All known carboxypeptidases are either metallo carboxypeptidases or serine
carboxypeptidases (EC 3.4.16.5 and EC 3.4.16.6). The catalytic activity of
the serine carboxypeptidases, like that of the trypsin family serine
proteases, is provided by a charge relay system involving an aspartic acid
residue hydrogen-bonded to a histidine, which is itself hydrogen-bonded to a
serine [1]. Proteins known to be serine carboxypeptidases are:
Barley and wheat serine carboxypeptidases I, II, and III [2].
Yeast carboxypeptidase Y (YSCY) (gene PRC1), a vacuolar protease involved
in degrading small peptides.
Yeast KEX1 protease, involved in killer toxin and α-factor precursor
processing.
Fission yeast sxa2, a probable carboxypeptidase involved in degrading or
processing mating pheromones [3].
Vertebrate protective protein / cathepsin A [5], a lysosomal protein which
is not only a carboxypeptidase but also essential for the activity of both
β-galactosidase and neuraminidase.
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