...
  http://istudy.pk/digestion-proteins-proteases/
*  PatBase classification lookup
Cysteine endopeptidases (3.4.22), e.g. stem bromelain, papain, ficin, cathepsin H. ... Vasoactive intestinal peptide [VIP]; Related peptides (e.g. Exendin). A61K38/2285: . . . . Endothelin, vasoactive intestinal ... Mixtures of enzymes or proenzymes covered by more than a single one of groups A61K38/44 - A61K38/46 or A61K38/51 - A61K38/53. ... Serine endopeptidases (3.4.21). A61K38/4826: . . . . . . Trypsin (3.4.21.4) Chymotrypsin (3.4.21.1). ...
  https://www.patbase.com/linkclass.asp?CCC=CPC&CLASS=A61K38%2F00
*  Protease - Wikipedia
... others attack internal peptide bonds of a protein (endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). ... One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or ... Peptide lyases[edit]. A seventh catalytic type of proteolytic enzymes, asparagine peptide lyase, was described in 2011. Its ... Serine, threonine and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ...
  https://en.wikipedia.org/wiki/E1101
*  The ubiquitous gp63-like metalloprotease from lower trypanosomatids: in the search for a function
Proteolytic enzymes: serine and cysteine peptidases. Methods Enzymol 244: 1-15. [ Links ]. BARRETT AJ. 1995. Proteolytic ... whereas endopeptidases cleave peptide bonds within a polypeptide chain. Based on their site of action at the NH2 or COOH ... Human and parasitic papain-like cysteine proteases:their role in physiology and pathology and recent developments in inhibitors ... PROTEOLYTIC ENZYMES. Proteases are degradative enzymes that catalyze the cleavage of peptide bonds in macromolecular proteins ...
  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652006000400006&lng=en&tlng=en
*  List of MeSH codes (D08) - Wikipedia
... cysteine endopeptidases MeSH D08.811.277.656.300.215.096 --- bromelains MeSH D08.811.277.656.300.215.120 --- calpain MeSH ... serine endopeptidases MeSH D08.811.277.656.300.760.030 --- acrosin MeSH D08.811.277.656.300.760.176 --- chymotrypsin MeSH ... peptide synthases MeSH D08.811.464.259.850.400 --- glutamate-cysteine ligase MeSH D08.811.464.259.850.500 --- glutathione ... Ubiquitin-activating enzyme MeSH D08.811.464.938.500 --- ubiquitin-conjugating enzymes MeSH D08.811.464.938.750 --- ubiquitin- ...
  https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)
*  Patent US7101697 - Restriction endonucleases, method of synthesis and use thereof - Google Patents
In particular, serine endopeptidases, cysteine endopeptidases, aspartic acid endopeptidases and/or metalloendopeptidases may be ... 3. A method of cleaving a DNA comprising cleaving the DNA with an enzyme, wherein the enzyme comprises the first restriction ... M. Reuter, et al., Regions of endonuclease EcoRII involved in DNA target recognition identified by membrane-bound peptide ... papain, pepsin, mycolysin and others may also be used. ... enzymes previously classified in enzyme group EC 3.4.99. After ...
  http://www.google.com/patents/US7101697?dq=6,654,957
*  EC 3 Introduction
These are the sub-subclasses of serine endopeptidases (EC 3.4.21), cysteine endopeptidases (EC 3.4.22), aspartic endopeptidases ... Enzyme: - S3 - S2 - S1 * S1'- S2'- S3'- In this representation, the catalytic site of the enzyme is marked *. The peptide bond ... 5. Berger, A. and Schechter, I. Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos. ... EC 3.5 Acting on Carbon-Nitrogen Bonds, other than Peptide Bonds. To this subclass belong those enzymes hydrolysing amides, ...
  http://www.sbcs.qmul.ac.uk/iubmb/enzyme/EC3/intro.html
*  Modeling and structural analysis of PA clan serine proteases
Serine proteases account for over a third of all known proteolytic enzymes; they are involved in a variety of physiological ... The PA clan of endopeptidases is the most abundant and over two thirds of this clan is comprised of the S1 family of serine ... I. Papain. Biochem Biophys Res Commun. 1967;27(2):157-162. doi: 10.1016/S0006-291X(67)80055-X. [PubMed] [Cross Ref] ... of these proteases involves nucleophilic attack of the carbonyl atom of the substrate peptide bond by a catalytic serine (Ser) ...
  http://pubmedcentralcanada.ca/pmcc/articles/PMC3434108/?lang=en-ca
*  Oligopeptidase - Wikipedia
The peptide has first to penetrate into a 4 Å hole on the surface of the enzyme in order to reach an 8,500Å3 internal cavity, ... Oligopeptidase is a term coined in 1979 to designate a sub-group of the endopeptidases, which are not involved in the digestion ... link) Fulöp V, Szeltner Z, Polgár L (2000). "Catalysis of serine oligopeptidases is controlled by a gating filter mechanism". ... 1993). "Dynorphin-derived peptides reveal the presence of a critical cysteine for the activity of brain endo-oligopeptidase A ...
  https://en.wikipedia.org/wiki/Oligopeptidase
*  Proteolytic Enzymes
Cysteine proteases Wed, 23 Nov 2016 , Proteolytic Enzymes Given their broad specificity for papain family members and fast- ... The serine peptidases Sun, 04 Oct 2015 , Proteolytic Enzymes This is the most thoroughly studied class of enzymes in the ... Peptide mass mapping Sat, 28 May 2016 , Proteolytic Enzymes Protein identification by peptide mass mapping is based on the idea ... Sun, 26 Apr 2015 , Proteolytic Enzymes Target proteinases some metallo-endopeptidases Molecular weight 543.6 Effective ...
  http://www.europeanmedical.info/proteolytic-enzymes/
*  Protease Inhibitor A, PIA 100x [PIA100X] - $48.75 Equl offers Enzyme Assay Kits, Reagent Mixtures, Enzymes, Glycobiology,...
... trypsin-like serine proteases, papain and cysteine proteases. Each vial contains 0.02 mg/ml antipain, 0.05 mg/ml leupeptin, and ... cocktail of two inhibitors in EDTA which has been optimized for the inhibition of calcium-dependent endopeptidases, ... cocktail of two inhibitors in EDTA which has been optimized for the inhibition of calcium-dependent endopeptidases, trypsin- ... like serine proteases, papain and cysteine proteases. Each vial contains 0.02 mg/ml antipain, 0.05 mg/ml leupeptin, and 50 mg/ ...
  http://www.equl.com/index.php?main_page=product_info&cPath=70_1083_1367&products_id=67634
*  US5830995A - Fanphiregulins: a family of heparin-binding epithelial cell growth factors - Google Patents
... tested in an ELISA that uses mouse monoclonal antibody 6R1C generated against a partially refolded peptide from the cysteine- ... The samples were incubated with 50 units/ml of enzyme for 48 hrs at 37° C. in a 100 mM sodium phosphate buffer at pH 7.5 ... and the two Fab or Fab fragments which can be generated by treating the antibody molecule with papain and a reducing agent. ... The compositions indicated presence of methionine and an additional equivalent of lysine and serine compared with the sequence ...
  https://patents.google.com/patent/US5830995A/en
*  WikiGenes - CTSC - cathepsin C
Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Turk, B., Turk, V., Turk, D ... The enzymes, except cathepsin C, are endopeptidases (reviewed in Kirschke et al., 1995), although cathepsin B was found also to ... of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme ... Using novel reversible peptide nitrile inhibitors of cathepsin C, and cell-based assays with U937 and EcoM-G cells, we ...
  https://www.wikigenes.org/e/gene/e/1075.html
*  US5279937A - Use of macroglobulins to improve the signal-to-background ratio in affinity binding assays - Google...
A wide range of endopeptidases, including serine, cysteine, aspartic and metalloproteinases thereby lose all activity toward ... The method of claim 15 wherein the reversible inhibitor is a peptide or protein and is inactivated with activated papain. ... Immunological testing involving labelled substances with enzyme label (including co-enzymes, co-factors, enzyme inhibitors or ... Use of Enzyme Inhibitors in Affinity Binding Assays. Enzyme inhibitors have been used as binding reagents (see March, U.S. Pat ...
  https://patents.google.com/patent/US5279937
*  Solid-state fermentation of corn-soybean meal mixed feed with Bacillus subtilis and Enterococcus faecium for degrading...
B. subtilis secretes many proteolytic enzymes during fermentation, including aminopeptidases, serine endopeptidases, and ... Peptide absorption and utilization: Implications for animal nutrition and health. J Anim Sci. 2008;86:2135-55.View Article ... Methionine and cysteine were analyzed as Met sulfone and cysteic acid after cold performic acid oxidation overnight before ... Improvement of the Nutritional Quality of Cottonseed Meal by Bacillus subtilis and the Addition of Papain. Int J Agric Biol. ...
  https://jasbsci.biomedcentral.com/articles/10.1186/s40104-017-0184-2