Results 11 to 20 of about 192,846 (155)
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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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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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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In vivo effects of bradykinin B2 receptor agonists with varying susceptibility to peptidases.
Frontiers in Pharmacology, 2016 We reported evidence of bradykinin (BK) regeneration from C-terminal extended BK sequences that behave as peptidase-activated B2 receptor (B2R) agonists.
Mélissa eJean +4 more
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Frontiers in Pharmacology, 2014 While bradykinin (BK) is known to be degraded by angiotensin converting enzyme (ACE), we have recently discovered that Met-Lys-BK-Ser-Ser is paradoxically activated by ACE.
Xavier eCharest-Morin +4 more
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Structure of the complex of carboxypeptidase B and N-sulfamoyl-
Acta Crystallographica Section F Structural Biology Communications, 2015 Porcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp 3-hybridized carbon in the scissile-bond surrogate. Crystals were grown in a form belonging to the same space group, P41212, as the uncomplexed enzyme.
Valery, Akparov +3 more
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The location of the arginine-specific carboxypeptidase in the membrane of Mycoplasma salivarium and its physiological functions [PDF]
FEMS Microbiology Letters, 1992 A non-penetrating probe, 2,4,6-trinitrobenzenesulfonate, inhibited the activity of the carboxypeptidase purified from the cell membranes of Mycoplasma salivarium and the same enzymatic activity of intact Mycoplasma cells as well. Growth of the organism in medium containing benzoylglycyl-L-arginine resulted in a higher pH and higher turbidity than ...
K, Shibata, T, Watanabe
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Changes in arginine carboxypeptidase (CPR) activity in stressed rats
Pathophysiology, 1994 Abstract An arginine carboxypeptidase (CPR) is generated from its precursor (ProCPR) by proteolytic enzyme and may function in vivo in the removal of C-terminal arginine from inflammatory peptides such as C3a and C5a. We studied changes in this enzyme activity in rats submitted to liver cirrhois, hepatectomy, splenectomy, burning or endotoxin ...
Katsumi Kato +5 more
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Protein Expression and Purification, 2010 Carboxypeptidases may serve as tools for removal for C-terminal affinity tags. In the present study, we describe the expression and purification of an A-type carboxypeptidase from the fungal pathogen Metarhizium anisopliae (MeCPA) that has been ...
B. P. Austin +4 more
semanticscholar +1 more source
Mutational replacement of methionine by arginine in the S′1 substrate binding site of yeast carboxypeptidase [PDF]
Carlsberg Research Communications, 1986 Alkylation of Met-398 in the S′1 binding site of carboxypeptidase Y drastically reduces kcat for hydrolysis of peptides, presumably due to introduction of a positively charged sulfonium ion. In the present work a positive charge has been introduced by means of site-directed mutagenesis, exchanging Met-398 with the cationic arginyl residue.
BECH, LM +4 more
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