ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.
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.
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.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Comparative molecular genetic profiles of anaplastic astrocytomas/glioblastomas multiforme and their subsequent recurrences. (1/4803)

Malignant glial tumors (anaplastic astrocytomas and glioblastomas multiforme) arise mostly either from the progression of low grade precursor lesions or rapidly in a de novo fashion and contain distinct genetic alterations. There is, however, a third subset of malignant gliomas in which genetic lesions remain to be identified. Following surgical resection, all gliomas appear to have an inherent tendency to recur. Comparative molecular analysis of ten primary malignant gliomas (three anaplastic astrocytomas and seven glioblastomas multiforme) with their recurrences identified two distinct subgroups of recurrent tumors. In one group, primary tumors harbored genetic aberrations frequently associated with linear progression or de novo formation pathways of glial tumorigenesis and maintained their genetic profiles upon recurrence. In the other subset with no detectable known genetic mutations at first presentation, the recurrent tumors sustained specific abnormalities associated with pathways of linear progression or de novo formation. These included loss of genes on chromosomes 17 and 10, mutations in the p53 gene, homozygous deletion of the DMBTA1 and p16 and/ or p15 genes and amplification and/or overexpression of CDK4 and alpha form of the PDGF receptor. Recurrent tumors from both groups also displayed an abnormal expression profile of the metalloproteinase, gel A, and its inhibitor, TIMP-2, consistent with their highly invasive behavior. Delineation of the molecular differences between malignant glioblastomas and their subsequent recurrences may have important implications for the development of rational clinical approaches for this neoplasm that remains refractory to existing therapeutic modalities.  (+info)

Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinases in human astrocytic tumors. (2/4803)

Three different membrane-type matrix metalloproteinases (MT1-, MT2-, and MT3-MMPs) are known to activate in vitro the zymogen of MMP-2 (pro-MMP-2, progelatinase A), which is one of the key MMPs in invasion and metastasis of various cancers. In the present study, we have examined production and activation of pro-MMP-2, expression of MT1-, MT2-, and MT3-MMPs and their correlation with pro-MMP-2 activation, and localization of MMP-2, MT1-MMP, and MT2-MMP in human astrocytic tumors. The sandwich enzyme immunoassay demonstrates that the production levels of pro-MMP-2 in the anaplastic astrocytomas and glioblastomas are significantly higher than that in the low-grade astrocytomas (P<0.05 and P<0.01, respectively), metastatic brain tumors (P<0.05), or normal brains (P<0.01). Gelatin zymography indicates that the pro-MMP-2 activation ratio is significantly higher in the glioblastomas than in other astrocytic tumors (P<0.01), metastatic brain tumors (P<0.01), and normal brains (P<0.01). The quantitative reverse transcription polymerase chain reaction analyses demonstrate that MT1-MMP and MT2-MMP are expressed predominantly in glioblastoma tissues (17/17 and 12/17 cases, respectively), and their expression levels increase significantly as tumor grade increases. MT3-MMP is detectable in both astrocytic tumor and normal brain tissues, but the mean expression level is approximately 50-fold lower compared with that of MT1-MMP and MT2-MMP in the glioblastomas. The activation ratio of pro-MMP-2 correlates directly with the expression levels of MT1-MMP and MT2-MMP but not MT3-MMP. In situ hybridization indicates that neoplastic astrocytes express MT1-MMP and MT2-MMP in the glioblastoma tissues (5/5 cases and 5/5 cases, respectively). Immunohistochemically, MT1-MMP and MT2-MMP are localized to the neoplastic astrocytes in glioblastoma samples (17/17 cases and 12/17 cases, respectively), which are also positive for MMP-2. In situ zymography shows gelatinolytic activity in the glioblastoma tissues but not in the normal brain tissues. These results suggest that both MT1-MMP and MT2-MMP play a key role in the activation of pro-MMP-2 in the human malignant astrocytic tumors and that the gelatinolytic activity is involved in the astrocytic tumor invasion.  (+info)

Enhanced tumor growth and invasiveness in vivo by a carboxyl-terminal fragment of alpha1-proteinase inhibitor generated by matrix metalloproteinases: a possible modulatory role in natural killer cytotoxicity. (3/4803)

Matrix metalloproteinases (MMPs) are believed to contribute to the complex process of cancer progression. They also exhibit an alpha1-proteinase inhibitor (alphaPI)-degrading activity generating a carboxyl-terminal fragment of approximately 5 kd (alphaPI-C). This study reports that overexpression of alphaPI-C in S2-020, a cloned subline derived from the human pancreas adenocarcinoma cell line SUIT-2, potentiates the growth capability of the cells in nude mice. After stable transfection of a vector containing a chimeric cDNA encoding a signal peptide sequence of tissue inhibitor of metalloproteinase-1 followed by cDNA for alphaPI-C into S2-020 cells, three clones that stably secrete alphaPI-C were obtained. The ectopic expression of alphaPI-C did not alter in vitro cellular growth. However, subcutaneous injection of the alphaPI-C-secreting clones resulted in tumors that were 1.5 to 3-fold larger than those of control clones with an increased tendency to invasiveness and lymph node metastasis. These effects could be a result of modulation of natural killer (NK) cell-mediated control of tumor growth in nude mice, as the growth advantage of alphaPI-C-secreting clones was not observed in NK-depleted mice, and alphaPI-C-secreting clones showed decreased NK sensitivity in vitro. In addition, production of alphaPI and generation of the cleaved form of alphaPI by MMP were observed in various human tumor cell lines and in a highly metastatic subline of SUIT-2 in vitro. These results provide experimental evidence that the alphaPI-degrading activity of MMPs may play a role in tumor progression not only via the inactivation of alphaPI but also via the generation of alphaPI-C.  (+info)

Collagenase-3 (MMP-13) is expressed by tumor cells in invasive vulvar squamous cell carcinomas. (4/4803)

Collagenase-3 (MMP-13) is a human matrix metalloproteinase specifically expressed by invading tumor cells in squamous cell carcinomas (SCCs) of the head and neck. Here, we have further elucidated the role of MMP-13 in tumor invasion by examining its expression in invasive malignant tumors of the female genital tract. Using in situ hybridization, expression of MMP-13 mRNA was detected in 9 of 12 vulvar SCCs, primarily in tumor cells, but not in intact vulvar epithelium, in cervical SCCs (n = 12), or in endometrial (n = 11) or ovarian adenocarcinomas (n = 8). MMP-13 expression was especially abundant in vulvar carcinomas showing metastasis to lymph nodes and was associated with expression of membrane type 1 MMP by tumor cells and gelatinase-A (MMP-2) by stromal cells, as detected by immunohistochemistry. MMP-13 mRNAs were detected in 9 of 11 cell lines established from vulvar carcinomas and in 4 of 6 cell lines from cervical carcinomas, whereas endometrial (n = 10) and ovarian (n = 9) carcinoma cell lines were negative for MMP-13 mRNA. No correlation was detected between MMP-13 expression and p53 gene mutations in vulvar SCC cell lines. However, MMP-13 expression was detected in 5 of 6 vulvar and cervical SCC cell lines harboring HPV 16 or 68 DNA. These results show that MMP-13 is specifically expressed by malignantly transformed squamous epithelial cells, including vulvar SCC cells, and appears to serve as a marker for their invasive capacity.  (+info)

The cytoplasmic carboxy-terminal amino acid determines the subcellular localization of proTGF-(alpha) and membrane type matrix metalloprotease (MT1-MMP). (5/4803)

Transforming growth factor alpha (TGF-(alpha)) is synthesized as a precursor transmembrane molecule (proTGF-(alpha)) whose ectodomain is shed from the cell surface generating mature, soluble, growth factor. In agreement with recent reports, here we show that the structural determinant that targets proTGF-(alpha) to the cell surface maps to the very C-terminal cytoplasmic amino acid, valine. The primary localization of proTGF-(alpha) C-terminal mutants is a perinuclear area that colocalizes with ER markers. Since the ectodomain shedding machinery that acts on proTGF-(alpha) is known to be located at the cell surface, deficient transport provides an explanation for the previously reported lack of PKC activated ectodomain shedding of proTGF-(alpha) C-terminal mutants. The transport of wild-type proTGF-(alpha) to the cell surface was found to be mediated by a mechanism that includes a specific component saturable by wild-type proTGF-(alpha) but not by cell surface transmembrane proteins whose trafficking is independent of their cytoplasmic tail such as betaglycan. C-terminal valines are likely to be a general determinant of the subcellular location of cell surface transmembrane proteins since the maturation and trafficking of MT1-MMP C-terminal mutants are severely impaired. Our data suggest the existence of a targeting mechanism that acts on cell surface transmembrane molecules as diverse as proTGF-(alpha) and MT1-MMP and that the interaction with such a mechanism depends on the identity of the C-terminal amino acid of the targeted molecules.  (+info)

A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties. (6/4803)

Computer-based database searching and protein multiple sequence alignment has identified a novel clan of zinc metallopeptidases, which, by phylogenetic analysis, has been shown to contain six subfamilies. The family is characterized by four common transmembrane segments and three conserved sequence motifs. The combination of topology analysis and motif identification has detected three potential Zn2+ coordinating residues. Only two of the sequences of this novel zinc metallopeptidase clan possess any functional annotation, one of which is able to cleave its substrate within a cytosol/transmembrane segment junction. A number of observations suggest that the remaining members of this novel clan may also cleave their substrates within transmembrane segments.  (+info)

Expression of stromelysin-3 in atherosclerotic lesions: regulation via CD40-CD40 ligand signaling in vitro and in vivo. (7/4803)

Stromelysin-3 is an unusual matrix metalloproteinase, being released in the active rather than zymogen form and having a distinct substrate specificity, targeting serine proteinase inhibitors (serpins), which regulate cellular functions involved in atherosclerosis. We report here that human atherosclerotic plaques (n = 7) express stromelysin-3 in situ, whereas fatty streaks (n = 5) and normal arterial specimens (n = 5) contain little or no stromelysin-3. Stromelysin-3 mRNA and protein colocalized with endothelial cells, smooth muscle cells, and macrophages within the lesion. In vitro, usual inducers of matrix metalloproteinases such as interleukin-1, interferon-gamma, or tumor necrosis factor alpha did not augment stromelysin-3 in vascular wall cells. However, T cell-derived as well as recombinant CD40 ligand (CD40L, CD154), an inflammatory mediator recently localized in atheroma, induced de novo synthesis of stromelysin-3. In addition, stromelysin-3 mRNA and protein colocalized with CD40L and CD40 within atheroma. In accordance with the in situ and in vitro data obtained with human material, interruption of the CD40-CD40L signaling pathway in low density lipoprotein receptor-deficient hyperlipidemic mice substantially decreased expression of the enzyme within atherosclerotic plaques. These observations establish the expression of the unusual matrix metalloproteinase stromelysin-3 in human atherosclerotic lesions and implicate CD40-CD40L signaling in its regulation, thus providing a possible new pathway that triggers complications within atherosclerotic lesions.  (+info)

Dynorphin A processing enzyme: tissue distribution, isolation, and characterization. (8/4803)

Limited proteolysis of the dynorphin precursor (prodynorphin) at dibasic and monobasic processing sites results in the generation of bioactive dynorphins. In the brain and neurointermediate lobe of the pituitary, prodynorphin is processed to produce alpha and beta neo endorphins, dynorphins (Dyn) A-17 and Dyn A-8, Dyn B-13, and leucine-enkephalin. The formation of Dyn A-8 from Dyn A-17 requires a monobasic cleavage between Ile and Arg. We have identified an enzymatic activity capable of processing at this monobasic site in the rat brain and neurointermediate lobe of the bovine pituitary; this enzyme is designated "dynorphin A-17 processing enzyme." In the rat brain and neurointermediate lobe, a majority of the Dyn A processing enzyme activity is membrane-associated and can be released by treatment with 1% Triton X-100. This enzyme has been purified to apparent homogeneity from the membrane extract of the neurointermediate lobe using preparative iso-electrofocussing in a granulated gel pH 3.5 to 10, FPLC using anion exchange chromatography, and non-denaturing electrophoresis. The Dyn A processing enzyme exhibits a pI of about 5.8 and a molecular mass of about 65 kDa under reducing conditions. The Dyn A processing enzyme is a metalloprotease and has a neutral pH optimum. It exhibits substantial sensitivity to metal chelating agents and thiol agents suggesting that this enzyme is a thiol-sensitive metalloprotease. Specific inhibitors of other metallopeptidases such as enkephalinase [EC 3.4.24.11], the enkephalin generating neutral endopeptidase [EC 3.4.24.15], or NRD convertase do not inhibit the Dyn A processing enzyme activity. In contrast, specific inhibitors of angiotensin converting enzyme inhibit the activity. The purified enzyme is able to process a number of neuropeptides at both monobasic and dibasic sites. These characteristics are consistent with a role for the Dyn A processing enzyme in the processing of Dyn A-17 and other neuropeptides in the brain.  (+info)

Metalloendopeptidases are a type of enzymes that cleave peptide bonds in proteins, specifically at interior positions within the polypeptide chain. They require metal ions as cofactors for their catalytic activity, typically zinc (Zn2+) or cobalt (Co2+). These enzymes play important roles in various biological processes such as protein degradation, processing, and signaling. Examples of metalloendopeptidases include thermolysin, matrix metalloproteinases (MMPs), and neutrophil elastase.

"Streptomyces griseus" is a species of bacteria that belongs to the family Streptomycetaceae. This gram-positive, aerobic, and saprophytic bacterium is known for its ability to produce several important antibiotics, including streptomycin, grisein, and candidin. The bacterium forms a branched mycelium and is commonly found in soil and aquatic environments. It has been widely studied for its industrial applications, particularly in the production of antibiotics and enzymes.

The medical significance of "Streptomyces griseus" lies primarily in its ability to produce streptomycin, a broad-spectrum antibiotic that is effective against many gram-positive and gram-negative bacteria, as well as some mycobacteria. Streptomycin was the first antibiotic discovered to be effective against tuberculosis and has been used in the treatment of this disease for several decades. However, due to the emergence of drug-resistant strains of Mycobacterium tuberculosis, streptomycin is now rarely used as a first-line therapy for tuberculosis but may still be used in combination with other antibiotics for the treatment of multidrug-resistant tuberculosis.

In addition to its role in antibiotic production, "Streptomyces griseus" has also been studied for its potential use in bioremediation and as a source of novel enzymes and bioactive compounds with potential applications in medicine and industry.

Zinc is an essential mineral that is vital for the functioning of over 300 enzymes and involved in various biological processes in the human body, including protein synthesis, DNA synthesis, immune function, wound healing, and cell division. It is a component of many proteins and participates in the maintenance of structural integrity and functionality of proteins. Zinc also plays a crucial role in maintaining the sense of taste and smell.

The recommended daily intake of zinc varies depending on age, sex, and life stage. Good dietary sources of zinc include red meat, poultry, seafood, beans, nuts, dairy products, and fortified cereals. Zinc deficiency can lead to various health problems, including impaired immune function, growth retardation, and developmental delays in children. On the other hand, excessive intake of zinc can also have adverse effects on health, such as nausea, vomiting, and impaired immune function.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

... at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Articles ... A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. Glucksman MJ, Orlowski M, Roberts JL ( ... April 1992). "Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin ...
IgA-specific+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... IgA-specific metalloendopeptidase (EC 3.4.24.13, immunoglobulin A1 proteinase, IgA protease, IgA1-specific proteinase, IgA1 ...
Beta-lytic+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... Beta-lytic metalloendopeptidase (EC 3.4.24.32, Myxobacter beta-lytic proteinase, achromopeptidase component, beta-lytic ...
Peptidyl-Lys+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... Peptidyl-Lys metalloendopeptidase (EC 3.4.24.20, Armillaria mellea neutral proteinase, peptidyllysine metalloproteinase) is an ...
Peptidyl-Asp+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ... Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33, endoproteinase Asp-N, peptidyl-Asp metalloproteinase) is an enzyme. This ... Hagmann ML, Geuss U, Fischer S, Kresse GB (1995). Peptidyl-Asp metalloendopeptidase. Methods in Enzymology. Vol. 248. pp. 782- ... cysteic acid bonds Peptidyl-Asp metalloendopeptidase was first discovered when it was isolated from the supernatant of ...
... metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ADAM proteins and matrix metalloproteinases, and M16 ...
J. S. Bond & R. J. Benyon (1995). "The astacin family of metalloendopeptidases". Protein Science. 4 (7): 1247-1261. doi:10.1002 ...
Norman MU, Lew RA, Smith AI, Hickey MJ (June 2003). "Metalloendopeptidases EC 3.4.24.15/16 regulate bradykinin activity in the ... Neurolysin, with 704 amino acid residues, is a zinc metalloendopeptidase with a conserved HEXXH motif. It has an overall ... Shrimpton CN, Smith AI, Lew RA (October 2002). "Soluble metalloendopeptidases and neuroendocrine signaling". Endocrine Reviews ... "Identification of membrane-bound variant of metalloendopeptidase neurolysin (EC 3.4.24.16) as the non-angiotensin type 1 (non- ...
The astacin family of metalloendopeptidases (EC 3.4.24.21) encompasses a range of proteins found in hydra to humans, in mature ... Bond JS, Beynon RJ (July 1995). "The astacin family of metalloendopeptidases". Protein Science. 4 (7): 1247-61. doi:10.1002/pro ... Proteins containing the astacin domain include: Astacin-like metallo-endopeptidase (ASTL) Bone morphogenetic protein 1 (BMP1) ... Astacins are a family of multidomain metalloendopeptidases which are either secreted or membrane-anchored. These ...
Murphy, G; Willenbrock, F (1995). "[30] Tissue inhibitors of matrix metalloendopeptidases". Proteolytic Enzymes: Aspartic and ...
Jiang W, Le B (2000). "Structure and expression of the human MEP1A gene encoding the alpha subunit of metalloendopeptidase ... 1991). "The astacin family of metalloendopeptidases". J. Biol. Chem. 266 (32): 21381-5. doi:10.1016/S0021-9258(18)54648-2. PMID ... for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively". Genomics ...
Blumberg S, Tauber Z (October 1983). "Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides". European Journal of ...
Rawlings, N.D.; Barrett, A.J. (1991). "Homologues of insulinase, a new superfamily of metalloendopeptidases". Biochem. J. 275 ( ...
"Entrez Gene: Membrane metallo-endopeptidase". Galy, Anne; Travis, Marilyn; Cen, Dazhi; Chen, Benjamin (Oct 1995). "Human T, B, ... Neprilysin (/ˌnɛprɪˈlaɪsɪn/), also known as membrane metallo-endopeptidase (MME), neutral endopeptidase (NEP), cluster of ...
"MME membrane metalloendopeptidase [Homo sapiens (human)]". www.ncbi.nlm.nih.gov. Retrieved 2022-02-06. Campbell DJ (2018-09-19 ...
Orlowski M, Michaud C, Chu TG (1983). "A soluble metalloendopeptidase from rat brain. Purification of the enzyme and ... involvement of a thermolysin-like metalloendopeptidase (enkephalinase), angiotensin-converting enzyme, and other unidentified ...
TOP2 (also known as thimet metalloendopeptidase 2) is located in the cytosol and has the AT5G10540 gene. The distinctive genes ... Orlowski M, Michaud C, Chu TG (September 1983). "A soluble metalloendopeptidase from rat brain. Purification of the enzyme and ... Tisljar U (February 1993). "Thimet oligopeptidase--a review of a thiol dependent metallo-endopeptidase also known as Pz- ... TOP1 (also known as OOP, organellar oligopeptidase, TOPorg, and thimet metalloendopeptidase 1) is located in the mitochondria ...
Turner AJ, Isaac RE, Coates D (March 2001). "The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function ...
Membrane metallo-endopeptidase-like 1 is a protein that in humans is encoded by the MMEL1 gene. The protein encoded by this ... "Entrez Gene: Membrane metallo-endopeptidase-like 1". Whyteside AR, Turner AJ (July 2008). "Human neprilysin-2 (NEP2) and NEP ... gene is a member of the neutral endopeptidase (NEP) or membrane metallo-endopeptidase (MME) family. Family members play ...
Ferro ES, Tullai JW, Glucksman MJ, Roberts JL (1999). "Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)". DNA Cell Biol. ... 1999). "The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane". ... "Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate ...
Becker AB, Roth RA (May 1992). "An unusual active site identified in a family of zinc metalloendopeptidases". Proceedings of ... Anastasi A, Knight CG, Barrett AJ (March 1993). "Characterization of the bacterial metalloendopeptidase pitrilysin by use of a ...
Astacin-like metalloendopeptidase is a protein that in humans is encoded by the ASTL gene. GRCh38: Ensembl release 89: ... "ASTL - Astacin-like metalloendopeptidase precursor - Homo sapiens (Human) - ASTL gene & protein". www.uniprot.org. Retrieved 16 ... "Entrez Gene: Astacin-like metallo-endopeptidase (M12 family)". Human ASTL genome location and ASTL gene details page in the ...
Its structure is similar to that of the M23 family of metalloendopeptidases. Unlike this family of peptidases, however, LECT2 ... Reveals a Mechanistic Basis of Functional Evolution in a Mammalian Protein with an M23 Metalloendopeptidase Fold". The Journal ... has not been found to possess enzymatic activity and does not appear to share any functions with M23 metalloendopeptidases. ...
"Menoufia University, Genetic Engineering and Biotechnology Research Institute describes research in metalloendopeptidases". ...
This membrane-bound metalloendopeptidase is present in mouse intestines. Kounnas MZ, Wolz RL, Gorbea CM, Bond JS (September ...
... (EC 3.4.24.51, Ophiophagus metalloendopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction ...
Nonaka, T; Y Hashimoto; K Takio (1998). "Kinetic characterization of lysine-specific metalloendopeptidases from Grifola ... "Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase". Nat Methods. 5 (5): 405-407. doi:10.1038/ ...
... is a metalloendopeptidase found in the mushroom Grifola frondosa that cleaves proteins on the amino side of lysine ... "Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase". Nature Methods. 5 (5): 405-7. doi:10.1038/ ... "Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies ...
Membrane metallo-endopeptidase". Flick, Andrew C.; Ding, Hong X.; Leverett, Carolyn A.; Kyne, Robert E.; Liu, Kevin K. -C.; ...
Metalloendopeptidase OMA1, mitochondrial is an enzyme that in humans is encoded by the OMA1 gene. OMA1 is a Zn2+-dependent ... OMA1 has a HEXXH Zn2+-binding motive and the MEROPS database classifies OMA1 as metalloendopeptidase of the M48C-family. OMA1's ... metalloendopeptidase in the inner membrane of mitochondria. The OMA1 acronym was derived from overlapping proteolytic activity ...
Metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Articles ... A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. Glucksman MJ, Orlowski M, Roberts JL ( ... April 1992). "Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin ...
GO:0004222: metalloendopeptidase activity (Molecular function). Catalysis of the hydrolysis of internal, alpha-peptide bonds ...
Metalloendopeptidases * SPG7 protein, human * Adenosine Triphosphatases * ATPases Associated with Diverse Cellular Activities ...
enables metalloendopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ...
... metalloendopeptidase; muscarinic receptors; oxidant injury; tachykinins; trachealis muscle ...
MMP Inhibitors on signaling pathway are available at Adooq Bioscience. Check MMP pathway , inhibitors reviews and assay information.
EC 3.4.24.* (metalloendopeptidase) inhibitor + matrix metalloproteinase inhibitor + protease inhibitor + A compound which ...
Soluble metalloendopeptidases and neuroendocrine signaling.. Journal. Endocr Rev 23:647-64 (2002). DOI:10.1210/er.2001-0032 ...
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27. ...
This cell surface metalloendopeptidase inactivates a number of signaling molecules and serves as a major regulator in the ... This cell surface metalloendopeptidase inactivates a number of signaling molecules and serves as a major regulator in the ... This cell surface metalloendopeptidase inactivates a number of signaling molecules and serves as a major regulator in the ... CD10 is encoded by MME (membrane metallo-endopeptidase). CD10 is a 100 kDa type II transmembrane glycoprotein that has neutral ...
endopeptidase activity metalloendopeptidase activity serine-type endopeptidase activity calcium ion binding protein binding ... MMP3 is capable of binding to zinc and calcium ions, and has metallo-endopeptidase activity. The active enzyme degrades ...
1999) Cloning and characterization of Aplysia neutral endopeptidase, a metallo-endopeptidase involved in the extracellular ...
Turner AJ, Isaac RE and Coates D: The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function. Bioessays. ...
Crotalus horridus metalloendopeptidase; hemorrhagic proteinase IV; Crotalus horridus horridus venom hemorrhagic proteinase. ...
MATH domains are present in mammalian tissue-specific metalloendopeptidases (meprins) and TNF receptor associated factor (TRAF ...
Metalloendopeptidases (MeSH) * Middle Aged (MeSH) * Myocardial Infarction (MeSH) * Survival Rate (MeSH) * Thrombolytic Therapy ...
metalloendopeptidase activity of MMP15 [plasma membrane] Physical Entity MMP15 [plasma membrane] (Homo sapiens) ...
Predicted to have metalloendopeptidase activity. Predicted to be involved in collagen catabolic process; extracellular matrix ...
Metalloendopeptidases [D08.811.277.656.300.480]. *Matrix Metalloproteinases [D08.811.277.656.300.480.525]. *Matrix ...
membrane metalloendopeptidase [Sourc.... MOCS2. 4338. MOCS2. molybdenum cofactor synthesis 2 [Sou.... MREG. 55686. MREG. ...
endopeptidase activity / integrin binding / metalloendopeptidase activity / metallopeptidase activity / protein ...
Metalloendopeptidases [D08.811.277.656.300.480] * Matrix Metalloproteinases [D08.811.277.656.300.480.525] * Matrix ... Metalloendopeptidases [D08.811.277.656.675.374] * Matrix Metalloproteinases [D08.811.277.656.675.374.525] * Matrix ... 2007; MATRIX METALLOPROTEINASE 16 was indexed under MATRIX METALLOPROTEINASES 2006 & under METALLOENDOPEPTIDASES 2005. History ...
GO:0004222 metalloendopeptidase activity GO:0005578 proteinaceous extracellular matrix GO:0006508 proteolysis GO:0008270 zinc ...
Metalloendopeptidases. 21. + 88. Somatostatin. 20. + 89. Opsonin Proteins. 20. + 90. Ethyldimethylaminopropyl Carbodiimide. 20 ...
METALLOENDOPEPTIDASES. MITOMYCIN C. MITOMYCIN. MUCOLIPIDOSIS. MUCOLIPIDOSES. MUSCULAR DYSTROPHY. MUSCULAR DYSTROPHIES. MYOTONIA ...
METALLOENDOPEPTIDASES. MITOMYCIN C. MITOMYCIN. MUCOLIPIDOSIS. MUCOLIPIDOSES. MUSCULAR DYSTROPHY. MUSCULAR DYSTROPHIES. MYOTONIA ...
  • A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. (wikipedia.org)
  • Phosphoramidon Disodium Salt is a metalloendopeptidase inhibitor. (adooq.com)
  • Predicted to have metalloendopeptidase activity. (zfin.org)
  • Vertebrate bone morphogenic protein 1 (BMP-1), a protein which induces cartilage and bone formation and expresses metalloendopeptidase activity. (embl.de)
  • 7. Homo- and heterotetrameric forms of the membrane-bound metalloendopeptidases meprin A and B. (nih.gov)
  • Serrapeptase is an extracellular metalloendopeptidase consisting of 470 amino acids and contains a zinc atom at the active site, which plays a vital role in its ability to cleave peptides. (enzyscience.com)
  • ENDOPEPTIDASAS que usan un metal como el ZINC en el mecanismo catalítico. (bvsalud.org)
  • One such protease, neprilysin (NEP), a zinc metalloendopeptidase, has been identified as a critical Aβ-degrading enzyme in the CNS. (nih.gov)
  • These genomic regions contained putative virulence genes relevant of BBD, such as an NAD-dependent epimerase/dehydratase (a gene with homologue function to the third and fourth most expressed gene in BBD), lysozyme/metalloendopeptidases and other genes for lipopolysaccharide modification. (edu.au)
  • 18. Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities. (nih.gov)