A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
Peptides composed of two amino acid units.
Serum globulins with high molecular weight. (Dorland, 28th ed)
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A brominating agent that replaces hydrogen atoms in benzylic or allylic positions. It is used in the oxidation of secondary alcohols to ketones and in controlled low-energy brominations. (From Miall's Dictionary of Chemistry, 5th ed; Hawley's Condensed Chemical Dictionary, 12th ed,).
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.
The process of cleaving a chemical compound by the addition of a molecule of water.
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.
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.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
The rate dynamics in chemical or physical systems.

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)

To substrater ble brukt i de eksperimetelle studiene. De er referet til som Bradykinin-lignende substrat og AGLA substrat i oppgaven. De eksperimentelle forsøkene gav Km verdi for Bradykinin lignende substrat for Thermolysin fra Bacillus thermoproteolyticus eubakterie på 17.7 +/- 4.3 μM og Pseudolysin fra Pseudomonas aeruginosa på 7.4 +/- 1.3 μM. For AGLA substrat ble Km for Thermolysin målt til 67.7 +/- 10.5 μM, mens for Pseudolysin ble Km målt til 124.8 +/- 22.9 μM. Seksten forbindelser fra en tidligere virtual screening studie av Maybridge databasen viste ingen hemmende effekt hverken på verken Thermolysin eller Pseudolysin. Både under preinkubering av hemmere og under alle forsøk var pH 7.3, mens temperaturen var 37 °C. Av totalt 50 forbindelser (42+8) fra samarbeidspartnere i Italia, viste forbindelse FF33 en IC50 på 754 nM mot Thermolysin og IC50 på 2.28 μM mot Pseudolysin. Forbindelse VDL22 hadde en IC50 på 11,14 μM mot Thermolysin. Forbindelse SM434 viste seg å ...
TY - JOUR. T1 - Kinetic study of thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-phenylalanyl-L-leucine ethyl ester in an ethyl acetate saturated aqueous system. AU - Nam, K.. AU - Lee, C. K.. AU - Jeong, S. W.. AU - Chi, Y. M.. PY - 2001. Y1 - 2001. N2 - The kinetics of the thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-phenylalanyl-L-leucine ethyl ester (Z-Phe-LeuOEt) from N-(benzyloxycarbonyl)-L-phenylalanine (Z-Phe) and L-leucine ethyl ester (LeuOEt) in an ethyl acetate saturated aqueous system in a batch operation were studied. The kinetics for the synthesis of Z-Phe-LeuOEt were expressed using a rate equation for the rapid equilibrium random bireactant mechanism. The four kinetic constants involved in the rate equation were determined numerically by the quasi-Newton method so as to fit the calculated results with the experimental data. Within the pH and temperature range examined, the kcat value for the synthesis of Z-Phe-LeuOEt reached a maximum at pH 7.0 and 45°C, ...
Topology analysis of membrane proteins can be obtained by enzymatic shaving in combination with MS identification of peptides. Ideally, such analysis could provide quite detailed information about the membrane spanning regions. Here, we examine the ability of some shaving enzymes to provide large-scale analysis of membrane proteome topologies. To compare different shaving enzymes, we first analyzed the detected peptides from two over-expressed proteins. Second, we analyzed the peptides from non-over-expressed Escherichia coli membrane proteins with known structure to evaluate the shaving methods. Finally, the identified peptides were used to test the accuracy of a number of topology predictors. At the end we suggest that the usage of thermolysin, an enzyme working at the natural pH of the cell for membrane shaving, is superior because: (i) we detect a similar number of peptides and proteins using thermolysin and trypsin; (ii) thermolysin shaving can be run at a natural pH and (iii) the ...
TY - JOUR. T1 - A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein. AU - Bargonetti, Jill. AU - Manfredi, James J.. AU - Chen, Xinbin. AU - Marshak, Daniel R.. AU - Prives, Carol. PY - 1993. Y1 - 1993. N2 - p53 is a sequence-specific DNA-binding oligomeric protein that can activate transcription from promoters bearing p53-binding sites. Whereas the activation region of p53 has been identified within the amino terminus, the location of the specific DNA-binding domain has not been reported. Thermolysin treatment of p53 protein generates a stable protease-resistant fragment that binds with marked specificity to p53 DNA-binding sites. Amino-terminal sequencing of the fragment located the thennolysin cleavage site to residue 91. Because the fragment does not contain the cdc2 phosphorylation site at Ser-315, we conclude that the the site-specific DNA-binding domain of p53 spans ...
1TRL: NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure.
1HYT: Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A.
The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with EMD- (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force. (see PDBe EMDB page ...
Looking for Inouye, Kaoru? Find out information about Inouye, Kaoru. 1835-1915, Japanese statesman. He was a leader of the antiforeign movement in his native Choshu fief, and helped set fire to the British legation in Edo in... Explanation of Inouye, Kaoru
Variants of this enzyme have been found in species of Bacillus including B. subtilis [1,6], B. amyloliquefaciens [5], B. megaterium (megateriopeptidase, [2]), B. mesentericus [10], B. cereus [3,8,9] and B. stearothermophilus [7]. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4 ...
SWISS-MODEL Template Library (SMTL) entry for 1hyt.1. RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS RELATION TO THE COMPLEX WITH CARBOXYPEPTIDASE A
SWISS-MODEL Template Library (SMTL) entry for 5tac.1. Conformational Sampling Differences across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin
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TY - JOUR. T1 - 3D-QSAR of Angiotensin-Converting Enzyme and Thermolysin Inhibitors. T2 - A Comparison of CoMFA Models Based on Deduced and Experimentally Determined Active Site Geometries. AU - DePriest, Scott A.. AU - Mayer, Dorica. AU - Naylor, Christopher B.. AU - Marshall, Garland R.. AU - Mayer, Dorica. AU - Naylor, Christopher B.. PY - 1993/6/1. Y1 - 1993/6/1. N2 - The ability of comparative molecular field analysis (CoMFA), a three-dimensional, quantitative structure-activity relationship (3-D QSAR) paradigm, to predict the activity of inhibitors of angiotensin-converting enzyme (ACE) and thermolysin was examined. Correlations derived from computationally and experimentally determined alignment rules were compared. The correlations derived for the ACE series using alignment rules determined from a systematic conformational search (Mayer, D.; Naylor, C. B.; Motoc, I.; Marshall, G. R. J. Comput.-Aided Molec. Des. 1987, 1, 3-16) were comparable to those derived for the thermolysin ...
Ungaro, V. A., Fairbanks, J. P. A., Rossi, L. M., & Machini, M. T. (2017). Thermolysin immobilized on Fe IND. 3O IND. [email protected] nanoparticle: preparation and characterization of a new recoverable biocatalyst. In Proceedings. Durham: International Union of Pure and Applied Chemistry (IUPAC). Recuperado de http://www.neopixdmi.com.br/@mci/iupac2017 ...
Hereditary mutations in the transforming growth factor beta induced (TGFBI) gene cause phenotypically distinct corneal dystrophies characterized by protein deposition in cornea. We show here that the Arg555Trp mutant of the fourth fasciclin 1 (FAS1-4) domain of the protein (TGFBIp/keratoepithelin/betaig-h3), associated with granular corneal dystrophy type 1, is significantly less susceptible to proteolysis by thermolysin and trypsin than the WT domain. High-resolution liquid-state NMR of the WT and Arg555Trp mutant FAS1-4 domains revealed very similar structures except for the region around position 555. The Arg555Trp substitution causes Trp555 to be buried in an otherwise empty hydrophobic cavity of the FAS1-4 domain. The first thermolysin cleavage in the core of the FAS1-4 domain occurs on the N-terminal side of Leu558 adjacent to the Arg555 mutation. MD simulations indicated that the C-terminal end of helix alpha3 containing this cleavage site is less flexible in the mutant domain, ...
Enzymatic hydrolysis of proteins is used to improve nutritional and functional properties of many foods. The desired degree of hydrolysis (DH) depends on food application. Effective hydrolysis requires optimal hydrolysis conditions for both the enzyme and the substrate protein. This study aimed to hydrolyze the oat globulins (OG) effectively under different conditions. Our first goal was to maximise the OG solubility and then to hydrolyze OG under optimised conditions. The solubility of isolated OG in Na-phosphate solutions containing 0 1 M NaCl was determined. Globulins were subjected to single-enzyme hydrolysis with either subtilisin, thermolysin or pepsin. In addition, OG were degraded in two-stage hydrolysis first with pepsin and then either with subtilisin or thermolysin. The hydrolysates were analysed by SDS-PAGE and DH was quantified with the OPA method. The solubility of OG increased when NaCl was added at pH 5 10. Under more acidic conditions the solubility, however, decreased with ...
0047] The above characteristics are optionally taken into account when producing a protein with reduced or improved enzymatic activity. Illustratively, substitutions in a substrate binding site, exosite, cofactor binding site, catalytic site, or other site in an enzyme may alter the activity of the enzyme toward a substrate. In considering such substitutions the sequences of other known naturally occurring or non-naturally occurring proteins may be taken into account. Illustratively, mutations of L134R and S320A in Bacillis licheniformis α-amylase improve the catalytic activity of the enzyme in acidic conditions 14-fold. Liu, et al., Appl Microbiol Biotechnol, 2008; 80:795-803. As another example, a corresponding mutation to that of Asp213 in thermolysin is operable such as that done by Mild, Y, et al., Journal of Molecular Catalysis B: Enzymatic, 1996; 1:191-199. Optionally, a substitution in thermolysin of L144S alone or along with substitutions of G8C/N60C/S65P are operable to increase the ...
Aceetate [ ACEETATE, n. [See Acid.] In chimistry, a neutral salt formed by the union of the acetic acid, or radical vinegar, with any salifiable base, as with earths, metals, and alkalies; as the acetate of alumine, of lime, or of copper. ]
Is able to inhibit all four classes of proteinases by a unique trapping mechanism. This protein has a peptide stretch, called the bait region which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases ...
Lysates from logarithmic growth phase T. brucei (2.5 × 108 cells) isolated from infected rats and from the logarithmic growth and late stationary phase (8.3 and 5.4 × 107 cells, respectively) organisms isolated from bloodstream-form cultures were prepared by hypotonic lysis using double-distilled water containing a cocktail of reversible and irreversible inhibitors (one tablet in 25 ml) of pancreas extract, pronase, thermolysin, chemotrypsin, trypsin, and papain (Complete™; Roche Diagnostics). For PG production from AA, we used the reaction mixture described by Ujihara et al. (21) with the following modifications: 100 mM sodium phosphate, pH 7.0, 2 μM hematin, 5 mM tryptophan, 1 mM AA, and 300 μl of the respective T. brucei lysates in a final volume of 500 μl. The mixture was incubated at 37°C for 30 min, and then the reaction was stopped by addition of 100 μl of 1 M HCl and 6 vol of cold ethyl acetate.. For PGF2α synthesis from PGH2, a standard reaction mixture that contained 100 mM ...
Methyl, Ethyl, Propyl, Butyl: Futile But Not for Water, as the Correlation of Structure and Thermodynamic Signature Shows in a Congeneric Series of Thermolysin Inhibitors ...
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Maybe Im missing something. I hook up my FBV3 to my computer and run Line6 FBV Control. changes I make on the screen are reflected immediately, on the pedal, which is fine. When I disconnect the USB and hook the FBV3 up to my Spider V 240, the settings revert back to original. Is there a save to ...
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Enzymatische Spaltung nativer cystinhaltiger Polypeptide durch Thermolysin (E.S. 3.4.4.), II: Vergleich von Thermolysin mit α-Protease aus Crotalus atrox-Gift und Subtilisin (Enzymic hydrolysis of native cystine-containing polypeptides with thermolysin. II. Comparison of thermolysin with α-protease from Crotalus atrox poison and subtilisin) ...
Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of thermolysin and bacillolysin [1]. A zinc metallopeptidase in family M4 (thermolysin family). Formerly included in EC 3.4.24.4 ...
2-{[3-(3,4-Dihydroxyphenyl)acryloyl]amino}benzoic acid | C16H13NO5 | CID 54039925 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more.
Rabbit monoclonal antibody raised against a human MKI67IP peptide using ARM Technology. A synthetic peptide of human MKI67IP is used for rabbit immunization.Customer or Abnova will decide on the preferred peptide sequence. (H00084365-K) - Products - Abnova
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation which is usually zinc, but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys. At least one other residue is required for catalysis, which may play an electrophillic role. Many metalloproteases contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site [(PUBMED:7674922)]. 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 ...
Inouye et al used some simple questions to screen patients for their level of social support. The authors are from Yale University in New Haven, Connecticut.
In 1 we will find the explanation of clinical results obtained by intravenous CH1 injections, even if the blood pH did not change.. In 2 we find the reason for clinical results obtained by increasing neutral salts intake. Ambard gives the following reaction:. NaCl+2CO3 NaHCO3+HCl. Whereas this reaction gives birth to infinitesimal quantities of HCl, if it takes place in the presence of albumin, the acid will impregnate the albumin and a new quantity of NaCl can be decomposed and liberates a new fraction of chlorine.. Here then we have first of all a new characteristic of proteins. It is therefore possible to perceive, that though the proteins are charged with acid, the medium many manifest a neutral reaction. Chabanier and Lobo-Onell have shown that even an increase of acid, producing an acidemia (of the medium), will allow the albumins to discharge themselves of HCl if the neutral salt content is diminished. It is possible, therefore, to have an acidemia (of the medium) and an alkalosis (of the ...
In well-known methods of estimating rates of irreversible disposal (utilization) in vivo the rates are calculated from the areas to infinity under specific radioactivity-time (S-t) or quantity-of-label-time (q-t) curves obtained by measurements on samples of plasma after intravenous injection of labelled substrate. The errors in the calculated rates are mostly those of the estimates of the areas. These errors are of two kinds: random, caused by the variances of the values of S or q, and systematic, caused by differences between the curves used to interpolate between these values and the true curves. A rigorous method is given for calculating the random errors from the variances of the values of S or q, and is applied to choosing the best times to sample the plasma from small animals from which few plasma samples can be taken. A procedure for estimating systematic errors is also given. Programs in BASIC language to carry out the calculations are deposited as Supplementary Publication SUP 50058 (5 ...
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It has been designed as a DIRECT REPLACEMENT in units such as the ZR33, Magnum Club Smoke, AF1 MkI, Magnum 2000 DMX interface, ZR12 DMX interface etc ...
The Liberase projects showed that collagenase and neutral protease were the enzymes required for the release of islets from human pancreatic tissue. Liberase contains purified class I and class II C histolyticum collagenase, and thermolysin or Dispase. Different formulations and doses were used to isolate cells from different tissues.. The identification of the C. histolyticum genes and corresponding protein domain structures of class I and class II collagenase provided new insights into the mechanism of enzyme-mediated tissue dissociation. Both classes of collagenase contain four protein domains: a large catalytic domain that cuts native collagen or gelatin, linking domain(s) (no known function), and collagen binding domain(s). Intact class I has one catalytic domain, a linking domain, and two collagen binding domains whereas intact class II has a catalytic domain, two linking domains, and one collagen binding domain. Only those forms of collagenase containing a catalytic domain and at least ...
The Liberase projects showed that collagenase and neutral protease were the enzymes required for the release of islets from human pancreatic tissue. Liberase contains purified class I and class II C histolyticum collagenase, and thermolysin or Dispase. Different formulations and doses were used to isolate cells from different tissues.. The identification of the C. histolyticum genes and corresponding protein domain structures of class I and class II collagenase provided new insights into the mechanism of enzyme-mediated tissue dissociation. Both classes of collagenase contain four protein domains: a large catalytic domain that cuts native collagen or gelatin, linking domain(s) (no known function), and collagen binding domain(s). Intact class I has one catalytic domain, a linking domain, and two collagen binding domains whereas intact class II has a catalytic domain, two linking domains, and one collagen binding domain. Only those forms of collagenase containing a catalytic domain and at least ...
Here we present the synthesis and post-polymerisation modification of poly(acryloyl hydrazide), a versatile scaffold for the preparation of functional polymers: poly(acryloyl hydrazide) was prepared from commercially available starting materials in a three step synthesis on a large scale, in good yields and high purity. Our synthetic approach included the synthesis of a Boc-protected acryloyl hydrazide, the preparation of polymers via RAFT polymerisation and the deprotection of the corresponding Boc-protected poly(acryloyl hydrazide). Post-polymerisation modification of poly(acryloyl hydrazide) was then demonstrated using a range of conditions for both hydrophilic and hydrophobic aldehydes. These experiments demonstrate the potential of poly(acryloyl hydrazide) as a scaffold in the synthesis of functional polymers, in particular those applications where in situ screening of the activity of the functionalised polymers may be required (e.g. biological applications ...
Page contains details about poly(D-α-tocopheryl polyethylene glycol 1000-2,2-bis(acryloyloxymethyl)propionate-co-N,N-bis(acryloyl)cystamine-co-1,6-hexanediol diacrylate-co-piperazine) nanoparticles in phosphate-buffered saline (pH 6.5) . It has composition images, properties, Characterization methods, synthesis, applications and reference articles : nano.nature.com
0022]The (meth)acryloyl groups in the linear (meth)acryloyl-containing compound of the present invention exist at parts of side chains relative to the molecular chain having the longest coupling length in a single molecule, and it is indispensable from the standpoint of satisfactory hardenability and sensitivity that an average of 3 or more be contained in a single molecule. With respect to the pertinent (meth)acryloyl groups, by selecting the structural units which configure the straight-chain portion, it is possible to easily adjust their concentration in a single molecule, that is, the molecular weight per (meth)acryloyl group. For example, when using residue excluding 2 hydroxyl groups from bisphenol as A in the aforementioned general formula (1) as described below, it is possible to obtain approximately the same concentration as with conventional bifunctional epoxy(meth)acrylate, and to have crosslink density in an appropriate range while having multifunctionality, thereby obtaining ...
Note: For nodular (composite) ganglioneuroblastomas with more than 1 nodule, degree of differentiation and mitotic-karyorrhectic index (MKI) must be given for each nodule. Please indicate the differentiation and MKI for the least favorable nodule in the checklist below. Classification of additional nodules can be described in the Comment. ...
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All text is © British Library Board and is available under a Creative Commons Attribution Licence, except where otherwise stated.. ...
All text is © British Library Board and is available under a Creative Commons Attribution Licence, except where otherwise stated.. ...
A SU-30 MKI combat jet belonging to the IAF crashed in the Pokhran firing range in Rajasthan during a firepower demonstration drill.
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I am 20 years old and have been with my boyfriend for 4 years. About a month ago we found out we were expecting. A few days later I was bleeding and went to the er, I was miscarrying. I later went back...
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 ...
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 ...
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 ...
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 ...
Partial proteolysis with thermolysin". Biochemical Journal. 289: 201-208. doi:10.1042/bj2890201. PMC 1132150. PMID 8424759. ...
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 ...
"Circular dichroism comparative studies of two bacterial collagenases and thermolysin". Biochimica et Biophysica Acta (BBA) - ...
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 ...
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): ...
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. ...
April 1997). "Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond". The Journal of Biological ...
2006). "A quenched fluorescent dipeptide for assaying dispase- and thermolysin-like proteases". Analytical Biochemistry. 352 (1 ...
Some silanediols and silanetriols inhibit hydrolytic enzymes such as thermolysin and acetylcholinesterase. Literally, silanol ...
Thermolysin - cuts before Ile, Met, Phe, Trp, Tyr, or Val, unless preceded by Pro. Sometimes cuts after Ala, Asp, His or Thr. ...
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 ...
"Substrate recognition and selectivity of peptide deformylase Similarities and differences with metzincins and thermolysin". J. ...
Structural and conformational energy studies of ligands of angiotensin converting enzyme and thermolysin (Thesis). Ottawa: ...
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 ...
Lipases, thermolysin, galactosidase, nucleases, and trypsin have all been used in the removal of cells. After a cell is lysed ...
Kester WR, Matthews BW (1977). "Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for ...
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". ...
Joudiou C, Carvalho KM, Camarao G, Boussetta H, Cohen P (June 1993). "Characterization of the thermolysin-like cleavage of ...
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. ...
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 ...
... may refer to: Subtilisin, an enzyme Thermolysin, an enzyme This disambiguation page lists articles associated with ...
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: ...
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 ...
... which distinguished this enzyme from thermolysin This thermostable enzyme is isolated from Vibrio proteolyticus. Holmquist B, ...
... involvement of a thermolysin-like metalloendopeptidase (enkephalinase), angiotensin-converting enzyme, and other unidentified ...
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 ... 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 ... All of the evidence indicated that this protease is a thermolysin-like peptidase. ...
... 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% ...
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 ...
Thermolysin: A. SMTL:PDB. SMTL Chain Id:. PDB Chain Id:. A. A ...
A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN ... A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN. ... Holland, D.R. et al., Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci. (1995) Release ...
THERMOLYSIN IN COMPLEX WITH INHIBITOR (JC67) - 5LVD , canSARS ... THERMOLYSIN IN COMPLEX WITH INHIBITOR (JC67) EXPRESSION SYSTEM( ...
THERMOLYSIN IN COMPLEX WITH INHIBITOR JC277 - 5N31 , canSARS ... THERMOLYSIN IN COMPLEX WITH INHIBITOR JC277 EXPRESSION SYSTEM(S ...
Thermolysin (+ other enzyme). 6. 3.8. 40. 18.7. 5. 5.0. ,0.01. Pulmozyme (+ other enzyme). 56. 35.2. 136. 63.6. 69. 69.0. ,0.01 ...
Limited proteolysis using thermolysin can be used to study the heterodimerization of these human AHR and ARNT proteins. ...
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 ...
1992) Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic ...
Selective binding of matrix metalloproteases MMP-9 and MMP-12 to inhibitor-assisted thermolysin-imprinted beads. RSC Advances, ...
Thermolysin activates equine lamellar hoof matrix metalloproteinases. J Comp Path 126: 9-16. ...
the N-terminal half of the structure is multihelical; the C-terminal half contains the thermolysin-like catalytic domain. ...
One in particular, a thermolysin-like metalloprotease, activates the bradykinin pathway, causing an increase in vascular ... a member of the thermolysin family. Infect Immun. 1998 Oct. 66(10):4851-5. [QxMD MEDLINE Link]. ...
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 ...
the N-terminal half of the structure is multihelical; the C-terminal half contains the thermolysin-like catalytic domain. ...
Thermolysin as a catalyst in the synthesis of di-and tripeptides containing aspa... ...
Liberase TL, TM and TH Research Grade contain collagenase I, II and the neutral protease thermolysin. Liberase DL and DH ...
Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II.. Miranda MT; Tominaga M. Int J Pept ...
Separation of Rat Epidermis and Dermis with Thermolysin to Detect Site-Specific Inflammatory mRNA and Protein ...
The importance of Glu234 in the catalytic activity of the light chain, possibly analogous to Glu143 of thermolysin, was ...
... the zinc site is analogous to those of zinc hydrolases such as thermolysin or bacterial carboxypeptidase A (Hall et al., 1995 ...
Detection and characterization of proteinase K-sensitive disease related prion protein with thermolysin. Biochem J 2008; 416: ...
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 ...
... thermolysin-like protease from geobacillus stearothermophilus as a test case. ACS Omega 3 (4), pp. 4148 - 4156 (2018) ...
They were then treated with pronase (1 mg/6-20 ml) at 31°C for 20-45 min and subsequently with thermolysin (1 mg/6-20 ml) under ... Drugs used in the experiments were gramicidin D, thermolysin, ethacrynic acid (Sigma, St. Louis, MO), pronase (Calbiochem, San ...
Aminopeptidase N from Escherichia coli is a M1 class aminopeptidase with the active-site region related to that of thermolysin ...
  • 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)
  • 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)
  • 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)
  • Several proteolytic enzymes including trypsin, papain and thermolysin potently inactivated PCP receptors. (elsevier.com)
  • 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)
  • Beynon, R.J. & Beaumont, A. (1998) M4 proteases: thermolysins. (phbuffers.org)
  • LA, a known pseudopeptidic inhibitor of thermolysin, which blocks the conformational transition of Asn112. (unibas.ch)
  • Effect of water and enzyme concentration on thermolysin-catalysed solid-solid peptide synthesis. (hw.ac.uk)
  • 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)
  • 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)
  • Active peptides were obtained by hydrolysis of whey proteins with thermolysin and proteinase enzymes from B. subtilis. (cambridge.org)
  • 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)
  • 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)
  • Thermolysin (e.c.3.4.24.27) Complexed with (2-sulphanyl-3- Phenylpropanoyl)-phe-tyr. (me.uk)
  • Thermolysin (e.c.3.4.24.27) Complexed with (2- Sulphanylheptanoyl)-phe-ala. (me.uk)
  • 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)
  • 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)
  • 17. Thermolysin as a catalyst in enzymatic synthesis of asparagine-containing peptides II. (nih.gov)
  • Thermolysin as a catalyst in the synthesis of di-and tripeptides containing aspa. (usp.br)
  • Structural analysis of zinc substitutions in the active site of thermolysin. (expasy.org)
  • The deduced amino acid sequence confirmed that VFP was a member of the thermolysin family. (nih.gov)
  • 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)
  • 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)