Aspartic Acid Endopeptidases
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
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.
Aspartic Acid Proteases
Amino Acid Sequence
A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.
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.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
PHEX Phosphate Regulating Neutral Endopeptidase
A membrane-bound metalloendopeptidase that may play a role in the degradation or activation of a variety of PEPTIDE HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Genetic mutations that result in loss of function of this protein are a cause of HYPOPHOSPHATEMIC RICKETS, X-LINKED DOMINANT.
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.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Proteins prepared by recombinant DNA technology.
Peptides composed of between two and twelve amino acids.
Sequence Homology, Amino Acid
Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Amino Acid Substitution
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Chromatography, High Pressure Liquid
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A biologically active tridecapeptide isolated from the hypothalamus. It has been shown to induce hypotension in the rat, to stimulate contraction of guinea pig ileum and rat uterus, and to cause relaxation of rat duodenum. There is also evidence that it acts as both a peripheral and a central nervous system neurotransmitter.
A 25-kDa peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC 22.214.171.124.
Serine Proteinase Inhibitors
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
Electrophoresis, Polyacrylamide Gel
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 126.96.36.199. (Formerly EC 188.8.131.52).
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Protein Structure, Tertiary
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Protein Processing, Post-Translational
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Atrial Natriuretic Factor
A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.
An enzyme that activates aspartic acid with its specific transfer RNA. EC 184.108.40.206.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
Protein Structure, Secondary
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Chromatography, Ion Exchange
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.
A nonapeptide messenger that is enzymatically produced from KALLIDIN in the blood where it is a potent but short-lived agent of arteriolar dilation and increased capillary permeability. Bradykinin is also released from MAST CELLS during asthma attacks, from gut walls as a gastrointestinal vasodilator, from damaged tissues as a pain signal, and may be a neurotransmitter.
Botulinum Toxins, Type A
Disciplines that apply sciences to law. Forensic sciences include a wide range of disciplines, such as FORENSIC TOXICOLOGY; FORENSIC ANTHROPOLOGY; FORENSIC MEDICINE; FORENSIC DENTISTRY; and others.
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
Sequence Homology, Nucleic Acid
Polymerase Chain Reaction
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
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.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Recombinant Fusion Proteins
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
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 220.127.116.11 and EC 18.104.22.168.
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 22.214.171.124.
2S Albumins, Plant
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
Amino Acid Motifs
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
Familial Hypophosphatemic Rickets
A hereditary disorder characterized by HYPOPHOSPHATEMIA; RICKETS; OSTEOMALACIA; renal defects in phosphate reabsorption and vitamin D metabolism; and growth retardation. Autosomal and X-linked dominant and recessive variants have been reported.
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.
Angiotensin-Converting Enzyme Inhibitors
A class of drugs whose main indications are the treatment of hypertension and heart failure. They exert their hemodynamic effect mainly by inhibiting the renin-angiotensin system. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc, when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. It may also have endopeptidase activity on some substrates. (From Enzyme Nomenclature, 1992) EC 126.96.36.199.
A type of ion exchange chromatography using diethylaminoethyl cellulose (DEAE-CELLULOSE) as a positively charged resin. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Sequence Analysis, DNA
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
Proenzymes secreted by chief cells, mucous neck cells, and pyloric gland cells, which are converted into pepsin in the presence of gastric acid or pepsin itself. (Dorland, 28th ed) In humans there are 2 related pepsinogen systems: PEPSINOGEN A (formerly pepsinogen I or pepsinogen) and PEPSINOGEN C (formerly pepsinogen II or progastricsin). Pepsinogen B is the name of a pepsinogen from pigs.
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.
A generic term used to describe a group of polypeptides with related chemical structures and pharmacological properties that are widely distributed in nature. These peptides are AUTACOIDS that act locally to produce pain, vasodilatation, increased vascular permeability, and the synthesis of prostaglandins. Thus, they comprise a subset of the large number of mediators that contribute to the inflammatory response. (From Goodman and Gilman's The Pharmacologic Basis of Therapeutics, 8th ed, p588)
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).
Seed Storage Proteins
The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.
A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 188.8.131.52.
Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase. (1/2015)We have developed a system for expression and purification of wild-type human T-cell leukemia virus type 1 (HTLV-1) proteinase to attain sufficient quantities for structural, kinetic, and biophysical investigations. However, similar to the human immunodeficiency virus type 1 (HIV-1) proteinase, HTLV-1 proteinase also undergoes autoproteolysis rapidly upon renaturation to produce two products. The site of this autoproteolytic cleavage was mapped, and a resistant HTLV-1 proteinase construct (L40I) as well as another construct, wherein the two cysteine residues were exchanged to alanines, were expressed and purified. Oligopeptide substrates representing the naturally occurring cleavage sites in HTLV-1 were good substrates of the HTLV-1 proteinase. The kinetic parameters kcat and Km were nearly identical for all the three enzymes. Although three of four peptides representing HTLV-1 proteinase cleavage sites were fairly good substrates of HIV-1 proteinase, only two of nine peptides representing HIV-1 proteinase cleavage sites were hydrolyzed by the HTLV-1 proteinase, suggesting substantial differences in the specificity of the two enzymes. The large difference in the specificity of the two enzymes was also demonstrated by inhibition studies. Of the several inhibitors of HIV-1 or other retroviral proteinases that were tested on HTLV-1 proteinase, only two inhibit the enzyme with a Ki lower than 100 nM. (+info)
Fus3p and Kss1p control G1 arrest in Saccharomyces cerevisiae through a balance of distinct arrest and proliferative functions that operate in parallel with Far1p. (2/2015)In Saccharomyces cerevisiae, mating pheromones activate two MAP kinases (MAPKs), Fus3p and Kss1p, to induce G1 arrest prior to mating. Fus3p is known to promote G1 arrest by activating Far1p, which inhibits three Clnp/Cdc28p kinases. To analyze the contribution of Fus3p and Kss1p to G1 arrest that is independent of Far1p, we constructed far1 CLN strains that undergo G1 arrest from increased activation of the mating MAP kinase pathway. We find that Fus3p and Kss1p both control G1 arrest through multiple functions that operate in parallel with Far1p. Fus3p and Kss1p together promote G1 arrest by repressing transcription of G1/S cyclin genes (CLN1, CLN2, CLB5) by a mechanism that blocks their activation by Cln3p/Cdc28p kinase. In addition, Fus3p and Kss1p counteract G1 arrest through overlapping and distinct functions. Fus3p and Kss1p together increase the expression of CLN3 and PCL2 genes that promote budding, and Kss1p inhibits the MAP kinase cascade. Strikingly, Fus3p promotes proliferation by a novel function that is not linked to reduced Ste12p activity or increased levels of Cln2p/Cdc28p kinase. Genetic analysis suggests that Fus3p promotes proliferation through activation of Mcm1p transcription factor that upregulates numerous genes in G1 phase. Thus, Fus3p and Kss1p control G1 arrest through a balance of arrest functions that inhibit the Cdc28p machinery and proliferative functions that bypass this inhibition. (+info)
Pregnancy detection and the effects of age, body weight, and previous reproductive performance on pregnancy status and weaning rates of farmed fallow deer (Dama dama). (3/2015)Fallow does (n = 502) of different ages (mature, 2-yr-old, and yearling) were maintained with bucks for a 60-d breeding season to determine whether previous reproductive performance and changes in BW affect doe pregnancy rates and to compare the effectiveness of ultrasonography and serum pregnancy-specific protein B (PSPB) for the detection of pregnancy in fallow does. Ultrasonography was performed, blood samples collected, and BW recorded at buck removal (d 0) and at 30 and 90 d after buck removal. Lactational status (lactating = WET; nonlactating = DRY) were determined from farm records taken at weaning prior to each breeding season (autumn 1990 through autumn 1994). Ultrasonography and PSPB for determining pregnancy were in agreement 93% of the time. Overall pregnancy rates did not differ (P>.10) relative to age of the doe; the combined pregnancy rate was 92%. We also determined that 82.9% of does conceived early in the breeding season and that the incidence of embryonal-fetal mortality during the first 90 d after buck removal was 2.8%. In general, mature and 2-yr-old DRY does were heavier and had lower pregnancy rates than WET does. The overall weaning rate for all does was 77.9%. Loss in the number of fawns from pregnancy detection to weaning was equivalent to 14.8% for mature does, 24.7% for 2 yr old does, and 42.5% for yearling does. These data indicate that even though pregnancy rates were relatively high, further study is needed to determine the causes associated with subsequent fawn losses, particularly among yearling does. As a production tool, lactational WET/ DRY status testing was found to be an acceptable means for determining the reproductive potential of individual does within the herd. In addition, serum PSPB may be used in place of ultrasonography for pregnancy diagnosis in fallow deer as early as d 30 after buck removal. (+info)
Endothelin-1 and its mRNA in the wall layers of human arteries ex vivo. (4/2015)BACKGROUND: The participation of endothelin-1 (ET-1) in the control of vascular tone in humans has been questioned, on the basis of the finding of subthreshold immunoreactive (ir) ET-1 plasma levels. However, because most ET-1 is secreted abluminally, it might attain a higher concentration in the tunica media than in plasma. Furthermore, evidence indicates that vascular smooth muscle cells (VSMCs) can synthesize ET-1 on stimulation in vitro. We therefore looked for irET-1 in the different layers of the wall of human arteries, including renal, gastric, and internal thoracic artery wall, obtained ex vivo from consenting patients with coronary artery disease and/or high blood pressure undergoing surgery, as well as from young organ donors. METHODS AND RESULTS: We performed immunohistochemistry with specific anti-ET-1 and anti-vWF antibodies followed by detection with an avidin-biotin complex ultrasensitive kit. The presence of preproET-1 and human endothelin-converting enzyme-1 (hECE-1) mRNA was also investigated by reverse transcription-polymerase chain reaction in homogenates of vessel wall, including preparations deprived of both endothelium and adventitia, and in isolated VSMCs. We detected irET-1 in the endothelium of all arteries and in the tunica media of internal thoracic artery from most patients with coronary artery disease. PreproET-1 and hECE-1 mRNA was also detected in VSMCs isolated from these vessels. irET-1 and irvWF staining in endothelium and tunica media was measured by use of microscope-coupled computer-assisted technology. Significant correlations between the amount of irET-1 in the tunica media and mean blood pressure (P<0.05), total serum cholesterol (P<0.05), and number of atherosclerotic sites (P<0.001) were found. Thus, in organ donors, irET-1 was detectable almost exclusively in endothelial cells, whereas in patients with coronary artery disease and/or arterial hypertension, sizable amounts of irET-1 were detectable in the tunica media of different types of arteries. In addition, VSMCs isolated from these vessels coexpressed the preproET-1 and hECE-1 genes. CONCLUSIONS: Collectively, these findings are consistent with the contention that endothelial damage occurs in most patients with atherosclerosis and/or hypertension and that ET-1 is synthesized in VSMCs of these patients. (+info)
Intranephron distribution and regulation of endothelin-converting enzyme-1 in cyclosporin A-induced acute renal failure in rats. (5/2015)Endothelin-1 (ET-1) is thought to play a significant role in acute renal failure induced by cyclosporin A (CsA). The cDNA sequence encoding endothelin-converting enzyme-1 (ECE-1), which produces the active form of ET-1 from big ET-1, was recently reported. To elicit the role of ECE-1 in the glomerular and tubular dysfunction induced by CsA, the effects of CsA on mRNA and protein expression of ECE-1 in rat kidney and on mRNA expression of prepro-ET-1 and ET A- and B-type receptors in glomeruli were studied. ECE-1 mRNA was detected in glomeruli and in whole nephron segments. ECE-1 mRNA expression was downregulated in all nephron segments at 24 h after CsA injection. Protein levels were also downregulated in glomeruli and in the outer and inner medulla. CsA rapidly increased prepro-ET-1 mRNA expression in glomeruli at 30 to 60 min after injection; this rapid increase was followed by an increase in plasma ET-1 levels. These increases were followed by decreased expression of ECE-1, ET A-type receptor, and ET B-type receptor mRNA at 6 h after injection, and serum creatinine levels were increased at 24 h after CsA injection. It is suggested that downregulation of glomerular and tubular ECE-1 expression may be caused by increased ET-1 synthesis in CsA-induced acute renal failure. (+info)
Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases? (6/2015)BACKGROUND: The aspartic proteinase renin catalyses the first and rate-limiting step in the conversion of angiotensinogen to the hormone angiotensin II, and therefore plays an important physiological role in the regulation of blood pressure. Numerous potent peptidomimetic inhibitors of this important drug target have been developed, but none of these compounds have progressed past clinical phase II trials. Limited oral bioavailability or excessive production costs have prevented these inhibitors from becoming new antihypertensive drugs. We were interested in developing new nonpeptidomimetic renin inhibitors. RESULTS: High-throughput screening of the Roche compound library identified a simple 3, 4-disubstituted piperidine lead compound. We determined the crystal structures of recombinant human renin complexed with two representatives of this new class. Binding of these substituted piperidine derivatives is accompanied by major induced-fit adaptations around the enzyme's active site. CONCLUSIONS: The efficient optimisation of the piperidine inhibitors was facilitated by structural analysis of the renin active site in two renin-inhibitor complexes (some of the piperidine derivatives have picomolar affinities for renin). These structural changes provide the basis for a novel paradigm for inhibition of monomeric aspartic proteinases. (+info)
Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. (7/2015)Proteolytic processing of the amyloid precursor protein by beta-secretase yields A4CT (C99), which is cleaved further by the as yet unknown gamma-secretase, yielding the beta-amyloid (Abeta) peptide with 40 (Abeta40) or 42 residues (Abeta42). Because the position of gamma-secretase cleavage is crucial for the pathogenesis of Alzheimer's disease, we individually replaced all membrane-domain residues of A4CT outside the Abeta domain with phenylalanine, stably transfected the constructs in COS7 cells, and determined the effect of these mutations on the cleavage specificity of gamma-secretase (Abeta42/Abeta40 ratio). Compared with wild-type A4CT, mutations at Val-44, Ile-47, and Val-50 led to decreased Abeta42/Abeta40 ratios, whereas mutations at Thr-43, Ile-45, Val-46, Leu-49, and Met-51 led to increased Abeta42/Abeta40 ratios. A massive effect was observed for I45F (34-fold increase) making this construct important for the generation of animal models for Alzheimer's disease. Unlike the other mutations, A4CT-V44F was processed mainly to Abeta38, as determined by mass spectrometry. Our data provide a detailed model for the active site of gamma-secretase: gamma-secretase interacts with A4CT by binding to one side of the alpha-helical transmembrane domain of A4CT. Mutations in the transmembrane domain of A4CT interfere with the interaction between gamma-secretase and A4CT and, thus, alter the cleavage specificity of gamma-secretase. (+info)
In vivo expression and localization of Candida albicans secreted aspartyl proteinases during oral candidiasis in HIV-infected patients. (8/2015)Isoforms of aspartyl proteinase (Sap), which are encoded by at least nine related SAP genes, have been implicated to be a major virulence factor of the opportunistic yeast Candida albicans in experimental infections. Although it is generally assumed that proteinases are important for infections, detailed information on the pathogenetic role of Saps is still lacking. The same applies to the question whether the genes and corresponding isoforms of the enzyme are expressed during oral infection. For in vivo investigations, parts of the lesional oral epithelium were collected from three HIV-infected patients with oropharyngeal candidiasis. Immunoelectron microscopy was performed (pre- and post-embedding gold labeling with silver enhancement) using an anti-Sap murine monoclonal antibody directed against the gene products Sap1-3. It was possible to demonstrate expression of Sap antigens in each of the three samples of human oral candidiasis. This suggests that at least one of the genes SAP1-3 was expressed at the time of sample collection. Furthermore, a possible role of the enzymes during the interaction of yeast cells and mucosal cells is suggested: the majority of Sap antigens is secreted by those C. albicans cells that adhere directly to the epithelial surface. Sap immunoreactivity can be detected in particular at the site of close contact between C. albicans and epithelial cells, suggesting a pathogenetic role of the Saps in host-fungal interaction. Thus, inhibition of the enzyme might prove to be an important alternative in the prevention and treatment of candidiasis. (+info)
P-glycoprotein efflux and other factors limit brain amyloid beta reduction by beta-site amyloid precursor protein-cleaving...
Meredith, J.E.; Thompson, L.A.; Toyn, J.H.; Marcin, L.; Barten, D.M.; Marcinkeviciene, J.; Kopcho, L.; Kim, Y.; Lin, A.; Guss, V.; Burton, C.; Iben, L.; Polson, C.; Cantone, J.; Ford, M.; Drexler, D.; Fiedler, T.; Lentz, K.A.; Grace, J.E.; Kolb, J.; Corsa, J.; Pierdomenico, M.; Jones, K.; Olson, R.E.; Macor, J.E.; Albright, C.F., 2008: P-glycoprotein efflux and other factors limit brain amyloid beta reduction by beta-site amyloid precursor protein-cleaving enzyme 1 inhibitors in mice
Two di-leucine-based motifs account for the different subcellular localizations of the human endothelin-converting enzyme (ECE...
Endothelin-converting enzyme (ECE-1) is a type II integral membrane protein which plays a key role in the biosynthetic pathway of the vasoconstricting endothelins. Three ECE-1 isoforms, differing by their N-terminal cytoplasmic tails, are generated from a single gene. When expressed in CHO cells, they display comparable enzymatic activity but whereas ECE-1a is strongly expressed at the cell surface, ECE-1b is exclusively intracellular and ECE-1c presents an intermediate distribution. In the present study these different localizations were further described at the ultrastructural level, by electron microscope immunocytochemistry. To characterize the motifs responsible for the intracellular localization of ECE-1b we constructed chimeric proteins and point mutants. Two di-leucine-based motifs, contained in the N-terminal part of ECE-1b, were thus identified. One of these motifs (LV), displayed by both ECE-1b and ECE-1c, accounts for the reduced surface expression of ECE-1c as compared to ECE-1a. ...
Secretory Aspartyl Proteinases Cause Vaginitis and Can Mediate Vaginitis Caused by Candida albicans in Mice | mBio
Secretory aspartyl proteinases (Sap) have long been considered key virulence traits of C. albicans, with rather strong experimental and clinical evidence for a major role in vaginal candidiasis (1, 3). However, the mechanisms by which this family of enzymes is involved in vaginal disease have remained unclear. Sap are active enzymes with a wide range of substrate specificities (26). Since some of these substrates (e.g., complement, histatins, and E-cadherin, and also Abs) play critical roles in both innate and adaptive immune responses, Sap expression is thought to enable the fungus to evade host immunity by enzymatic proteolysis of one or more of the above factors (1, 3). Concurrently, studies in well-established animal models and reconstituted human vaginal epithelia have provided indirect clues for a role of some members of the Sap family in facilitating fungus adherence and penetration into epithelial tissues (27-30). Evidence gathered with the use of anti-Sap Abs supports this proadherence ...
Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic...
A new aspartic protease from Saccharomyces cerevisiae, with a high degree of similarity with yapsin 1 and yapsin 2 and a specificity for basic residue cleavage sites of prohormones, has been cloned. This enzyme was named yapsin 3. Expression of a C-terminally truncated non-membrane anchored yapsin 3 in yeast yielded a heterogeneous protein between 135-200 kDa which, upon treatment with endoglycosidase H, migrated as a 60 kDa form. Amino-acid analysis of the N-terminus of expressed yapsin 3 revealed two different N-terminal residues, serine-48 and phenylalanine-54, which followed a dibasic and a monobasic residue respectively. Cleavage of several prohormones by non-anchored yapsin 3 revealed a specificity distinct from that of yapsin 1.. ...
Drosophila Signal Peptide Peptidase Is an Essential Protease for Larval Development | Genetics
Our goal in this work was to determine if signal peptide peptidase is necessary for normal animal development. We present data showing that Drosophila Spp encodes the fly ortholog of human signal peptide peptidase and show that Drosophila Spp provides an essential function required during the larval stages. We also show that SPP is strongly expressed in only a limited set of cells and that the mutant phenotype is consistent with a need for its function in these tissues. Further work will be needed to establish whether the role of Drosophila SPP is a general one that cleanses membranes of signal peptides or if it has specific targets and generates essential products through its action.. Human SPP is an intramembrane aspartyl protease whose active site is predicted to be buried within the lipid bilayer. It belongs to a family of enzymes conserved among animals, plants, and fungi (Ponting et al. 2002; Weihofen et al. 2002). The Drosophila and human SPPs have strong sequence similarity, with the ...
Featured Papers in 2013 | Alomone Labs
This paper focuses deals with the cleavage of NaVβ2 via BACE-1 (Beta-site APP-cleaving enzyme 1), leading to increased NaV1.1 levels, which do not translocate to the cell plasma membrane. Reinforcing that decreased NaV1.1 levels are involved in AD development/progression. This work cites the use of Alomone Labs Anti-SCN1A (NaV1.1) Antibody (#ASC-001) and Anti-NaVβ2 Antibody (#ASC-007).. The early stages of Alzheimers disease (AD), an incurable neurological affliction with adverse effects on memory and cognition, are often accompanied by aberrant neuronal activity and epileptic seizures - events which are increasingly seen as having a direct influence on ADs progression. Cortical accumulation of amyloid β (Aβ), a peptide derived from amyloid precursor protein (APP), seems to play a prominent role on the onset of AD. Beta-site APP-cleaving enzyme 1 (BACE1) - the rate-determining factor in Aβ synthesis - is significantly high in both AD patients and APP mice (transgenic line with ...
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Beta-site APP-cleaving enzyme 1 isoform C (BACE) polyclonal antibody - Allele Biotech
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Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u | The EMBO Journal
Intramembrane proteases cleave peptide bonds within cellular membranes and thereby control important processes ranging from transcription regulation to growth factor secretion (Lemberg, 2011). The largest and most diverse group of these unusual enzymes is formed by the GxGD aspartyl proteases including presenilin/γ‐secretase as well as signal peptide peptidase (SPP) (Wolfe, 2009; Lichtenthaler et al, 2011). SPP localizes to the endoplasmic reticulum (ER) where it cleaves signal peptides that have been removed from precursors of secretory and membrane proteins (Weihofen et al, 2002). Like for most characterized intramembrane proteases, this release is part of a two‐step mechanism: First signal peptidase cleaves off the substrate proteins ectodomains, which enables the subsequent SPP‐catalyzed intramembrane cut (Lemberg & Martoglio, 2002). So far, known functions of SPP include generation of signal peptide‐derived bioactive peptides in immune surveillance and proteolytic maturation of ...
Signal peptide peptidase - Wikipedia
In molecular biology, the Signal Peptide Peptidase (SPP) is a type of protein that specifically cleaves parts of other proteins. It is an intramembrane aspartyl protease with the conserved active site motifs YD and GxGD in adjacent transmembrane domains (TMDs). Its sequences is highly conserved in different vertebrate species. SPP cleaves remnant signal peptides left behind in membrane by the action of signal peptidase and also plays key roles in immune surveillance and the maturation of certain viral proteins. Physiologically SPP processes signal peptides of classical MHC class I preproteins. A nine amino acid-long cleavage fragment is then presented on HLA-E receptors and modulates the activity of natural killer cells. SPP also plays a pathophysiological role; it cleaves the structural nucleocapsid protein (also known as core protein) of the Hepatitis C virus and thus influences viral reproduction rate. In mice, a nonamer peptide originating from the SPP protein serves as minor ...
RCSB PDB for 3RTM
3RTM: From Fragment Screening to In Vivo Efficacy: Optimization of a Series of 2-Aminoquinolines as Potent Inhibitors of Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1 (BACE1).
Enhancement of immunoreactivity for endothelin-1 and endothelin-converting enzyme-1 in the cadmium-treated rat thoracic aorta. ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
endothelin-converting enzyme 1(EC 184.108.40.206) - Creative Enzymes
A phosphoramidon-sensitive metalloendopeptidase in peptidase family M13 (neprilysin family). An integral membrane protein predominantly of endothelial cells, which genera
OriGene - BACE1 (NM 012104) cDNA Clone
BACE1 - BACE1 (untagged)-Human beta-site APP-cleaving enzyme 1 (BACE1), transcript variant a available for purchase from OriGene - Your Gene Company.
PMAP: SubstrateDB : Isoform Delta of Protachykinin-1
Isoform Delta of Protachykinin-1 contains a PF02202 domain.. Isoform Delta of Protachykinin-1 contains a PF02202 domain.. Isoform Delta of Protachykinin-1 is proteolytically cut by dipeptidyl-peptidase II (S28.002) cleavage. --RP-KPQQ.. Isoform Delta of Protachykinin-1 is proteolytically cut by (S9F.001) cleavage. FFGL-MNH2--.. Isoform Delta of Protachykinin-1 is proteolytically cut by penicillolysin (M35.001) cleavage. RPKP-QQFF.. Isoform Delta of Protachykinin-1 is proteolytically cut by aminopeptidase P1 (M24.009) cleavage. ---R-PKPQ.. Isoform Delta of Protachykinin-1 is proteolytically cut by endothelin-converting enzyme 1 (M13.002) cleavage. PQQF-FGLM.. Isoform Delta of Protachykinin-1 is proteolytically cut by endothelin-converting enzyme 1 (M13.002) cleavage. KPQQ-FFGL.. Isoform Delta of Protachykinin-1 is proteolytically cut by neprilysin (M13.001) cleavage. PQQF-FGLM.. Isoform Delta of Protachykinin-1 is proteolytically cut by neprilysin (M13.001) cleavage. KPQQ-FFGL.. Isoform Delta of ...
Multiple myeloma (MM) can be an indolent B-cell disease that develops in the bone tissue marrow and it is connected with osteolytic lesions in 1174043-16-3 the advanced phases . site thats turned on in Tyr1356 and Tyr1349. The phosphorylation of the region leads to the induction of MET signaling through the activation of many downstream …Read More. ...
Christina Scharnagl - Intramembrane Proteolysis
Intramembrane proteolysis, Alzheimer´s disease, Parkinsons disease, type-2 diabetes, γ-secretase, signal peptide peptidase , substrate enzym interactions, TMD, DFG Verbundprojekt, Lemberg, Fluhrer, Lichtenthaler, Steiner, Langosch, Haass, Frishman, Scharnagl, Luy, Huster,
Dieter Langosch - Intramembrane Proteolysis
Intramembrane proteolysis, Alzheimer´s disease, Parkinsons disease, type-2 diabetes, γ-secretase, signal peptide peptidase , substrate enzym interactions, TMD, DFG Verbundprojekt, Lemberg, Fluhrer, Lichtenthaler, Steiner, Langosch, Haass, Frishman, Scharnagl, Luy, Huster,
RCSB PDB - 1OEX: Atomic Resolution Structure of Endothiapepsin in Complex with a Hydroxyethylene Transition State...
1OEX: Atomic Resolution Analysis of the Catalytic Site of an Aspartic Proteinase and an Unexpected Mode of Binding by Short Peptides
Recombinant Human BACE1 protein, His-tagged BACE1-891H - Creative BioMart
Recombinant Human BACE1 precursor extracellular domain (Met 1-Thr 457) (NP_036236.1), fused with a C-terminal polyhistidine tag, was produced in Human Cell.
SPPL3 Gene - GeneCards | SPPL3 Protein | SPPL3 Antibody
Complete information for SPPL3 gene (Protein Coding), Signal Peptide Peptidase Like 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
SPPL2B Gene - GeneCards | SPP2B Protein | SPP2B Antibody
Complete information for SPPL2B gene (Protein Coding), Signal Peptide Peptidase Like 2B, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Research Brief: New BACE Inhibitor Joins the Fold | ALZFORUM
Vitae Pharmaceuticals BACE inhibitor, VTP-37948, lowered cerebrospinal fluid Aβ by up to 80 percent in healthy volunteers, according to topline data from a Phase 1 clinical trial. A second Phase 1 trial that used a single-ascending-dose strategy suggested that volunteers tolerated the drug well. Vitae chief scientific officer Richard Gregg told Alzforum that the companies will soon test the inhibitor in multiple rising dose trials. Results should be available early next year, said Vitae CEO Jeffrey Hatfield. The company will develop the inhibitor, also known as BI 1181181, in partnership with Boehringer Ingelheim.. Vitae used a structure-based approach to develop the drug, which fits the catalytic pocket of the aspartyl protease. VTP-37948 joins BACE inhibitors being developed by other pharmaceutical companies including Merck, AstraZeneca/Lilly, and Novartis. The Vitae inhibitor, like the other compounds under development, does not discriminate between β-secretase isoforms, blocking both ...
OriGene - Ece1 (NM 199307) cDNA Clone
Ece1 - Ece1 (untagged) - Mouse endothelin converting enzyme 1 (Ece1), (10ug) available for purchase from OriGene - Your Gene Company.
ECE1 overexpression lysate - LY419958 | acris-antibodies.com
ECE1 overexpression lysate, 0.1 mg. Transient overexpression lysate of endothelin converting enzyme 1 (ECE1), transcript variant 1
Help!: post #1
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The proteins BACE1 and BACE2 and β-secretase activity in normal and Alzheimers disease brain | Biochemical Society...
The insidious progression of AD (Alzheimers disease) is believed to be linked closely to the production, accumulation and aggregation of the ∼4.5 kDa protein fragment called Aβ (amyloid β-peptide). Aβ is produced by sequential cleavage of the amyloid precursor protein by two enzymes referred to as β- and γ-secretase. β-Secretase is of central importance, as it catalyses the rate-limiting step in the production of Aβ and was identified 7 years ago as BACE1 (β-site APP-cleaving enzyme 1). Soon afterwards, its homologue BACE2 was discovered, and both proteins represent a new subclass of the aspartyl protease family. Studies examining the regulation and function of β-secretase in the normal and AD brain are central to the understanding of excessive production of Aβ in AD, and in targeting and normalizing this β-secretase process if it has gone awry in the disease. Several reports indicate this, showing increased β-secretase activity in AD, with recent findings by our group showing ...
A fourth secreted aspartyl proteinase gene (SAP4) and a CARE2 repetitive element are located upstream of the SAP1 gene in...
Candida albicans secreted aspartyl proteinases (Sap), products of the SAP genes, which are presumed to act as virulence factors. In the C. albicans strain WO-1, the ability to secrete Sap1 is regulated with switch phenotype, another putative virulence factor. KpnI restriction fragment length polymorphisms differentiate between several distinct SAP1 alleles in laboratory and clinical strains. Both SAP1 alleles from strain WO-1 along with their 5- and 3-flanking regions were cloned and sequenced, as were both alleles from another strain, SS. The 5-flanking regions were remarkably similar in all four of the sequenced alleles over approximately 1,500 nucleotides. S1 analysis revealed that both alleles of WO-1 are transcribed. Characterization of the one allele from strain WO-1 identified a 284-nucleotide insertion flanked by 8-bp direct repeats that shows homology to the CARE2 repetitive element and that is not present in the other alleles. Characterization of the SAP1 alleles also identified a ...
Patent US7115652 - Aspartyl protease inhibitors - Google Patenten
The present invention provides compounds having the formula: wherein R1, R′, R2, R3, R3′, R4, X1, X2 and X3 are as defined herein, and pharmaceutical compositions thereof. The present invention also provides methods of inhibiting proteases, more specifically aspartyl proteases. In certain embodiments, compounds inhibit BACE (β-site APP-cleaving enzyme), and thus are useful in the treatment or prevention of a disease characterized by β-amyloid deposits in the brain (including, but not limited to, Alzheimers Disease). The present invention also provides methods for preparing compounds of the invention.
A Live-Cell Assay for Studying Extracellular and Intracellular Endothelin-Converting Enzyme Activity | Hypertension
The present study describes a novel sensitive live-cell assay for studying ECE activity. ET-1 is formed from its precursor preproET-1 via the cleavage of the intermediate bigET-1 by ECE-1. However, the subcellular site at which this step occurs is not clear: It could occur intravesicularly along the secretory pathway or bigET-1 may be released and processed extracellularly. To address this point, we have developed an integrated autocrine system.. Until now, ECE activity has been evaluated in solubilized membrane fractions by high-performance liquid chromatography assays,32 immunoassays,12 fluorogenic determinations,33 receptor assays,34 and fluorescence polarization assays.35 Most of these assays require an incubation in vitro with high concentrations of substrate, and all of them need an independent second step to measure the product, ET-1.. In the present study, a recombinant CHO reporter cell line permanently expressing the human ETA receptor and a reporter gene sensitive to its activation ...
APH1, PEN2, and Nicastrin increase Aβ levels and γ-secretase activity<...
TY - JOUR. T1 - APH1, PEN2, and Nicastrin increase Aβ levels and γ-secretase activity. AU - Marlow, Laura. AU - Canet, Rosa M.. AU - Haugabook, Sharie J.. AU - Hardy, John A.. AU - Lahiri, Debomoy K.. AU - Sambamurti, Kumar. PY - 2003/6/6. Y1 - 2003/6/6. N2 - A major component of the amyloid plaque core in Alzheimers disease (AD) is the 40-42-residue amyloid β peptide (Aβ). Mutations linked to AD such as those in presenilins 1 (PS1) and 2 (PS2) invariably increase the longer Aβ42 species that forms neurotoxic oligomers. It is believed that PS1/2 constitute the catalytic subunit of the γ-secretase responsible for the final step in Aβ biogenesis. Recent genetic studies have identified a number of additional genes encoding APH1a, APH1b, PEN2, and Nicastrin proteins, which are part of the γ-secretase complex with PS1. Further, knockout studies using RNAi showed that these components are essential for γ-secretase activity. However, the nature of γ-secretase and how the aforementioned ...
2OHR | X-RAY CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 6A | 2OHR A | P56817 | BACE1 | Beta-secretase 1 | 3D...
cansSAR 3D Structure of 2OHR | X-RAY CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 6A | 2OHR_A | Beta-secretase 1 - Also known as BACE1_HUMAN, BACE1, BACE, KIAA1149. Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase (PubMed:10656250, PubMed:10677483, PubMed:20354142). Cleaves CHL1 (By similarity). Monomer. Interacts (via DXXLL motif) with GGA1, GGA2 and GGA3 (via their VHS domain); the interaction highly increases when BACE1 is phosphorylated at Ser-498 (PubMed:14567678, PubMed:15886016). Interacts with RTN3 and RTN4 (PubMed:15286784, PubMed:16965550, PubMed:16979658). Interacts with SNX6 (PubMed:20354142). Interacts with PCSK9 (PubMed:18660751). Interacts with NAT8 and NAT8B (PubMed
Aspartic protease - Wikipedia
Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. In general, they have two highly conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin. Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised. More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin and archaean preflagellin have been described. Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, arising from ancestral duplication. Retroviral and retrotransposon proteases (retroviral aspartyl proteases) are much smaller and appear to be homologous to a single domain of the eukaryotic aspartyl proteases. Each domain contributes a catalytic Asp residue, with an extended active ...
In vivo reconstitution of gamma-secretase in Drosophila results in substrate specificity - MDC Repository
The intramembrane aspartyl protease gamma-secretase plays a fundamental role in several signaling pathways involved in cellular differentiation and has been linked with a variety of human diseases, including Alzheimers disease. Here, we describe a transgenic Drosophila model for in vivo-reconstituted gamma-secretase, based on expression of epitope-tagged versions of the four core gamma-secretase components, Presenilin, Nicastrin, Aph-1, and Pen-2. In agreement with previous cell culture and yeast studies, coexpression of these four components promotes the efficient assembly of mature, proteolytically active gamma-secretase. We demonstrate that in vivo-reconstituted gamma-secretase has biochemical properties and a subcellular distribution resembling those of endogenous gamma-secretase. However, analysis of the cleavage of alternative substrates in transgenic-fly assays revealed unexpected functional differences in the activity of reconstituted gamma-secretase toward different substrates, ...
IJMS | Free Full-Text | Effect of Different Phospholipids on α-Secretase Activity in the Non-Amyloidogenic Pathway of...
Alzheimers disease (AD) is characterized by extracellular accumulation of amyloid-β peptide (Aβ), generated by proteolytic processing of the amyloid precursor protein (APP) by β- and γ-secretase. Aβ generation is inhibited when the initial ectodomain shedding is caused by α-secretase, cleaving APP within the Aβ domain. Therefore, an increase in α-secretase activity is an attractive therapeutic target for AD treatment. APP and the APP-cleaving secretases are all transmembrane proteins, thus local membrane lipid composition is proposed to influence APP processing. Although several studies have focused on γ-secretase, the effect of the membrane lipid microenvironment on α-secretase is poorly understood. In the present study, we systematically investigated the effect of fatty acid (FA) acyl chain length (10:0, 12:0, 14:0, 16:0, 18:0, 20:0, 22:0, 24:0), membrane polar lipid headgroup (phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine), saturation grade and the FA double-bond
Intramembrane proteolysis and post-targeting functions of signal peptides | Biochemical Society Transactions
Signal sequences are the addresses of proteins destined for secretion. In eukaryotic cells, they mediate targeting to the endoplasmic reticulum membrane and insertion into the translocon. Thereafter, signal sequences are cleaved from the pre-protein and liberated into the endoplasmic reticulum membrane. We have recently reported that some liberated signal peptides are further processed by the intramembrane-cleaving aspartic protease signal peptide peptidase. Cleavage in the membrane-spanning portion of the signal peptide promotes the release of signal peptide fragments from the lipid bilayer. Typical processes that include intramembrane proteolysis is the regulatory or signalling function of cleavage products. Likewise, signal peptide fragments liberated upon intramembrane cleavage may promote such post-targeting functions in the cell.. ...
Napsin A Detection: ELISAs and Antibodies
Novel Aspartic Proteinase of the PepSIN Family (Napsin A, or NAPSA) belongs to the peptidase A1 family and plays a role in pneumocyte surfactant processing. It is also known as aspartyl protease 4 (ASP4), KAP, Kdap, napsin-1, NAP1, NAPA, and SNAPA. Two closely related proteins are known, Napsin A and Napsin B. Napsin A is a single-chain, 38-kDa protein. It is expressed at high levels in human lung and kidney, and at lower levels in spleen. Napsin A expression has been detected in type II pneumocytes and in lung adenocarcinomas.. ...
www.MOLUNA.de Aspartic Proteinases  - The 5th International Conference on Aspartic Proteinases was held on September 19 through 24, 1993, at Naito Museum of Pharmaceutical Science and Industry, Kawashima cho, Gifu Prefecture, Japan, about 15 miles northwest of Nagoya City. About 100 scientists attended the conference, including 52 from 14 countries outside Japan, and 32
Dynamic changes in the secondary structure of ECE-1 and XCE account for their different substrate specificities | BMC...
X-converting enzyme (XCE) involved in nervous control of respiration, is a member of the M13 family of zinc peptidases, for which no natural substrate has been identified yet. In contrast, its well characterized homologue endothelin-converting enzyme-1 (ECE-1) showed broad substrate specificity and acts as endopeptidase as well as dipeptidase. To explore the structural differences between XCE and ECE-1, homology model of XCE was built using the complex structure of ECE-1 with phosphoramidon (pdb-id: 3DWB) as template. Phosphoramidon was docked into the binding site of XCE whereas phosphate oxygen of the inhibitor was used as water molecule to design the apo forms of both enzymes. Molecular dynamics simulation of both enzymes was performed to analyze the dynamic nature of their active site residues in the absence and presence of the inhibitor. Homology model of XCE explained the role of non-conserved residues of its S2 subsite. Molecular dynamics (MD) simulations identified the flexible transitions of
endothelin converting enzymes - oi
Integral membrane proteins (ECEs) that are zinc-binding metallopeptidases of the same family as neprilysin with a role in processing various neuropeptides. ECE-1 (EC 220.127.116.11, 770 aa) converts big endothelin-1 (ET-1) to active ET-1 and is important in regulating blood pressure. Isoforms of endothelin-converting enzyme-1 (ECE-1a-d) are present in early endosomes, where they degrade various neuropeptides and regulate postendocytic sorting of receptors. Defects in the ECE-1 gene are associated with Hirschsprungs disease. ECE-2 (883 aa) has been implicated in Alzheimers disease and knockout mice show deficiencies in learning and memory. ...
Beta Secretase Substrate (ab101160) | Abcam
Beta Secretase Substrate Functional Assay Kits datasheet (ab101160). Abcam offers quality products including antibodies, assays and other reagents.
Circulation Editors Picks | Circulation
Hypertension is largely attributed to abnormal renal sodium handling; however, a growing body of evidence now suggests that primary abnormalities in vessels can also cause aberrations in blood pressure. Very often, the source of the abnormality resides in the endothelial cells that regulate the functional state of the entire vessel, and this knowledge has directed our search for new diagnostic and therapeutic targets. To date, the role of transcriptional mechanisms in blood pressure regulation is poorly characterized. In this study, we found that E2F2, a transcription factor involved in cell-cycle control, regulates blood pressure by modulating vessel contractility. This previously unknown function of E2F2 evolves from the unique role of the molecule in endothelial cells: suppression of endothelin-converting enzyme 1 (ECE-1). ECE-1 converts the inactive precursor molecule big endothelin-1 into the potent vasoconstrictor endothelin-1, and genetic deletion of E2F2 in mice was associated with both ...
ALZFORUM | NETWORKING FOR A CURE
Hansson CA, Frykman S, Farmery MR, Tjernberg LO, Nilsberth C, Pursglove SE, Ito A, Winblad B, Cowburn RF, Thyberg J, Ankarcrona M. Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria ...
Regulated intramembrane proteolysis is certainly a central mobile practice included in | Role of NK1 and NK2 receptors in mouse...
Regulated intramembrane proteolysis is certainly a central mobile practice included in sign membrane layer and transduction proteins turnover. condition of MHCII-containing endosomes, highlighting SPPL2a as a possible medicinal focus on for using up and/or modulating T cells. The concept of intramembrane proteases (I-CLIPs) cleaving within the phospholipid bilayer was originally place forwards structured on digesting of the sterol regulatory elementCbinding proteins (SREBP; Goldstein and Brown, 1997; Kopan and Wolfe, 2004). Generally, I-CLIPs operate as component of a proteolytic series known to as governed intramembrane proteolysis (Split; Lichtenthaler et al., 2011). Intracellular websites (ICDs) of many Split substrates function as signaling elements after their proteolytic discharge as exemplified by the Level path (De Strooper et al., 1999; Freeman and Urban, 2002). Structured on their catalytic middle, serine, metallo, or aspartyl I-CLIPs (Wolfe, 2009) can end up being differentiated. The ...
Related Articles. Structure-Based Design of Inhibitors of the Aspartic Protease Endothiapepsin by Exploiting Dynamic Combinatorial Chemistry.. Angew Chem Int Ed Engl. 2014 Feb 14 ...
Substitution of disulphide bonds to hydrophobic amino acids in BACE1
The study and understanding of Alzheimers disease on protein level is fundamentally important in the search for its treatment and there is a demand for proteins that can be used together with candidate drugs in crystallography trials. The refolding time reaching up to three weeks for beta-site APP cleaving enzyme 1 (BACE1), the proposed disease-generating protein, is presently not optimal and new protein constructs are needed. In attempts to shorten the refolding time the six cysteins in BACE1 were substituted to hydrophobic valine or alanine residues. The proteins, both wild type and mutant BACE1, were expressed in Escherichia coli, refolded for one week and purified by ion exchange chromatography and gel filtration. The final products were characterised by measuring stability, homogeneity and enzyme activity. There was significantly lower protein yield for the mutants compared to the wild type BACE1, indicating that generation of the disulphide bonds are important for correctly folded and ...
Follow the Endothelin | Science Signaling
The neurons of the sympathetic nervous system have distinct properties that allow them to regulate a particular end organ. Various models have been proposed to explain how such precise wiring of neurons to their synaptic targets might come about during development. The neurons might grow in a relatively random manner and then adopt appropriate characteristics after interacting with their target tissue, or there might be molecular markers that guide particular neurons to the right target. Makita et al. provide new evidence in favor of the latter scheme for a set of neurons of the superior cervical ganglia (SCG) that follow along the external carotid artery to reach their salivary gland targets. The authors examined mRNA from external carotid artery in microarray analysis to search for expression of transcripts that might encode guidance molecules. They found specific expression of mRNA encoding endothelin-converting enzyme (which converts precursors of endothelin into the active form). ...
SMART: Pfam domain A1 Propeptide
This entry represents the N-terminal domain of the aspartic peptidases. Aspartic peptidase, also known as aspartyl proteases ([intenz:3.4.23.-]) are a widely distributed family of proteolytic enzymes [ (PUBMED:6795036) (PUBMED:2194475) (PUBMED:1851433) ] known to exist in vertebrates, fungi, plants, retroviruses and some plant viruses. Aspartate proteases of eukaryotes are monomeric enzymes which consist of two domains. Each domain contains an active site centred on a catalytic aspartyl residue. The two domains most probably evolved from the duplication of an ancestral gene encoding a primordial domain. Currently known eukaryotic aspartyl proteases are: ...
Beta-Secretase 1 ELISA Kits | Biocompare.com
Compare Beta-Secretase 1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
INT191919 - wiki-pain
The most important allergen associated with IgE responses, Bla g 2, belongs to a subgroup of the aspartic proteinase family of enzymes that is enzymatically inactive (Arruda et al. 2001; Pomes et al. 2002 ...
BACE1 polyclonal antibody - (PAB9981) - Products - Abnova
Rabbit polyclonal antibody raised against synthetic peptide of BACE1. A synthetic peptide corresponding to C-terminus of human BACE1. (PAB9981) - Products - Abnova
Memapsin 2 - Википедија, слободна енциклопедија
Hong, L., Turner, R.T., Koelsch, G., Shin, D., Ghosh, A.K. and Tang, J. (2002). „Crystal structure of memapsin 2 (β-secretase) in complex with an inhibitor OM00-3. Biochemistry. 41: 10963-10967. PMID 12206667 ...
JEM | The Journal of Experimental Medicine
Liu et al. describe a previously unrecognized cellular complex (∼5 MD) containing β- and γ-secretases that generates a full array of Aβ peptides with physiological Aβ42/40 ratios by sequential cleavages of holo-APP. Such coordinated substrate processing also occurs with the α- and γ-secretases in the RIP mechanism.. ...
Broad Spectrum - Intramembrane Proteolysis
Supplementary MaterialsFigure S1: Kinetic parameter distribution of SNs before evolution. pone.0050905.s003.tif (81K) GUID:?270C2747-8D2C-40C2-A1ED-52BFDFB4C35A Abstract Transmission transduction is the process of routing information inside cells when receiving stimuli from their environment that modulate the behavior and function. In such natural procedures, the receptors, after getting the corresponding indicators, switch on several biomolecules which transduce the sign […]. ...
5??- - Intramembrane Proteolysis
Supplementary MaterialsVideo 1 Time-lapse imaging cells expressing both mt-roGFP and Smac mCherry treated with cisplatin stably. with an indicated medication with 10?nm of TMRM. Live cell imaging was TMP 269 biological activity completed as defined. mmc6.mp4 (20M) GUID:?20E6FE9E-0743-40DF-9A25-5E8A9CEF2F51 TMP 269 biological activity Video 7 EGCG: U2Operating-system cells stably expressing mt-roGFP were stained with TMRM to […]. ...
ece302hw8 - 3:32 we g(a Find H in rectangular components at P(2 3 4 if there is a current ﬁlament on the z axis carrying 8rnA...
View Notes - ece302hw8 from ECE ECE 302 at Cal Poly Pomona. 3:32 we g (a) Find H in rectangular components at P(2, 3, 4) if there is a current ﬁlament on the z axis carrying 8rnA in the aZ
BACE2 peptide (ab5869) | Abcam
Buy our BACE2 peptide. Ab5869 is a blocking peptide and has been validated in BL. Abcam provides free protocols, tips and expert support for WB and a 12 month…
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... The MEROPS online database for peptidases and their inhibitors: Aspartic Peptidases. *Aspartic+Endopeptidases at the US ... Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised. More recently, ... Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides. The animal ...
Proteasome endopeptidase complex
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... Proteasome endopeptidase complex (EC 18.104.22.168, ingensin, macropain, multicatalytic endopeptidase complex, prosome, ... Proteasome+endopeptidase+complex at the US National Library of Medicine Medical Subject Headings (MeSH) ... Retrieved from "https://en.wikipedia.org/w/index.php?title=Proteasome_endopeptidase_complex&oldid=826116286" ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... serine-type endopeptidase activity. Cellular component. • lamellipodium membrane. • extracellular exosome. • lysosomal membrane ... 1x70: HUMAN DIPEPTIDYL PEPTIDASE IV IN COMPLEX WITH A BETA AMINO ACID INHIBITOR ... 2oph: Human dipeptidyl peptidase IV in complex with an alpha amino acid inhibitor ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... 1990). "Galactosialidosis: simultaneous deficiency of esterase, carboxy-terminal deamidase and acid carboxypeptidase activities ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... aspartic-type endopeptidase activity. Cellular component. • multivesicular body. • late endosome. • endoplasmic reticulum lumen ... BACE1 is an aspartic-acid protease important in the formation of myelin sheaths in peripheral nerve cells: in mice the ... BACE1 is distantly related to the pathogenic aspartic-acid protease plasmepsin, which is a potential target for future anti- ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ...
Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. *HslU-HslV peptidase ... aspartic acid, metallo- and acid proteases) nucleophilic so that it can attack the peptide carboxyl group. One way to make a ... aspartic, and metallo proteases. The threonine and glutamic-acid proteases were not described until 1995 and 2004 ... depending on the amino acid sequence of a protein, or completely break down a peptide to amino acids (unlimited proteolysis). ...
Aspartic Acid -OOC-CH2- Oxaloacetate → Aspartic Acid (aminotransferase) Glutamic Acid -OOC-(CH2)2- α-ketoglutarate → Glutamic ... EndopeptidasesEdit. Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that ... Amino Acid SynthesisEdit. Pathways that form each amino acid. Amino Acid R-group‡ Pathway* ... The main amino acids involved are serine, histidine, and aspartic acid. They all play a role in cleaving the peptide bond. ...
"Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11". FEBS Lett. ... in the case of the metallopeptidases and aspartic, the nucleophiles clan or family for example MA, is an activated water ... Ecadotril is a neutral endopeptidase inhibitor ((NEP) EC 22.214.171.124) and determined by the presence of peptidase family M13 as a ... Malfroy B, Schofield PR, Kuang WJ, Seeburg PH, Mason AJ, Henzel WJ (April 1987). "Molecular cloning and amino acid sequence of ...
Signal peptide peptidase
Another family of signal aspartic endopeptidases was found in bacteria. Bacteria produce a number of protein precursors that ... A nine amino acid-long cleavage fragment is then presented on HLA-E receptors and modulates the activity of natural killer ... Martoglio B, Golde TE (October 2003). "Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide ... which differ from mature pilin by virtue of containing a 6-8 residue leader peptide consisting of charged amino acids. Mature ...
"Acid and non-acid reflux in patients with persistent symptoms despite acid suppressive therapy: a multicentre study using ... Pepsin is an endopeptidase that breaks down proteins into smaller peptides (that is, a protease). It is produced in the stomach ... Dunn BM (Nov 2001). "Overview of pepsin-like aspartic peptidases". Current Protocols in Protein Science. Chapter 21: Unit 21.3 ... Weak or non-acid reflux is correlated with reflux symptoms and mucosal injury. Under non-acid conditions ( ...
But more often groups in substrate and active site act as Brønsted-Lowry acid and base. This is called general acid and general ... Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide. It ... HIV protease belongs to aspartic protease family and has a similar mechanism. Firstly the aspartate residue activates a water ... In some reactions, protons and hydroxide may directly act as acid and base in term of specific acid and specific base catalysis ...
Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... The thioester bond is subsequently hydrolyzed to generate a carboxylic acid moiety on the remaining substrate fragment, while ... and the aspartic protease precursor pepsinogen. The protease is activated by removal of an inhibitory segment or protein. ... Cysteine proteases are used as feed additives for livestock to improve the digestibility of proteins and nucleic acids. ...
serine-type endopeptidase activity. • cysteine-type endopeptidase activity. • aspartic-type endopeptidase activity. ... The catalytic sites of cathepsin D include two critical aspartic residues (amino acid 33 and 231) located on the 14 kDa and ... Similar to other aspartic protainases, cathepsin D accommodates up to 8 amino acid residues in the binding cleft of the active ... "Nucleic Acids Research. 15 (9): 3773-86. doi:10.1093/nar/15.9.3773. PMC 340781 . PMID 3588310.. ...
Acid/base catalysisEdit. In some reactions, protons and hydroxide may directly act as acid and base in term of specific acid ... Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide. ... HIV protease belongs to aspartic protease family and has a similar mechanism. Firstly the aspartate residue activates a water ... The active site usually contains non-polar amino acids, although sometimes polar amino acids may also occur. The binding of ...
Energy-dependent acid transport was verified and the postulated proton pump purified. With the successful culture of ... The matrix metalloproteinases (MMPs) comprise a family of more than 20 zinc-dependent endopeptidases. The role of matrix ... The function of these cysteine and aspartic proteases is generally unknown within bone, and they are expressed at much lower ... Attachment to the bone matrix is facilitated by integrin receptors, such as αvβ3, via the specific amino acid motif Arg-Gly-Asp ...
The CASP8 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases ... cysteine-type endopeptidase activity involved in execution phase of apoptosis. Cellular component. • cell body. • cytosol. • ... cysteine-type endopeptidase activity. • hydrolase activity. • ubiquitin protein ligase binding. • peptidase activity. • ... cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • protein complex binding. • scaffold protein ...
... one histidine residue and one aspartic acid residue) and two from carbonate or bicarbonate ions. ... serine-type endopeptidase activity. • hydrolase activity. • lipopolysaccharide binding. • cysteine-type endopeptidase inhibitor ... Interaction with nucleic acidsEdit. One of the important properties of lactoferrin is its ability to bind with nucleic acids. ... There are differences in amino acid sequences: 8 in Homo sapiens, 6 in Mus musculus, 6 in Capra hircus, 10 in Bos taurus and 20 ...
Amino acid-derived. *Major excitatory/inhibitory systems: Glutamate system: Agmatine. *Aspartic acid (aspartate) ... role of aminopeptidases and endopeptidases". Peptides. 12 (5): 1119-25. doi:10.1016/0196-9781(91)90068-z. PMID 1800950.. ... response to retinoic acid. • positive regulation of renal sodium excretion. • regulation of receptor activity. • G-protein ... Hornig D (September 1975). "Distribution of ascorbic acid, metabolites and analogues in man and animals". Annals of the New ...
Amino acid-derived. *Major excitatory/inhibitory systems: Glutamate system: Agmatine. *Aspartic acid (aspartate) ... cysteine-type endopeptidase inhibitor activity involved in apoptotic process. • neurohypophyseal hormone activity. • receptor ... the value in the table above of 164 amino acids is that obtained before the hormone is activated by cleavage.) The amino acid ... negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • regulation of blood vessel size. • ...
Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u | The EMBO Journal
Our previous analysis of SPP revealed hydrophilic and small amino acid residues as primary determinant for signal peptide ... dendritic cells require the intramembrane endopeptidase SPPL2A. J Exp Med 210: 31-40. ... type aspartic protease. Science 296: 2215-2218. ... aminohexanoic acid, 100 mM Bis-Tris pH 7.0, and 5% (w/v) ... trichloroacetic acid, washed with acetone, and resuspended in SDS sample buffer. ...
Polyclonal Antibody Flow Cytometry Aspartic-Type Endopeptidase Activity to Polyclonal Antibody Fatty Acid Catabolic Process...
Polyclonal Antibody Flow Cytometry Amino Acid Transport, Polyclonal Antibody Flow Cytometry Adherens Junction Dynamics ... Polyclonal Antibody Flow Cytometry Aspartic-Type Endopeptidase Activity, Polyclonal Antibody Flow Cytometry Apoptosis, ... Category listing: Polyclonal Antibody Flow Cytometry Aspartic-Type Endopeptidase Activity to Polyclonal Antibody Fatty Acid ... Polyclonal Antibody Flow Cytometry Aspartic-Type Endopeptidase Activity Polyclonal Antibody Flow Cytometry Aspartic-Type ...
Aspartic endopeptidases | Article about Aspartic endopeptidases by The Free Dictionary
Find out information about Aspartic endopeptidases. organic compound, one of the 20 amino acids amino acid , any one of a class ... of simple organic compounds containing carbon, hydrogen, oxygen, nitrogen, and... Explanation of Aspartic endopeptidases ... aspartic acid. (redirected from Aspartic endopeptidases). Also found in: Dictionary, Thesaurus, Medical. aspartic acid. (əspär` ... Aspartic acid is not essential to the human diet. It was discovered in protein in 1868.. aspartic acid. [ə′spärd·ik ′as·əd] ( ...
The role of Candida albicans secreted aspartic proteinase in the development of candidoses. - PubMed - NCBI
Aspartic Acid Endopeptidases/genetics. *Aspartic Acid Endopeptidases/metabolism. *Aspartic Acid Endopeptidases/physiology* ... The secreted aspartic proteinase of C. albicans was first described in 1965 and has proved to be a major factor in virulence. ... The role of Candida albicans secreted aspartic proteinase in the development of candidoses.. Hoegl L1, Ollert M, Korting HC. ... This enzyme belongs to the class of aspartic proteinases which includes pepsin and renin in humans. Although found in some ...
A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain
Aspartic Acid Endopeptidases * Brain / metabolism * CCAAT-Enhancer-Binding Proteins* * Cells, Cultured * Cytoplasm / metabolism ...
Transcriptional profiling of developing mouse epidermis reveals novel patterns of coordinated gene expression
Natural products inhibiting Candida albicans secreted aspartic proteases from Tovomita krukovii.
Aspartic Acid Endopeptidases / drug effects, metabolism, secretion. Candida albicans / drug effects*. Clusiaceae*. Magnetic ... Aspartic Acid Endopeptidases; EC 126.96.36.199/Pepsin A ... 15247137 - Effect of folic acid supplementation on the folate ... 4-dihydroxybenzoic acid (14). Compounds 2, 3, 12 and 13 showed inhibitory effects against Candida albicans secreted aspartic ... 17830317 - Abscisic acid induces formation of floating leaves in the heterophyllous aquatic angios.... 20183257 - Two new ...
MEDLINE - Resultado p gina 1
Cathepsin D | Harvard Catalyst Profiles | Harvard Catalyst
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 ... The amino acid sequence and/or the amino acid sequence that is at least 80% homologous with it, preferably at least 90%, refers ... This amino acid sequence may also include other amino acids of the hinge-loop region, as explained above. ... In a preferred embodiment, the amino acid sequences ID No. 1 or ID No. 2 or amino acid sequences that are at least 80% ...
... serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in ... Endopeptidase 3.4.21-24. Serine proteases - Cysteine protease - Aspartic acid protease - Metalloendopeptidases. ... and aspartic acid (Asp 102). Located very near one another near the heart of the enzyme, these three key amino acids each play ... Instead of having the hydrophobic pocket of the chymotrypsin, there exists an aspartic acid residue at the base of the pocket. ...
a) Immunoblot analysis of β-catenin, cyclin D1, cycli | Open-i
cyprosin | Semantic Scholar
Aspartic Acid Endopeptidases. Papers overview. Semantic Scholar uses AI to extract papers important to this topic. ... The cDNA encoding the precursor of an aspartic proteinase from the flowers of the cardoon, Cynara cardunculus, was expressed in ... Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its ... Substrate specificity and molecular modelling of aspartic proteinases (cyprosins) from flowers of Cynara cardunculus subsp. ...
RCSB PDB - 1A86: MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR
MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR ... are a family of zinc endopeptidases, which have been implicated ... MMP8 WITH MALONIC AND ASPARTIC ACID BASED INHIBITOR. *DOI: 10.2210/pdb1A86/pdb ... Among the hydroxamic acids, malonic acid derivatives have been used as MMP inhibitors, although optimization of their ... Various classes of MMP inhibitors, including hydroxamic acids, phosphinic acids, and thiols, have been previously described ... ...
nepenthesin(EC 188.8.131.52) - Creative Enzymes
secretions) and Drosera peltata (ground-up leaves). Aspartic endopeptidases are probably present in many other plants, inclu ... Nepenthes aspartic proteinase; Nepenthes acid proteinase; nepenthacin; nepenthasin; aspartyl endopeptidase. Reaction. Similar ... secretions) and Drosera peltata (ground-up leaves). Aspartic endopeptidases are probably present in many other plants, ...
EMDB-1710: Cryo-EM 3D model of the icosahedral particle composed of Rous sar... - Yorodumi
Aspartic endopeptidases / viral capsid / nucleic acid binding / aspartic-type endopeptidase activity / zinc ion binding ... Aspartic peptidase, active site / Retroviral nucleocapsid protein Gag, p24 fragment / Retrovirus capsid, N-terminal / ... Aspartic peptidase, active site / Retroviral nucleocapsid protein Gag, p24 fragment / Retrovirus capsid, N-terminal / ... Buffer solution: 0.1M citric acid, 5mM MOPS/KOH, 725mM NaCl, 0.25mM Na azide, 0.125mM TCEP-HCl. pH: 5 Support film. Holey ...
Differential localization of ALP and other vacuolar pr | Open-i
A biotechnology perspective of fungal proteases
Aspartic acid proteases, commonly known as acidic proteases, are the endopeptidases that depend on aspartic acid residues for ... Acid protease. Wheat bran. (Merheb-Dini et al., 2010). Thermomyces lanuginosus. SmF. 6.0. 50 °C. 0.71. -. Glucose, citric acid ... Acid protease. Czapek-Dox, peptone. (Larsen et al., 1998). Phanerochaete chrysosporium. SSF. 4.5. 25 °C. 35. Acid and ... based on the nature of the amino acid residues at the active site of the enzymes. Endopeptidases are characterized by their ...
Endopeptidase, NLPC/P60 domain (IPR000064) | InterPro | EMBL-EBI
... usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. In only one family of cysteine peptidases ... Structural basis of murein peptide specificity of a gamma-D-glutamyl-l-diamino acid endopeptidase.. Structure 17 303-13 2009 ... Endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme contains two major domains: a bacterial SH3-like ... They are inhibited by thiol chelators such as iodoacetate, iodoacetic acid, N-ethylmaleimide or p-chloromercuribenzoate. ...
Other names: Rhizopus aspartic proteinase; neurase; Rhizopus acid protease; Rhizopus acid proteinase. Comments: From the ... A similar endopeptidase is found in R. niveus . In peptidase family A1 (pepsin A family). Formerly EC 184.108.40.206, and included ... Substrate specificity of acid protease of Rhizopus chinensis. Agric. Biol. Chem. 33 (1969) 1419-1426. 2. Kurono, Y., Chidimatsu ... 4. Suguna, K., Padlan, E.A., Smith, C.W., Carlson, W.D. and Davies, D.R. Binding of a reduced peptide inhibitor to the aspartic ...
DNA binding, RNA binding, RNA-directed DNA polymerase activity, aspartic-type endopeptidase activity, nucleic acid binding, ... crystallization of nucleic acid complexes. Protein Sci, 7:1575-82 [Medline info for 9684890] ... structures of an N-terminal fragment from Moloney murine leukemia virus reverse transcriptase complexed with nucleic acid: ...
Reduced cerebrospinal flu… - University of Gothenburg, Sweden
Cerebral Hemorrhage, Traumatic; Brain Hemorrhage, Cerebral, Traumatic; Cerebral Hematoma, Traumatic; Intracerebral Hemorrhage,...
"Proenkephalin-processing enzymes in chromaffin granules: model for neu" by Vivian Y. Hook, Martin R. Schiller et al.
Our finding that only PTP (not PC1/3, PC2, or the aspartic proteinase) possesses the ability to convert pro-NPY to NPY suggests ... Adrenal medulla; Adrenal Medulla/enzymology; Amino acid sequence; Animals; Aspartic acid; Aspartic Acid Endopeptidases/ ... Our finding that only PTP (not PC1/3, PC2, or the aspartic proteinase) possesses the ability to convert pro-NPY to NPY suggests ... Endopeptidases; Enkephalins; Enkephalins/metabolism; Enzymology; Furin; Humans; Men; Models; Biological; Molecular Sequence ...
Article abstract | Medical Science Monitor
Keywords: Aspartic Acid Endopeptidases - genetics, Amyloid beta-Peptides - metabolism, Amyloid Precursor Protein Secretases, ... Alzheimer Disease - prevention & control, Cell Line, Tumor, Endopeptidases - genetics, Gene Expression Regulation, Enzymologic ...
adenocarcinoma bile duct type liver 2005:2010[pubdate] *count=100 - BioMedLib™ search engine
Endopeptidases; EC 3.4.23.- / Aspartic Acid Endopeptidases; EC 220.127.116.11 / BACE1 protein, human; EC 18.104.22.168 / Bace1 protein, ... Aspartic Acid Endopeptidases. Bile Ducts / cytology. Cell Line, Transformed. Cholangitis, Sclerosing / metabolism. Cholangitis ... Nucleic Acid, Nucleoside, or Nucleotide. A22.214.171.124.1.6. Organophosphorus Compound. A126.96.36.199.1.7. Amino Acid, Peptide, or Protein ... A188.8.131.52.2. Amino Acid Sequence. A184.108.40.206.3. Carbohydrate Sequence. A220.127.116.11. Geographic Area. A2.2. Finding. A2.2.1. ...
rous sarcoma drug therapy 2000:2010[pubdate] *count=100 - BioMedLib™ search engine
Chemical-registry-number] 0 / Oligopeptides; 0 / Protease Inhibitors; EC 3.4.23.- / Aspartic Acid Endopeptidases; EC 3.4.23 ... Nucleic Acid, Nucleoside, or Nucleotide. A18.104.22.168.1.6. Organophosphorus Compound. A22.214.171.124.1.7. Amino Acid, Peptide, or Protein ... Amino Acid Sequence. Humans. Models, Molecular. Molecular Sequence Data. Sequence Homology, Amino Acid ... A126.96.36.199.2. Amino Acid Sequence. A188.8.131.52.3. Carbohydrate Sequence. A184.108.40.206. Geographic Area. A2.2. Finding. A2.2.1. ...
Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) and Proteome Quantitation of Mouse Embryonic Stem Cells to a...
... allowing for cleavage N-terminal to proline and between aspartic acid and proline (18). Carbamidomethylcysteine was set as a ... Achromobacter lyticus lysyl endopeptidase, and human keratins; a total of 52,355 forward entries) and concatenated with ... For the SILAC technology, cells are grown in the presence of light or heavy forms of amino acids, such as arginine and lysine. ... Rogers, M. B., Hosler, B. A., and Gudas, L. J. (1991) Specific expression of a retinoic acid-regulated, zinc-finger gene, Rex-1 ...
Protease Digestion for Mass Spectrometry | Protein Digest Protocols
Primarily on the N-terminal side of aspartic acid residues. Cleavage on the N-terminal side of glutamic acid residues can occur ... Arg-C, Sequencing Grade (Cat.# V1881), also known as clostripain, is an endopeptidase that cleaves at the C-terminus of ... In phosphate buffers, cleavage also occurs at aspartic acid residues. Glu-C activity is optimal at pH 4.0-9.0. ... is an endoproteinase that hydrolyzes peptide bonds at the N-terminal side of aspartic acid residues. Asp-N activity is optimal ...
Expression of active trypsin-like serine peptidases in the midgut of sugar-feeding female Anopheles aquasalis | Parasites &...
... aspartic acid and histidine [19, 20]. In mosquitoes, serine peptidases are related primarily to food digestion, and blood ... Peptidases are proteolytic enzymes that can be subdivided into endopeptidases and exopeptidases . Serine peptidases are a ... Mobile phase A consisted of 0.1 % (v/v) formic acid in water, and mobile phase B consisted of 0.1 % (v/v) formic acid in ... An analysis of the alignment of the amino acid sequence of these peptidases showed the following: (i) the conserved amino acid ...
Gag polyprotein - Avian myeloblastosis virus
aspartic-type endopeptidase activity Source: InterPro. *nucleic acid binding Source: InterPro. *structural molecule activity ... IPR001969. Aspartic_peptidase_AS. IPR004028. Gag_M. IPR000721. Gag_p24. IPR012344. Matrix_HIV/RSV_N. IPR001995. Peptidase_A2_ ... IPR001969. Aspartic_peptidase_AS. IPR004028. Gag_M. IPR000721. Gag_p24. IPR012344. Matrix_HIV/RSV_N. IPR001995. Peptidase_A2_ ... IPR021109. Peptidase_aspartic_dom_sf. IPR034170. Retropepsin-like_cat_dom. IPR018061. Retropepsins. IPR008916. Retrov_capsid_C ...
- Natural products inhibiting Candida albicans secreted aspartic proteases from Tovomita krukovii. (biomedsearch.com)
- Compounds 2, 3, 12 and 13 showed inhibitory effects against Candida albicans secreted aspartic proteases (SAP) with IC50 values of 15 microg/ml, 25 microg/ml, 40 microg/ml, and 6.5 microg/ml, respectively, while the other compounds were inactive. (biomedsearch.com)
- In biochemistry , serine proteases or serine endopeptidases (newer name) are a class of peptidases ( enzymes that cleave peptide bonds in proteins ) that are characterised by the presence of a serine residue in the active site of the enzyme . (bionity.com)
- Located very near one another near the heart of the enzyme, these three key amino acids each play an essential role in the cleaving ability of the proteases. (bionity.com)
- Proteases hydrolyze the peptide bonds of proteins into peptides and amino acids, being found in all living organisms, and are essential for cell growth and differentiation. (scielo.br)
- Proteases are classified as peptide hydrolases or peptidases (EC 3.4) and constitute a large family of enzymes, divided into endopeptidases (EC 3.4.21-99) and exopeptidases (EC 3.4.11-19), classified according to the position of the peptide bond to be cleaved. (scielo.br)
- Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. (wikipedia.org)
- Eukaryotic aspartic proteases include pepsins , cathepsins , and renins . (wikipedia.org)
- While a number of different mechanisms for aspartyl proteases have been proposed, the most widely accepted is a general acid-base mechanism involving coordination of a water molecule between the two highly conserved aspartate residues. (wikipedia.org)
- Five superfamilies (clans) of aspartic proteases are known, each representing an independent evolution of the same active site and mechanisms . (wikipedia.org)
- Positive and negative contributions have been described for other enzymes, including the aspartyl proteases cathepsins D and E and asparagine endopeptidase (AEP). (jimmunol.org)
- Therefore, PepA-P can be used in studying the role of intracellular aspartic proteases in the MHC class II antigen processing pathway. (edu.kz)
- Evolutionarily conserved functional mechanics across pepsin-like and retroviral aspartic proteases. (ebi.ac.uk)
- The threonine and glutamic acid proteases were not described until 1995 and 2004 , respectively. (wikidoc.org)
- Proteases are involved in digesting long protein chains into short fragments, splitting the peptide bonds that link amino acid residues. (wikidoc.org)
- Proteases are divided into four major groups according to the character of their catalytic active site and conditions of action: serine proteinases, cysteine (thiol) proteinases, aspartic proteinases, and metalloproteinases . (wikidoc.org)
- The two main groups of proteases are exopeptidases and endopeptidases. (pediaa.com)
- Presenelins are related to the signal peptide peptidase (SPP) family of aspartic proteases that promote intramembrane proteolysis to release biologically important peptides. (embl-heidelberg.de)
- In only one family of cysteine peptidases, is the role of the general base assigned to a residue other than a histidine: in peptidases from family C89 (acid ceramidase) an arginine is the general base. (ebi.ac.uk)
- Peptidases are proteolytic enzymes that can be subdivided into endopeptidases and exopeptidases [ 18 ]. (biomedcentral.com)
- The presence and position of disulfide bridges are other conserved features of aspartic peptidases. (wikipedia.org)
- The mechanism used to cleave a peptide bond involves making an amino acid residue that has the cysteine and threonine (peptidases) or a water molecule (aspartic acid, metallo- and glutamic acid peptidases) nucleophilic so that it can attack the peptide carbonyl group. (wikidoc.org)
- Peptidases can either break specific peptide bonds ( limited proteolysis ), depending on the amino acid sequence of a protein, or break down a complete peptide to amino acids ( unlimited proteolysis ). (wikidoc.org)
- Sedolisins are acid-acting endopeptidases or tripeptidyl peptidases. (expasy.org)
- This group of aspartic peptidases belong to MEROPS peptidase family A22 (presenilin family, clan AD). (embl-heidelberg.de)
- Proteins containing this domain belong to the aspartic peptidase A1 family (peptidase family A1, subfamily A1B). (ebi.ac.uk)
- Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism . (wikipedia.org)
- Dietary proteins are first broken down to individual amino acids by various enzymes and hydrochloric acid present in the gastrointestinal tract. (wikipedia.org)
- Proteins are made from amino acids. (wikipedia.org)
- Background Folding nucleus of globular proteins formation starts by the mutual interaction of a group of hydrophobic amino acids whose close contacts allow subsequent formation and stability of the 3D structure. (capecodmushroom.org)
- They hydrolyze peptide bonds between amino acids in both proteins and peptides. (pediaa.com)
- Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. (ebi.ac.uk)
- Asparagine endopeptidase (AEP) or legumain is a potentially important Ag-processing enzyme that introduces limited cleavages that trigger unfolding and class II MHC binding of different Ag substrates. (jimmunol.org)
- Amino acid CV, % Alanine 5.0 Arginine 6.8 Asparagine 8.6 Aspartic acid 7.4 Citrulline 8.8 Cystine 8.1 Glutamic acid 8.8 Glutamine 4.1 Glycine 5.2 Histidine 6.6 Isoleucine 9.0 Leucine 5.0 Lysine 4.0 Methionine 5.5 Ornithine 4.0 Phenylalanine 9.2 Proline 12.1 Serine 4.8 Taurine 7.3 Threonine 4.5 Tryptophan 9.8 Tyrosine 5.9 Valine 8.8 Table 3. (thefreedictionary.com)
- Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides . (wikipedia.org)
- Ecadotril is a neutral endopeptidase inhibitor ((NEP) EC 220.127.116.11) and determined by the presence of peptidase family M13 as a neutral endopeptidase inhibited by phosphoramidon. (wikipedia.org)
Peptides and amino acids1
- Daechon Kamakmen Bay Aspartic acid 16.5 (2.5) 18.5 (2.1) Glutamic acid 28.3 (7.7) 34.2 (6.8) Serine 13.2 (1.5) 10.1 (1.7) Glycine 69.0 (20.6) 42.8 (8.7) [beta]-Alanine 15.9 (3.3) 5.2 (0.1) Taurine 200.7 (48.3) 324.4 (45.1) L-Alanine 37.3 (11.0) 29.7 (7.2) T/G ratio 2.9 7.6 TOTAL 380.8 (91.9) 464.8 (60.6) TABLE 2. (thefreedictionary.com)
- Equal amount of aspartic acid and glutamic acid by weight were substituted for the graded amounts of methionine in the basal diet to maintain the isonitrogenous of the seven experimental diets. (thefreedictionary.com)
- Typically aspartic acid, glutamic acid. (docplayer.net)
- The proteolytic enzymes are subdivided into two major groups, exopeptidases and endopeptidases, depending on their site of action. (scielo.br)
- In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent, except for the catalytic site motif, which is very conserved. (wikipedia.org)
- Lombard V. et al "The carbohydrate-active enzymes database (CAZy) in 2013" Nucleic Acids Res. (wellnessadvocate.com)
- 4 . The process according to claim 1 , wherein the one or more proteolytic enzymes comprise both endopeptidase and exopeptidase activity. (google.ch)
- The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp (SED in single-letter notation), as well as the presence of an aspartic acid residue in the oxyanion hole. (expasy.org)
- Chymotrypsin is responsible for cleaving peptide bonds following a bulky hydrophobic amino acid residue. (bionity.com)
- Trypsin is responsible for cleaving peptide bonds following a positively-charged amino acid residue. (bionity.com)
- Instead of having the hydrophobic pocket of the chymotrypsin , there exists an aspartic acid residue at the base of the pocket. (bionity.com)
- Elastase is responsible for cleaving peptide bonds following a small neutral amino acid residue, such as Alanine , glycine and valine. (bionity.com)
- Aminopeptidases (EC 3.4.14) act at a free N terminus of the polypeptide chain and liberate a single amino acid residue, a dipeptide, or a tripeptide. (scielo.br)
- Insulin human is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. (drugbank.ca)
- Amino acid residue: the portion of the amino acid that remains after incorporation into a polypeptide chain. (docplayer.net)
- Moreover, the active site residue of pepsin is aspartic acid . (pediaa.com)
- Cloning, expression, and purification of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase: crystallization of nucleic acid complexes. (molmovdb.org)
- however they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. (expasy.org)
- Pepsin has a three-dimensional structure, of which one or more polypeptide chains twist and fold, bringing together a small number of amino acids to form the active site, or the location on the enzyme where the substrate binds and the reaction takes place. (wikidoc.org)
- Especially, pepsin is an endopeptidase that hydrolyzes internal peptide bonds. (pediaa.com)
- Furthermore, pepsin is responsible for the hydrolysis of peptide bonds between large hydrophobic amino acids. (pediaa.com)
- The results showed a decrease in the relative quantity of dimeric, trimeric and anhydrous units, and a smaller reduction in monomer disaccharide pentapeptide (M5) levels, validating the occurrence of D,D-carboxypeptidase and D,D-endopeptidase activities. (biomedcentral.com)
Internal peptide bonds1
- They are inhibited by thiol chelators such as iodoacetate, iodoacetic acid, N -ethylmaleimide or p -chloromercuribenzoate. (ebi.ac.uk)
- Acidic amino acids: Those whose side chains can carry a negative charge at certain ph values. (docplayer.net)
Amino acid sequences3
- A novel mutagenesis strategy identifies distantly spaced amino acid sequences that are required for the phosphorylation of both the oligosaccharides of procathepsin D by N-acetylglucosamine 1-phosphotransferase. (ox.ac.uk)
- Igs are produced in many different forms, each with different amino acid sequences and antigen binding sites. (shepherdsheart.life)
- DNA and Amino acid sequences are also provided on this block. (systemsbiology.net)