Dipeptidyl-aminopeptidase

Dipeptidyl aminopeptidase (from rat brain) [9031-94-1] [EC 3.4.11.10]. Purified about 2000-fold by column chromatography on CM-cellulose, hydroxylapatite and Gly-Pro AH-Sepharose. [Imai et al. J Biochem (Tokyo)93 431 1983.]... 

Dipeptidyl aminopeptidase IV hydrolyzes substrates with free a-amino groups. Peptide bonds involving the carboxy group of either Pro or Ala are cleaved by this enzyme to X-Pro or X-Ala, where X may be any amino acid. It has been shown that peptides with the X-Pro moiety are hydrolyzed more completely than those with X-Ala [79],... 

Augustyns, K., der Veken, P.V., Senten, K. and Haemers, A. (2005) The therapeutic potential of inhibitors of dipeptidyl peptidase IV (DPP-IV) and related proline-specific dipeptidyl aminopeptidases. Current Medicinal Chemistry, 12, 971-998 (c) Augustyns, K., der Veken, P.V. and Haemers, A. 

This enzyme [EC 3.4.14.5] (also referred to as dipeptidyl aminopeptidase IV, Xaa-Pro-dipeptidylaminopepti-... 

Several enzymes catalyze stepwise removal of amino acids from one or the other end of a peptide chain. Carboxypeptidases232 remove amino acids from the carboxyl-terminal end, while aminopeptidases attack the opposite end. Using chromatographic methods, the amino acids released by these enzymes may be examined at various times and some idea of the sequence of amino acids at the chain ends may be obtained. A dipeptidyl aminopeptidase from bovine spleen cuts dipeptides one at a time from the amino terminus of a chain. These can be converted to volatile trimethylsilyl derivatives and identified by mass spectrometry.233 If the chain is shortened by one residue using the Edman degradation (Section 3) and the dipeptidyl aminopeptidase is again used, a different set of dipeptides that overlaps the first will be obtained and a sequence can be deduced. Carboxypeptidase Y can be used with MALDI mass spectrometry to deduce the C-terminal amino acid sequence for a peptide. However, He and Leu cannot be distinquished. 

Cysteine proteases are so called because of a critical cysteine involved (together with an adjacent histidine) in the catalytic mechanism. Cysteine proteases include papain-related proteases, calpain-related proteases and the caspases. Papain-like cysteine proteases include the plant enzymes actinidin, aleurain, bromelain, caricain, chymopapain, ficin and papain and the lysosomal cathepsins B, C, H, K, L and S. Cathepsin C is multimeric (MW -200,000), but the other papain-related proteases are monomeric with MWs of about 20,000-35,000. While cathepsin C is a dipeptidyl aminopeptidase, the other enzymes are endopeptidases. Cathepsin B is an endopeptidase and a dipeptidyl carboxypeptidase. Cathepsin H is an endopeptidase and an aminopeptidase. In higher animals, cathepsin B generates peptides from antigens for presentation to T cells by the major histocompatibility... 

Julius, D., Blair, L., Brake, A., Sprague, G., and Thorner, J. (1983). Yeast alpha factor is processed from a larger precursor polypeptide the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell 32 839-852. 

Dipeptidylpeptidase IV (EC 3.4.11.5 postproline dipeptidyl aminopeptidase CD26) is a serine protease located in the plasma membrane. Notable neuropeptide substrates include substance P. neuropeptide Y, peptide YY and enterostatin. Inhibitors include diprotin A (lle-Pro-lle) and diprotin B (Val-Pro-Leu)... 

Another type of enzyme, termed a dipeptidyl aminopeptidase, releases dipeptides rather than amino acids from the /V-terminus. Cathepsin C is one such enzyme and it will remove dipeptides consecutively from the /V-terminus of a peptide until either Lys or Arg becomes the /V-terminal amino acid or until Pro is in position 2 or 3 in the chain. Thus two dipeptides, Asp—Arg and Val—Tyr are cleaved from angiotensin II ... 

A limited amount of information can be obtained by the use of proteolytic enzymes that detach either amino acids or dipeptides sequentially from the C-terminus. They are thus complementary to the aminopeptidases and dipeptidyl aminopeptidases. Two pancreatic enzymes, carboxypeptidases A and B, differ in specificity. The former preferentially liberates C-terminal amino acids with aromatic side chains, somewhat less readily amino acids with alkyl side chains and, more slowly still, other amino acids, but not Pro, Arg, Lys and His. In contrast, carboxypeptidase B releases only C-terminal Arg, Lys and His. Carboxypeptidase Y is much less specific and is capable of removing all amino acids, although Gly and Pro are liberated only slowly. As with aminopeptidases, it is advisable to analyse the hydrolysate at intervals in order to determine the C-terminal sequence of amino acids. An interesting recent development (Carles et al., 1988) uses carboxypeptidase to effect transpeptidation between the protein being sequenced and a tritiated amino acid. The labelled protein is then degraded by various specific methods and then the labelled fragments are isolated by gel electrophoresis and subjected to Edman degradation. 

Dipeptidyl carboxypeptidases remove the C-terminal dipeptide intact and therefore are analogous to the dipeptidyl aminopeptidases such as cathepsin C. One such enzyme, angiotensin-converting enzyme, is important biologically for converting angiotensin I into the hypertensive angiotensin II (see Section 9.3). This enzyme does not hydrolyse bonds of the type X—Pro but will hydrolyse Pro—X bonds. The use of dipeptidyl carboxypeptidases for sequence determination would probably increase if pure enzymes were readily available commercially. 

Dipeptidyl aminopeptidase (dipeptidyl peptidase IV, from rat brain) ]9031-94-l, 54249-88-6] Mr 87,500 (monomer SDS-PAGE), (88,107 from nucleotide sequence), up to 4000,000... 

Klemba, M., Gluzman, I. Y., and Goldberg, D. E. (2004). A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. ]. Biol. Chem. 279, 43000-43007. 

Cathepsin C. Cathepsin J. Dipeptidyl aminopeptidase I. Dipeptidyl transferase. 

Atlan, D., Laloi, P., and Portalier, R. (1990). X-Proline-dipeptidyl aminopeptidase of Lactobacillus delbrueckii subsp. bulgaricus Characterization of the enzyme and isolation of deficient mutants. Appl Environ. Microbiol 56, 2174-2179. 

Bockelmann, W., Fobker, M., and Teuber, M. (1991). Purification and characterization of the X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus and Lactobacillus acidophilus. Ini Dairy J. 1, 51-66... 

Booth, M., Ni Fhaolain, I., Jennings, P. V., and O Cuinn, G. (1990a). Purification and characterization of a post-proline dipeptidyl aminopeptidase from Streptococcus cremoris AM2. J. Dairy Res. 57,89-99. 

Khalid, N. M., and Marth, E. H. (1990d). Purification and partial characterization of a prolyl-dipeptidyl aminopeptidase from Lactobacillus helveticus CNRZ 32. Appl. Environ. Microbiol. 56, 381-388. 

Kiefer-Partch, B., Bockelman, W., Geis, A., and Teuber, M. (1989). Purification of a X-propyl-dipeptidyl aminopeptidase from the cell wall proteolytic system of Lactococcus lactis subsp. cremoris. Appl. Microbiol. Biotechnol. 31, 75-78. 

Meyer, J., and Jordi, R. (1987). Purification and characterization of X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus lactis and from Streptococcus thermophilus. J. Dairy Sci. 70, 738-745. 

Miyakawa, H., Hashimoto, I., Nakamura, T., Ishibashi, N., Shimamura, S., and Igoshi, K. (1994). Purification and characterization of an X-prolyl dipeptidyl aminopeptidase from Lactobacillus helveticus LHE-511. Milchwissenschaft 49, 670-673. 

TAGZyme kit/E. coli MK(HQ)6QJ,-Protein and various, other His tags optimized for this kit Dipeptidyl aminopeptidase 1 (DPP 1) alone or a combination of DPP 1, glutamine cyclotransferase (GCT) and pyroglutamyl aminopeptidase (PGAP) UNYZYME Laboratories, Horsholm... 

Acetoxymercuri)aniline (36) Affinity chromatography of dipeptidyl aminopeptidase I 333 ... 

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