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Cellular and Molecular Life Sciences, 2006
This review describes the structure and function of prolyl endopeptidase (PEP) enzymes and how they are being evaluated as drug targets and therapeutic agents. The most well studied PEP family has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain to hydrolyze the peptide bond on the carboxyl side of ...
J, Gass, C, Khosla
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This review describes the structure and function of prolyl endopeptidase (PEP) enzymes and how they are being evaluated as drug targets and therapeutic agents. The most well studied PEP family has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain to hydrolyze the peptide bond on the carboxyl side of ...
J, Gass, C, Khosla
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2013
In the course of solubilization and purification of fusicoccin binding sites present in microsomal fractions of spinach (Spinaciaoleracea L.)leaves,some endogenous hydrolases responsible for the poor stability of the receptors were identified [1]. Among them there was a serine proteinase displaying leucine-specific proteolytic activity.To reflect its ...
ADUCCI, PATRIZIA, Ascenzi, P.
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In the course of solubilization and purification of fusicoccin binding sites present in microsomal fractions of spinach (Spinaciaoleracea L.)leaves,some endogenous hydrolases responsible for the poor stability of the receptors were identified [1]. Among them there was a serine proteinase displaying leucine-specific proteolytic activity.To reflect its ...
ADUCCI, PATRIZIA, Ascenzi, P.
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Prolyl endopeptidase inhibitors
Il Farmaco, 2000Selective prolyl endopeptidase inhibitors were elaborated by modification of the structure of SUAM-1221, by using a CoMFA study and protein crystallography. The most active representatives of omega-(N-hetaryl)alkanoylprolylpyrrolidines, containing 2- or 3-methylene chain links have high activity (IC50 10(-9)-10(-11)) and exhibit significant in vivo ...
I, Hermecz, K, Kánai
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Proline-Specific Endopeptidases
Russian Journal of Bioorganic Chemistry, 2003Prolyl endopeptidases, or post-proline-cleaving enzymes, are the specific endopeptidases that hydrolyze peptide substrates at the carbonyl of the internal Pro residue. All the currently known prolyl endopeptidases from animals, microorganisms, fungi, and plants as well as the post-proline-cleaving enzymes that do not exhibit the strict specificity to ...
D V, Besedin, G N, Rudenskaia
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Molecular and Cellular Biochemistry, 1983
This review summarizes our knowledge of pituitary endopeptidases. Emphasis has been placed on well-characterized enzymes and their potential roles in proteolytic processes of the pituitary. Because of space limitations, degradation of biologically active peptide by crude preparations has generally not been discussed.
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This review summarizes our knowledge of pituitary endopeptidases. Emphasis has been placed on well-characterized enzymes and their potential roles in proteolytic processes of the pituitary. Because of space limitations, degradation of biologically active peptide by crude preparations has generally not been discussed.
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Life Sciences, 1983
Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin ...
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Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin ...
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Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15
Peptides, 1995Lysylbradykinin (LBK), a potent bioactive peptide with pleiotropic actions, is the major kinin generated in the extravascular space. To explore possible mechanisms of inactivation of this peptide in tissues, we evaluated its degradation by endopeptidase 24.11 (EP 24.11) and endopeptidase 24.15 (EP 24.15), two zinc metalloenzymes widely distributed in ...
C, Rosenbaum, C, Cardozo, M, Lesser
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