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A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases , which cleave peptide bonds at the N-terminus of proteins.
Carboxypeptidase A (CPA) contains a zinc (Zn 2+) metal center in a tetrahedral geometry with amino acid residues in close proximity around zinc to facilitate catalysis and binding. Out of the 307 amino acids bonded in a peptide chain, the following amino acid residues are important for catalysis and binding; Glu-270, Arg-71, Arg-127, Asn-144 ...
Carboxylesterases are widely distributed in nature, and are common in mammalian liver. Many participate in phase I metabolism of xenobiotics such as toxins or drugs; the resulting carboxylates are then conjugated by other enzymes to increase solubility and eventually excreted.
Carboxypeptidase B2 (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable fibrinolysis inhibitor (TAFI), is an enzyme that, in humans, is encoded by the gene CPB2.
The third number (the sub-subclass) gives more information about the catalytic mechanism of the reaction. Lysine carboxypeptidase is in sub-subclass 17: metallocarboxypeptidases. 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 ...
Overstimulation and -activation of glutamate receptors as well as “disturbances in the cellular mechanisms that protect against the adverse consequences of physiological glutamate receptor activation” [40] have been known to cause neuron damage and death, which have been associated with multiple neurological diseases.
CPA3 has a pH optimum in the neutral to basic range. CPA3 functions together with endopeptidases secreted from mast cells such as chymases and tryptases to degrade proteins and peptides, including the apolipoprotein B component of LDL particles and angiotensin I. [9] [10] Upon mast cell activation and degranulation, CPA3, the chymases, and tryptases are released in complexes with heparin ...
Carboxypeptidase B (EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L-arginine]hydrolase) is a carboxypeptidase that preferentially cleaves off basic amino acids arginine and lysine from the C-terminus of a peptide.