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The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). [1] Members of the H family have longer C-termini than those of family A, [2] and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble.
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 ...
Zinc fingers help read DNA sequences.. Zinc is an essential trace element for humans [1] [2] [3] and other animals, [4] for plants [5] and for microorganisms. [6] Zinc is required for the function of over 300 enzymes and 1000 transcription factors, [3] and is stored and transferred in metallothioneins.
Zinc carboxypeptidase This page was last edited on 13 March 2019, at 11:15 (UTC). Text is available under the Creative Commons Attribution-ShareAlike 4.0 License ...
This second enzyme is a metallocarboxypeptidase (i.e. uses a zinc ion in the active site instead of a serine residue) and is broadly expressed in mammalian tissues. [5] Like the serine carboxypeptidase, the metallocarboxypeptidase D also removes C-terminal arginine or lysine residues from peptides, with an optimal pH range of 5 to 7 ...
Zinc-rich foods include beef, poultry, pumpkin seeds, fortified breakfast cereals, and seafood (in fact, oysters contain more zinc than any other food). Because zinc is found in so many foods ...
This gene is a member of the carboxypeptidase A/B subfamily, and it is located in a cluster with three other family members on chromosome 7. Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage.
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