- An
exopeptidase is any
peptidase that
catalyzes the
cleavage of the
terminal (or the penultimate)
peptide bond; the
process releases a
single amino acid...
- peptides.
Exopeptidases are
enzymes that can
cleave the end of an
amino acid side
chain mostly through the
addition of water.
Exopeptidase enzymes exist...
-
nonterminal amino acids (i.e.
within the molecule), in
contrast to
exopeptidases,
which break peptide bonds from end-pieces of
terminal amino acids....
-
Carboxypeptidase A
usually refers to the
pancreatic exopeptidase that
hydrolyzes peptide bonds of C-terminal
residues with
aromatic or
aliphatic side-chains...
-
sequence is not
necessary if
exopeptidases are used to
remove N-terminal His-tags (e.g.,
Qiagen TAGZyme). Furthermore,
exopeptidase cleavage may
solve the unspecific...
-
their tendency to
cleave peptide bonds at the
terminus of a
protein (
exopeptidases) vs
peptide bonds at the
interior of the
protein (endopeptidases). Pepsin...
- An
exopeptidase inhibitor is a drug that
inhibits one or more
exopeptidase enzymes.
Exopeptidases are one of two
types of
proteases (enzymes that break...
- system, the
other two
being chymotrypsin and trypsin.
There are also
exopeptidases which remove individual amino acids at both ends of
proteins (carboxypeptidases...
-
involved are
proteinases (cathepsins – B, D, H & L, and calpains) and
exopeptidases (peptidase and aminopeptidase).
These enzymes cause proteolysis of muscle...
-
endopeptidase genes and 69
exopeptidase genes, and A.
sojae strain SMF134 has 83
endopeptidase genes and 67
exopeptidase genes. Similarly, starch-degrading...
