Targeting carboxypeptidase A/B activity with the phosphinic inhibitor C28 reduces the asthmatic response in a mouse model of house dust mite-induced asthma. [PDF]
Inflamm ResObjectiveMetallo-carboxypeptidases are implicated in several pathological contexts but their role in asthma and their potential as therapeutic targets in asthmatic settings are only partly understood.
Allam VSRR +10 more
europepmc +3 more sources
Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase. [PDF]
Microbiology (Reading)\ua9 2024 The Authors. The twin-arginine protein transport (Tat) system exports folded proteins across the cytoplasmic membranes of prokaryotes and the energy transducing-membranes of plant thylakoids and mitochondria.
Gallego-Parrilla JJ +3 more
europepmc +3 more sources
Prodrugs Activated by Vascular Ectopeptidases: Proof of Concept
Medical Sciences Forum, 2022 Several vascular ectopeptidases reside in blood vessels and efficiently regulate peptide hormones. For instance, bradykinin (BK) is inactivated by angiotensin converting enzyme (ACE) or arginine-carboxypeptidases (Arg-CPs), and aminopeptidase N (APN ...
François Marceau
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Guanidine derivatives restore activity to carboxypeptidase lacking arginine‐127 [PDF]
Protein Science, 1992 AbstractArg‐127 stabilizes the oxyanion of the tetrahedral intermediate formed during Zn2+ carboxypeptidase A‐catalyzed hydrolysis. Mutant carboxypeptidases lacking Arg‐127 exhibit substantially reduced rates of hydrolysis with the change manifest almost entirely in kcat (kcat/Km is decreased by 104 for R127A).
M A, Phillips, L, Hedstrom, W J, Rutter
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Measurement of Arginine Carboxypeptidase‐Generating Activity of Adult Plasma [PDF]
Microbiology and Immunology, 1998 AbstractArginine carboxypeptidase (CPR) is a novel carboxypeptidase which was first described by Campbell and Okada. CPR is generated from a stable precursor of CPR (proCPR) during coagulation or under other circumstances and is promptly inactivated at 37 C. Therefore, it is not easy to determine CPR in blood samples. Since proCPR can be separated from
M, Watanabe +3 more
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Arginine 127 stabilizes the transition state in carboxypeptidase
Journal of Biological Chemistry, 1990 Crystallographic studies suggest that Arg-127 is a key amino acid in the hydrolysis of peptides and esters by carboxypeptidase A. The guanidinium group of Arg-127 is hypothesized to stabilize the oxyanion of the tetrahedral intermediate formed by the attack of water on the scissile carbonyl bond. We have replaced this amino acid in rat carboxypeptidase
M A, Phillips +2 more
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Purification and characterization of an arginine-specific carboxypeptidase from Mycoplasma salivarium [PDF]
Journal of Bacteriology, 1988 The carboxypeptidase which had been shown to be present exclusively in nonfermentative mycoplasmas was found to be associated with cell membranes of Mycoplasma salivarium. The enzyme was released from the membranes with Triton X-100 and purified by ion-exchange chromatography on DEAE-Sephacel, affinity chromatography on arginine-Sepharose 4B, and ...
K, Shibata, T, Watanabe
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Purification and Characterization of Arginine Carboxypeptidase Produced by Porphyromonas gingivalis [PDF]
Infection and Immunity, 2002 ABSTRACT Arginine carboxypeptidase was isolated from the cytoplasm of Porphyromonas gingivalis 381 and purified by DEAE-Sephacel column chromatography, followed by high-performance liquid chromatography on DEAE-5PW and TSK G2000SW XL .
Kaname, Masuda +3 more
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Arginine and lysine as products of basic carboxypeptidase activity associated with fibrinolysis [PDF]
Biomeditsinskaya Khimiya, 2012 Blood carboxypeptidases play an important role in the regulation of fibrinolysis. We have proposed here the method for the assay of blood carboxypeptidase activity associated with coagulation/fibrinolysis using the natural substrate fibrin and the detection of basic amino acids arginine and lysine as products in the conditions close to those in vivo ...
A A, Zhloba +4 more
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C-Terminal Arginine-Selective Cleavage of Peptides as a Method for Mimicking Carboxypeptidase B
Organic Letters, 2023 C-Terminal residues play a pivotal role in dictating the structure and functions of proteins. Herein, we report a mild, efficient, chemoselective, and site-selective chemical method that allows for precise chemical proteolysis at C-terminal arginine dictated by 9,10-phenanthrenequinone independent of the remaining sequence.
Lyndsey C. Prosser +3 more
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