Description Carboxypeptidase M (CPM) is a membrane-bound zinc-dependent protease that cleaves C-terminal basic residues, such as arginine or lysine, from peptides/proteins. (razikurd.ir)
Because these residues work as docking sites for plasmin and tPA, small plasmin is certainly generated in the lack of these carboxy-terminal lysine and arginine residues, thus safeguarding the clot against degradation6. (cell-signaling-pathways.com)
Endoproteinase Lys-C is a serine protease specific for cleavage of amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues. (marvelgent.com)
Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. (marvelgent.com)
Secreted as a component of pancreatic juice, it is decomposed right into activated trypsin by the limitation of enterokinase or trypsin, which is an endopeptidase that can cut off the carboxyl side of lysine and also arginine residues in the polypeptide chain. (zhishangchemical.com)
The active site contains an aspartate residue for acid-base catalysis, and a carboxylated lysine and four histidine residues for binding of a binuclear metal centre. (scilifelab.se)
To examine the role of water penetration, we have measured the 17O and 2H magnetic relaxation dis- persions (MRD) for the V66E and V66K mutants of staphylococcal nuclease, where glutamic acid and lysine residues are buried in predominantly apolar environments. (lu.se)
[4] At the C-terminus Carboxypeptidase E then removes the terminal lysine and arginine residues. (wikidoc.org)
A carboxypeptidase that is specific for proteins that contain two ALANINE residues on their C-terminal. (nih.gov)
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. (wakehealth.edu)
Proteins4
A carboxypeptidase that removes C-terminal lysine or arginine from peptides and proteins. (bvsalud.org)
When plasminogen is bound to cell-surface proteins with C-terminal lysines via its lysine binding sites, its activation to plasmin is accelerated, and cell-bound plasmin is protected from inactivation by natural inhibitors. (imrpress.com)
Two pathways for modulation of plasminogen receptors have been characterized: A protease-dependent pathway can either up-regulate or down-regulate plasminogen binding to cells by changing the availability of plasminogen-binding proteins with C-terminal lysines. (imrpress.com)
An Evaluation Study of Heat- Processing Effects on Flour Proteins by Digestive Enzymes-Pepsin, Trypsin, and Trypsin-Carboxypeptidase-B. (cerealsgrains.org)
Peptidase4
The "4" places lysine carboxypeptidase in the "peptidase" subclass. (wikipedia.org)
재료 CNBr 활성 Sepharose 4B, amino peptidase, carboxypeptidase A, carboxypeptidase B, carboxypeptidase Y는 Sigma(St. Louis, MO) 제를, Bondapak C18 10 μM 컬럼은 W a t e r s (Milford, MA)제를 사용하였고, Nε - (γ- g l utamyl) lysine은 미국 N I H의 Folk 박사로 부터 제공받았다. (ksoem.or.kr)
On prostate cancer (PC) cells, the cell surface enzyme prostate-specific membrane antigen (PSMA), also known as glutamate carboxypeptidase II or N -acetyl- l -aspartyl- l -glutamate peptidase, is highly upregulated, whereas it shows low or no expression in the normal prostate ( 3 ). (snmjournals.org)
Thrombin Activatab2
Mature thrombin activatable fibrinolysis inhibitor (TAFIa) is a carboxypeptidase that stabilizes fibrin clots by detatching C-terminal arginines and lysines from partially degraded fibrin. (cell-signaling-pathways.com)
The carboxypeptidase TAFIa (triggered thrombin activatable fibrinolysis inhibitor) is usually a central participant in fibrinolysis (Assisting Information, Body S1)4,5. (cell-signaling-pathways.com)
Peptidyl-L-lysine2
Lysine carboxypeptidase is also known as: carboxypeptidase N arginine carboxypeptidase kininase I anaphylatoxin inactivator plasma carboxypeptidase B creatine kinase conversion factor bradykinase kininase Ia hippuryllysine hydrolase bradykinin-decomposing enzyme protaminase CPase N creatinine kinase convertase peptidyl-L-lysine(-L-arginine) hydrolase CPN All enzymes are assigned an Enzyme Commission number based on the chemical reaction they catalyze. (wikipedia.org)
The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. (rush.edu)
Carboxy-terminal1
TAFIa gets rid of carboxy-terminal lysines and arginines from partly degraded fibrin. (cell-signaling-pathways.com)
Amino acids2
Carboxypeptidase C & Y: (citrus leaves, yeast) all amino acids. (flashcardmachine.com)
Carboxypeptidase B catalyzes the hydrolysis of basic amino acids lysine, arginine, and histidine at the C-terminal end of polypeptides. (marvelgent.com)
Preferential1
Preferential release of a C-terminal lysine or arginine amino acid. (cathdb.info)
Prostate-specific membrane antigen2
Several radiolabeled prostate-specific membrane antigen (PSMA) inhibitors based on the lysine-urea-glutamate (KuE) motif as the pharmacophore proved to be suitable tools for PET/SPECT imaging of the PSMA expression in prostate cancer patients. (tum.de)
PURPOSE: [68Ga]Trishydroxypyridinone (THP)-prostate-specific membrane antigen (PSMA) is a novel tracer that can be labeled in one step by cold reconstitution of a kit with unprocessed generator eluate, targeting PSMA via the lysine-urea-glutamate (KuE) motif. (tum.de)
Carboxyl1
Enterokinase is a specific protease that cleaves at the carboxyl side of Lysine residue when it is preceded by four Aspartic acids (Asp-Asp-Asp-Asp-Lys) and is not followed by Proline. (marvelgent.com)
The recombinant protein is N-terminally truncated, thermostable, has optimal activity at pH ~6 and 66°C, and is more efficient in ochratoxin A hydrolysis than carboxypeptidase A and Y, the two previously known enzymes capable of degrading this mycotoxin. (scilifelab.se)
Exopeptidase1
This subclass first defines lysine carboxypeptidase as an exopeptidase (sub-subclasses 11 and 13-19) which means that it only acts on terminal bonds of a polypeptide chain. (wikipedia.org)
Catalytic1
It also contains the catalytic and substrate binding areas and is thus referred to as the carboxypeptidase domain. (wikipedia.org)
Enzyme found1
However, standard administration in the form of capsules may have a limited effect in the body because GHK is highly sensitive to the action of carboxypeptidase (20), an enzyme found in the gut. (proteinexplorer.org)
Receptors1
Following central idea of chemical substance genetics that equivalent receptors bind equivalent ligands20, the experience of anabaenopeptins against carboxypeptidase A motivated their check against TAFIa. (cell-signaling-pathways.com)
Mutants1
Partial activation of lysine mutants by K+ and NH4+ represents a throwback to the primordial state of the 1st substrate promiscuous family member. (bio-cavagnou.info)
Membrane1
Carboxypeptidase M, also known as CPM, is a membrane-bound arginine/lysine carboxypeptidase which is a member of the carboxypeptidases family. (betalifesci.com)
Reaction1
This enzyme catalyses the following chemical reaction: Release of a C-terminal basic amino acid (lysine or arginine), preferentially lysine. (wikipedia.org)
The human copper-binding peptide GHK-Cu (glycyl-l-histidyl-l-lysine) is a small, naturally occurring tri-peptide present in human plasma that also can be released from tissues in case of an injury. (proteinexplorer.org)
Molecular1
Lysine carboxypeptidase has a molecular weight of between 270 and 330 kDa (kilodaltons). (wikipedia.org)
Distinct1
Lysine carboxypeptidase can be found in nearly 400 distinct species, all being jawed vertebrates. (wikipedia.org)
Primary2
Breddam, K., Sørensen, S.B. and Svendsen, I. Primary structure and enzymatic properties of carboxypeptidase II from wheat bran. (enzyme-database.org)
A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. (rush.edu)
Blood3
Metabolically stable bradykinin B2 agonists, methionine-lysine-bradykinin and labradimil, had differential effects on the transvascular flow rate of Gd-DTPA across the blood-brain tumor barrier. (biomedcentral.com)
Both methionine-lysine-bradykinin and labradimil increased the blood half-life of Gd-DTPA sufficiently enough to increase significantly the tumor tissue Gd-DTPA area under the time-concentration curve. (biomedcentral.com)
Metabolically stable bradykinin B2 receptor agonists, methionine-lysine-bradykinin and labradimil, enhance the transvascular delivery of small chemotherapy drugs across the BBTB of malignant gliomas by increasing the blood half-life of the co-infused drug. (biomedcentral.com)
Function3
Dmochowska, A., Dignard, D., Henning, D., Thomas, D.Y. and Bussey, H. Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and α-factor precursor processing. (enzyme-database.org)
the pseudo C-terminal residue is certainly from the -amino function of lysine-2 via an ureido connection. (cell-signaling-pathways.com)
or receptor function may be lost by removal of C-terminal lysines. (imrpress.com)
Specifically2
It is more specifically a carboxypeptidase (sub-subclasses 16-18) which acts on a C-terminus to break off one amino acid. (wikipedia.org)
For simplicity and due to a lack of research of this enzyme in other organisms, the information discussed in this article will be centered around human lysine carboxypeptidase, specifically. (wikipedia.org)
Activation1
It not just has the features of digestive enzymes, but also can restrict the decomposition of other forerunners of various Enzymes such as chymotrypsinogen, carboxypeptidase, as well as phospholipase, and work as an activation feature. (zhishangchemical.com)
Human2
Among the carboxypeptidases CPM is of particular importance because of its constitutive expression in an active form at the surface of specialized cells and tissues in the human body. (betalifesci.com)
The human peptide GHK (glycyl-l-histidyl-l-lysine) has multiple biological actions, all of which, according to our current knowledge, appear to be health positive. (proteinexplorer.org)