Thermolysin
Trypsin
Amino Acid Sequence
Bromosuccinimide
Peptide Fragments
Chymotrypsin
Bacillus
Protease Inhibitors
Endopeptidases
Glycopeptides
Neprilysin
Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.
Zinc
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
Enzyme Stability
Carboxypeptidases A
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.
Binding Sites
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Peptide Hydrolases
Cyanogen Bromide
Thiorphan
Amino Acids
Different regulation of the p53 core domain activities 3'-to-5' exonuclease and sequence-specific DNA binding. (1/552)
In this study we further characterized the 3'-5' exonuclease activity intrinsic to wild-type p53. We showed that this activity, like sequence-specific DNA binding, is mediated by the p53 core domain. Truncation of the C-terminal 30 amino acids of the p53 molecule enhanced the p53 exonuclease activity by at least 10-fold, indicating that this activity, like sequence-specific DNA binding, is negatively regulated by the C-terminal basic regulatory domain of p53. However, treatments which activated sequence-specific DNA binding of p53, like binding of the monoclonal antibody PAb421, which recognizes a C-terminal epitope on p53, or a higher phosphorylation status, strongly inhibited the p53 exonuclease activity. This suggests that at least on full-length p53, sequence-specific DNA binding and exonuclease activities are subject to different and seemingly opposing regulatory mechanisms. Following up the recent discovery in our laboratory that p53 recognizes and binds with high affinity to three-stranded DNA substrates mimicking early recombination intermediates (C. Dudenhoeffer, G. Rohaly, K. Will, W. Deppert, and L. Wiesmueller, Mol. Cell. Biol. 18:5332-5342), we asked whether such substrates might be degraded by the p53 exonuclease. Addition of Mg2+ ions to the binding assay indeed started the p53 exonuclease and promoted rapid degradation of the bound, but not of the unbound, substrate, indicating that specifically recognized targets can be subjected to exonucleolytic degradation by p53 under defined conditions. (+info)The cyclic structure of microcin J25, a 21-residue peptide antibiotic from Escherichia coli. (2/552)
Microcin J25 (MccJ25) is the single representative of the immunity group J of the microcin group of peptide antibiotics produced by Enterobacteriaceae. It induces bacterial filamentation in susceptible cells in a non-SOS-dependent pathway [R. A. Salomon and R. Farias (1992) J. Bacteriol. 174, 7428-7435]. MccJ25 was purified to homogeneity from the growth medium of a microcin-overproducing Escherichia coli strain by reverse-phase HPLC. Based on amino acid composition and absolute configuration determination, liquid secondary ion and electrospray mass spectrometry, extensive two-dimensional NMR, enzymatic and chemical degradations studies, the structure of MccJ25 was elucidated as a 21-residue peptide, cyclo(-Val1-Gly-Ile-Gly-Thr- Pro-Ile-Ser-Phe-Tyr-Gly-Gly-Gly-Ala-Gly-His-Val-Pro-Glu-Tyr-Phe21- ). Although MccJ25 showed high resistance to most of endoproteases, linearization by thermolysin occurred from cleavage at the Phe21-Val1 bond and led to a single peptide, MccJ25-L. While MccJ25 exhibited remarkable antibiotic activity towards Salmonella newport and several E. coli strains (minimal inhibitory concentrations ranging between 0.01 and 0.2 microgram.mL-1), the thermolysin-linearized microcin showed a dramatic decrease of the activity, indicating that the cyclic structure is essential for the MccJ25 biological properties. As MccJ25 is ribosomally synthesized as a larger peptide precursor endowed with an N-terminal extremity, the present study shows that removal of this extension and head-tail cyclization of the resulting propeptide are the only post-translational modifications involved in the maturation of MccJ25, that appears as the first cyclic microcin. (+info)Studies on the formation and stability of a complex between Streptomyces proteinaceous metalloprotease inhibitor and thermolysin. (3/552)
The effects of certain physicochemical parameters on the formation and stability of a complex between Streptomyces proteinaceous metalloprotease inhibitor (SMPI) and thermolysin were investigated. SMPI had its lowest Ki value at a pH of around 6.5 (similar to the pH dependence of the kcat/K(m) of thermolysin catalysis), reflecting the splitting mechanism of the SMPI inhibition of thermolysin. This Ki increased with an increase in pressure, and in (Ki-1) was almost linear with respect to pressure. The volume of the reaction (delta Vcomp), which is the volume change accompanying enzyme-inhibitor complex formation, was calculated as +8.1 +/- 0.3 mL.mol-1, which has a sign opposite to delta Vcomp for neutral peptide inhibitors and acyl-peptide substrates. The temperature dependence of Ki-1 gave the reaction enthalpy (delta Hcomp) and reaction entropy (delta Scomp) of the complex formation as 34.6 +/- 1.4 kJ.mol-1 and 298 +/- 5 J.mol-1.K-1, respectively. These positive reaction volumes and reaction entropies were related to the electrostatic interactions and ionic strength dependence of Ki which corresponded to the key ionic interaction during complex formation. Complex formation with SMPI stabilized thermolysin against pressure perturbation as observed by the changes in the Trp fluorescence of thermolysin with increasing pressure. Thermal stability, however, was affected very little by complex formation with SMPI. Phosphoramidon, Cbz-Phe-Gly-NH2 and Cbz-Phe also positively affected the pressure-tolerance of thermolysin, in the following order: Cbz-Gly-Phe-NH2 < Cbz-Phe << phosphoramidon. The third compound exhibited stabilizing effects comparable with those of SMPI, which suggests that the interaction between SMPI and thermolysin was localized to the reactive site. (+info)A Kazal-type trypsin inhibitor from the protochordate Ciona intestinalis. (4/552)
A trypsin inhibitor from Ciona intestinalis, present throughout the animal, was purified by ion-exchange chromatography followed by four HPLC steps. By MS the molecular mass of the native form was determined to be 6675 Da. The N-terminal amino acid sequence was determined by protein sequencing, but appeared to be partial because the theoretical molecular mass of the protein was 1101 Da too low. Thermolysin treatment gave rise to several fragments each containing a single disulphide bridge. By sequence analysis and MS intramolecular disulphide bridges could unequivocally be assigned to connect the pairs Cys4-Cys37, Cys8-Cys30 and Cys16-Cys51. The structure of the inhibitor is homologous to Kazal-type trypsin inhibitors. The inhibitor constant, KI, for trypsin inhibition was 0.05 nM whereas chymotrypsin and elastase were not inhibited. To reveal the complete sequence the cDNA encoding the trypsin inhibitor was isolated. This cDNA of 454 bp predicts a protein of 82 amino acid residues including a 20 amino acid signal peptide. Moreover, the cDNA predicts a C-terminal extension of 11 amino acids compared to the part identified by protein sequencing. The molecular mass calculated for this predicted protein is in accordance with the measured value. This C-terminal sequence is unusual for Kazal-type trypsin inhibitors and has apparently been lost early in evolution. The high degree of conservation around the active site strongly supports the importance of the Kazal-type inhibitors. (+info)Parvalbumin from rabbit muscle. Isolation and primary structure. (5/552)
A parvalbumin, with its characteristic low molecular weight (approximately 12000) acidic isoelectric point (approximately 5.5), ultraviolet spectrum (maxm 259 nm) and Ca2+-binding capacity (2 mol/mol protein) has been isolated from rabbit (Oryctolagus cuniculus) muscle. Its primary structure has been determined from a study of its tryptic peptides and of overlapping peptides generated by limited tryptic digestion and by chymotryptic and thermolytic digestions of the protein. The amino acid sequence so obtained is considered in comparison with those known for other parvalbumin and for rabbit troponin C. (+info)A three-dimensional construction of the active site (region 507-749) of human neutral endopeptidase (EC.3.4.24.11). (6/552)
A three-dimensional model of the 507-749 region of neutral endopeptidase-24.11 (NEP; E.C.3.4.24.11) was constructed integrating the results of secondary structure predictions and sequence homologies with the bacterial endopeptidase thermolysin. Additional data were extracted from the structure of two other metalloproteases, astacin and stromelysin. The resulting model accounts for the main biological properties of NEP and has been used to describe the environment close to the zinc atom defining the catalytic site. The analysis of several thiol inhibitors, complexed in the model active site, revealed the presence of a large hydrophobic pocket at the S1' subsite level. This is supported by the nature of the constitutive amino acids. The computed energies of bound inhibitors correspond with the relative affinities of the stereoisomers of benzofused macrocycle derivatives of thiorphan. The model could be used to facilitate the design of new NEP inhibitors, as illustrated in the paper. (+info)The compact conformation of fibronectin is determined by intramolecular ionic interactions. (7/552)
Fibronectin exists in a compact or extended conformation, depending upon environmental pH and salt concentration. Using recombinant fragments expressed in bacteria and baculovirus, we determined the domains responsible for producing fibronectin's compact conformation. Our velocity and equilibrium sedimentation data show that FN2-14 (a protein containing FN-III domains 2 through 14) forms dimers in low salt. Experiments with smaller fragments indicates that the compact conformation is produced by binding of FN12-14 of one subunit to FN2-3 of the other subunit in the dimer. The binding is weakened at higher salt concentrations, implying an electrostatic interaction. Furthermore, segment FN7-14+A, which contains the alternatively spliced A domain between FN11 and 12, forms dimers, whereas FN7-14 without A does not. Segment FN12-14+A also forms dimers, but the isolated A domain does not. These data imply an association of domain A with FN12-14, and the presence of A may favor an open conformation by competing with FN2-3 for binding to FN12-14. (+info)Insertion of atToc34 into the chloroplastic outer membrane is assisted by at least two proteinaceous components in the import system. (8/552)
Toc34 is a member of the outer membrane translocon complex that mediates the initial stage of protein import into chloroplasts. Toc34, like most outer membrane proteins, is synthesized in the cytosol at its mature size without a cleavable transit peptide. The majority of outer membrane proteins do not require thermolysin-sensitive components on the chloroplastic surface or ATP for their insertion into the outer membrane. However, different results have been obtained concerning the factors required for Toc34 insertion into the outer membrane. Using an Arabidopsis homologue of pea Toc34, atToc34, we show that the insertion of atToc34 was greatly reduced by thermolysin pretreatment of chloroplasts as assayed either by protease digestion or by alkaline extraction. The insertion was also dependent on the presence of ATP or GTP. A mutant of atToc34 with the GTP-binding domain deleted still required ATP for optimal insertion, indicating that ATP was used by other protein components in the import system. The ATP-supported insertion was observed even in thermolysin-pretreated chloroplasts, suggesting that the protein component responsible for ATP-stimulated insertion is a different protein from the thermolysin-sensitive component that assists atToc34 insertion. (+info)
Munin: Eksperimentell in vitro screening og molekylær dokking av forbindelser med mulig hemmende effekt på Thermolysin og...
Kinetic study of thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-phenylalanyl-L-leucine ethyl ester in an ethyl...
Membrane protein shaving with thermolysin can be used to evaluate topology predictors
A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from...
RCSB PDB
- 1TRL: NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316 OF THERMOLYSIN: A DIMER FORMED BY SUBUNITS...
RCSB PDB
- 1HYT: RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS...
PDB-1fjq: THERMOLYSIN (70% ACETONE SOAKED CRYSTALS) - Yorodumi
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Thermolysin
However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis. Thermolysin is ... Like all bacterial extracellular proteases thermolysin is first synthesised by the bacterium as a pre-proenzyme. Thermolysin is ... Thermolysin has a T50 value of 86.9 °C, making it the most thermo stable member of the TLP family. Studies on the contribution ... Thermolysin has a molecular weight of 34,600 Da. Its overall structure consists of two roughly spherical domains with a deep ...
Brian Matthews (biochemist)
Kresge, Nicole; Simoni, Robert D.; Hill, Robert L. (2009). "Structural Studies of Thermolysin: the Work of Brian W. Matthews". ... Matthews BW, Colman PM, Jansonius JN, Titani K, Walsh KA, Neurath H (1972). "Structure of thermolysin". Nature New Biology. 238 ... He also solved early structures of the thermophilic bacterial enzyme thermolysin, the helix-turn-helix DNA-binding ...
NLN (gene)
The catalytic site is contained within a thermolysin-like region found in many metallopeptidases and located in the domain near ... Matthews BW, Weaver LH, Kester WR (December 1974). "The conformation of thermolysin". The Journal of Biological Chemistry. 249 ...
Phosphoramidon
It is an inhibitor of the enzyme thermolysin, of the membrane metallo-endopeptidase, and of the endothelin converting enzyme. ... "Binding between thermolysin and its specific inhibitor, phosphoramidon". Journal of Biochemistry. 95 (2): 529-34. PMID 6715312 ...
Brian S. Hartley
Partial proteolysis with thermolysin". Biochemical Journal. 289: 201-208. doi:10.1042/bj2890201. PMC 1132150. PMID 8424759. ...
Fast parallel proteolysis
The protease thermolysin can be fully inactivated by EDTA. This feature of thermolysin makes FASTpp compatible with subsequent ... in a thermal gradient PCR cycler to different maximal temperatures in presence of the thermostable protease thermolysin (see ...
Microbial collagenase
"Circular dichroism comparative studies of two bacterial collagenases and thermolysin". Biochimica et Biophysica Acta (BBA) - ...
Talopeptin
It is a known reversible inhibitor of thermolysin and is expected to inhibit other metalloproteinases. Chemically, talopeptin ... Kitagishi, Keiko; Hiromi, Keitaro (1984). "Inhibitory spectrum of talopeptin (MKI), a specific inhibitor of thermolysin". ... "Equilibrium study on the binding between thermolysin and Streptomyces metalloprotease inhibitor, talopeptin (MKI)". Journal of ...
MMP3
Alternatively, it has been shown for thermolysin (another metalloproteinase) that the amide product can be released in its ... Hangauer DG, Monzingo AF, Matthews BW (Nov 1984). "An interactive computer graphics study of thermolysin-catalyzed peptide ... "A theoretical study of the mechanism for peptide hydrolysis by thermolysin". Journal of Biological Inorganic Chemistry. 7 (3): ...
Ecadotril
Thermolysin complexed with the inhibitor (S)-thiorphan are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 (also ... The peptidase domain for members of this family also contains a bacterial member and resembles that of thermolysin the ... "Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin". Biochemistry. 28 (4): ... predicted active site residues for members of this family and thermolysin occur in the motif HEXXH. ...
Thermostability
April 1997). "Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond". The Journal of Biological ...
Dispase
2006). "A quenched fluorescent dipeptide for assaying dispase- and thermolysin-like proteases". Analytical Biochemistry. 352 (1 ...
Silanol
Some silanediols and silanetriols inhibit hydrolytic enzymes such as thermolysin and acetylcholinesterase. Literally, silanol ...
Endopeptidase
Thermolysin - cuts before Ile, Met, Phe, Trp, Tyr, or Val, unless preceded by Pro. Sometimes cuts after Ala, Asp, His or Thr. ...
Astacin
The overall topology of this domain is shared by the archetypal zinc-endopeptidase thermolysin. Astacin protease domains also ... the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the ... The protein fold of the peptidase domain for members of this family resembles that of thermolysin, ... molecular structure and comparison with thermolysin". Journal of Molecular Biology. 229 (4): 945-68. doi:10.1006/jmbi.1993.1098 ...
Peptide deformylase
"Substrate recognition and selectivity of peptide deformylase Similarities and differences with metzincins and thermolysin". J. ...
Alice Vrielink
Structural and conformational energy studies of ligands of angiotensin converting enzyme and thermolysin (Thesis). Ottawa: ...
Ilomastat
Grobelny D, Poncz L, Galardy RE (August 1992). "Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas ... Examples of enzymes that ilomastat inhibit include rabbit MMP9, thermolysin, peptide deformylase, and anthrax lethal factor ...
Decellularization
Lipases, thermolysin, galactosidase, nucleases, and trypsin have all been used in the removal of cells. After a cell is lysed ...
Matrix metalloproteinase
Kester WR, Matthews BW (1977). "Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for ...
Bacillolysin
This enzyme catalyses the following chemical reaction Similar, but not identical, to that of thermolysin This enzyme is present ... "The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral ... from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin". ...
Dactylysin
Joudiou C, Carvalho KM, Camarao G, Boussetta H, Cohen P (June 1993). "Characterization of the thermolysin-like cleavage of ...
Transition state analog
Thermolysin is an enzyme produced by Bacillus thermoproteolyticus that catalyses the hydrolysis of peptides containing ... Holden HM, Tronrud DE, Monzingo AF, Weaver LH, Matthews BW (December 1987). "Slow- and fast-binding inhibitors of thermolysin ... mechanism starts form the small peptide molecule and replaces the zinc binding water molecule towards Glu143 of thermolysin. ...
Thermal shift assay
However, commercially available thermolysin is dependent on calcium ions for activity and denatures itself just above 85 ... In fast parallel proteolysis the researcher adds a thermostable protease (thermolysin) and takes out samples in parallel upon ... FastPP exploits that proteins become increasingly susceptible to proteolysis when unfolded and that thermolysin cleaves at ... showed that stabilization by ligand binding could impart resistance to proteolytic digestion with thermolysin. Protection ...
Thermoase
... may refer to: Subtilisin, an enzyme Thermolysin, an enzyme This disambiguation page lists articles associated with ...
Kenneth M. Merz Jr.
Free Energy Perturbation Simulations of the Inhibition of Thermolysin: Prediction of the Free Energy of Binding of a New ... Merz, Kenneth M.; Kollman, Peter A. (1989-07-01). "Free energy perturbation simulations of the inhibition of thermolysin: ...
Candoxatril
Holland, D.R.; Barclay, P.L.; Danilewicz, J.C.; Matthews, B.W.; James, K. (January 1994). "Inhibition of thermolysin and ... the gluzincins a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, Zincin is the ... neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor ...
Vibriolysin
... which distinguished this enzyme from thermolysin This thermostable enzyme is isolated from Vibrio proteolyticus. Holmquist B, ...
Oligopeptidase
... involvement of a thermolysin-like metalloendopeptidase (enkephalinase), angiotensin-converting enzyme, and other unidentified ...
Protease inhibitor (biology)
It has 102 amino acid residues with two disulphide bridges and specifically inhibits metalloproteinases such as thermolysin, ...
An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis: purification, characterization, and gene cloning ...
An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis: purification, characterization, and gene cloning ... An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis: purification, characterization, and gene cloning ... The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. VFP, like V. vulnificus protease, ... sensitivity to chelating agents or competitive inhibitors for thermolysin-like metalloproteases, and the substrate specificity ...
Expression, purification and identification of a thermolysin-like protease, neutral protease I, from Aspergillus oryzae with...
Expression, purification and identification of a thermolysin-like protease, neutral protease I, from Aspergillus oryzae with ... Expression, purification and identification of a thermolysin-like protease, neutral protease I, from Aspergillus oryzae with ... All of the evidence indicated that this protease is a thermolysin-like peptidase. ...
EC 3.4.24.27 - thermolysin
... 3D structures of EC 3.4.24.27 - thermolysin in Protein Data Bank. updated: 6 January 2022, 2:15 ... 5js3: Thermolysin in Complex with Jc114.. *5fxn: Structure of Thermolysin Solved by Sad from Data Collected by Direct Data ... 4d9w: Thermolysin in Complex with Ubtln32. *3zi6: Structure of Thermolysin Solved by Sad from Data Collected by Direct Data ... 5uu7: Tetragonal Thermolysin (295 K) in The Presence of 50% Mpd. *5un3: Tetragonal Thermolysin (295 K) in The Presence of 50% ...
Processing L498 thermolysin - cctbx xfel
Indexing the thermolysin data. A configuration file for processing the primary lattices in the thermolysin data is shown below ... thermolysin user = db_user } output { n_bins = 10 prefix = L498_thermolysin } scaling { algorithm = mark0 mtz_file = 2tli.mtz ... L498_thermolysin.mtz. ). Note that the version of merging programs from 28 March, 2013 do not not report the Rsplit statistic. ... To merge the thermolysin data, save the suitably modified configuration file to e.g. L498-merge.phil. , and run ...
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Publication Detail
Recombinant Human Kallikrein 7 Protein, CF (2624-SE): Novus Biologicals
When activated by thermolysin, it displays enzymatic activity towards a fluorogenic synthetic peptide described in the Activity ... Combine equal volumes of 200 μg/mL rhKLK7 and 20 μg/mL Thermolysin. ... Dilute Thermolysin to 20 μg/mL in Activation Buffer.. * ... Thermolysin) (Catalog # 3097-ZN) *EDTA (Sigma, Catalog # E-4884 ...
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Developing epithelia were dissected from associated mesenchyme using thermolysin and established in vitro as intact cochlear ... To examine this possibility, apical E12.5 epithelial pieces were treated with thermolysin and dissected away from their ... Finally, some E12.5 cochleas were treated with thermolysin to disconnect the cochlear epithelium from the underlying mesenchyme ... For coculture experiments, E12.5 cochleas were isolated, treated with thermolysin, and isolated into epithelial and mesenchymal ...
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MeSH Browser
Thermolysin S Narrower Concept UI. M0021306. Registry Number. 0. Terms. Thermolysin S Preferred Term Term UI T040591. Date10/01 ... Thermolysin Preferred Term Term UI T040590. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1971). ... Thermolysin Preferred Concept UI. M0021305. Registry Number. EC 3.4.24.27. Scope Note. A thermostable extracellular ... Thermolysin. Tree Number(s). D08.811.277.656.300.480.827. D08.811.277.656.675.374.827. Unique ID. D013820. RDF Unique ...
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Protease2
- Thermolysin is a protease isolated from hot springs. (netsolhost.com)
- Selected peptides obtained from digests with staphylococcal protease, thermolysin, and chymotrypsin provided the information necessary to align the tryptic peptides and the cyanogen bromide fragments. (nih.gov)
Metalloprotease2
- We determined association and dissociation rate constants for 17 inhibitors of the metalloprotease thermolysin by surface plasmon resonance spectroscopy and correlated kinetic data with high-resolution crystal structures in complex with the protein. (unibas.ch)
- The 3.8 angstrom structure of a complex with a CSIM tetrapeptide showed that the mode of binding of the substrate resembles that of an insect metalloprotease inhibitor in thermolysin. (ox.ac.uk)
Inhibitors3
- Interference with this retrograde induced-fit mechanism results in variation of the residence time of thermolysin inhibitors by a factor of 74 000. (unibas.ch)
- The binding sites of Calcium atom in the Dipeptide Inhibitors of Thermolysin (pdb code 2wi0 ). (atomistry.com)
- Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin To Be Published . (atomistry.com)
Proteolytic Enzymes1
- Several proteolytic enzymes including trypsin, papain and thermolysin potently inactivated PCP receptors. (elsevier.com)
Residue1
- The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. (embl.de)
19981
- Beynon, R.J. & Beaumont, A. (1998) M4 proteases: thermolysins. (phbuffers.org)
Inhibitor1
- LA, a known pseudopeptidic inhibitor of thermolysin, which blocks the conformational transition of Asn112. (unibas.ch)
Peptide1
- Effect of water and enzyme concentration on thermolysin-catalysed solid-solid peptide synthesis. (hw.ac.uk)
Inhibitors3
- Slow-and Fast-binding Inhibitors of Thermolysin Display Different Modes of Binding. (me.uk)
- Binding of N-carboxymethyl Dipepetide Inhibitors to Thermolysin Determined by X-ray Crystallography. (me.uk)
- In the present study we have synthesised a series of hydroxamate derivatives and validated the compounds as inhibitors of the M4 enzymes thermolysin and pseudolysin, and the endogenous metalloproteinases ADAM-17, MMP-2 and MMP-9 using experimental binding studies and molecular modelling. (uit.no)
Trypsin1
- Cycloviolacin O13, O14, O16 and O24 were tested for their stability against proteolytic degradation by pepsin, trypsin and thermolysin.No degradation by proteases was observed for any of the cyclotides tested following 6 hours of incubation with enzymes, while the linear control peptide was completely degraded in less than 5 minutes. (cybase.org.au)
Proteinase1
- Active peptides were obtained by hydrolysis of whey proteins with thermolysin and proteinase enzymes from B. subtilis. (cambridge.org)
Proteolysis3
- Limited proteolysis using thermolysin can be used to study the heterodimerization of these human AHR and ARNT proteins. (nih.gov)
- All mutants investigated show similar stability profiles to wild-type CRP with respect to thermolysin proteolysis as a function of temperature. (nih.gov)
- Proteolysis was performed with 2 ng of thermolysin at area heat range for 20 min, and ended with 1 L of 0.5 M EDTA (pH 8.0). (southpadremaps.com)
Proteolytic degradation1
- ASCT2 is protected from proteolytic degradation by thermolysin (TLN) in the presence of increasing concentrations of V-9302 (veh = -, + = 50 100 homology model of human ASCT2 (hASCT2)16. (ly2603618.com)
24.272
Alcalase1
- Dianabol UPsteroid for the after abruptly quitting cycles designed to harden the were prepared by treatment with five different proteases namely alcalase, thermolysin, neutrase, flavourzyme, and PTN. (wahoowebsite.com)
Hinge-bendin1
- D.M.F. van Aalten , A. Amadei, A.B.M. Linssen, V.G.H. Eijsink, G. Vriend, and H.J.C. Berendsen, "The essential dynamics of thermolysin - confirmation of the hinge-bending motion and comparison of simulations in vacuum and water", Proteins (1995), 22, 45-54. (google.com)
Peptides1
- 17. Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II. (nih.gov)
Catalyst1
- Thermolysin as a catalyst in the synthesis of di-and tripeptides containing aspa. (usp.br)
Substitutions1
- Structural analysis of zinc substitutions in the active site of thermolysin. (expasy.org)
Sequence1
- The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. (nih.gov)
Data2
- The thermolysin data for the cctbx.xfel paper was processed around March 28, 2013. (lbl.gov)
- To meaningfully process the thermolysin diffraction data, an average of all the images in a dark run -a run without any X-rays impinging on the detector-must be subtracted from the individual diffraction images. (lbl.gov)
Activity1
- The importance of Glu234 in the catalytic activity of the light chain, possibly analogous to Glu143 of thermolysin, was examined using site-directed mutagenesis. (nih.gov)