-
amino acid from the
carboxylic end of the peptide. Some
examples of
exopeptidases include:
Carboxypeptidase A -
cleaves C-terminal Phe, Tyr, Trp, or Leu...
-
nonterminal amino acids (i.e.
within the molecule), in
contrast to
exopeptidases,
which break peptide bonds from end-pieces of
terminal amino acids....
- An
exopeptidase inhibitor is a drug that
inhibits one or more
exopeptidase enzymes.
Exopeptidases are one of two
types of
proteases (enzymes that break...
- peptides.
Exopeptidases are
enzymes that can
cleave the end of an
amino acid side
chain mostly through the
addition of water.
Exopeptidase enzymes exist...
-
involved are
proteinases (cathepsins – B, D, H & L, and calpains) and
exopeptidases (peptidase and aminopeptidase).
These enzymes cause proteolysis of muscle...
-
hydrolysis of
interior peptide bonds in
peptide chains, as
opposed to
exopeptidases (another
class of enzymes, that
catalyze the
hydrolysis of terminal...
-
performing cytosolic digestion of
absorbed dipeptides.
Dipeptidases are
exopeptidases,
classified under EC
number 3.4.13.
Membrane dipeptidase Dipeptidases...
- cycle. The
species secretes more than 20
different proteases,
including exopeptidases and endopeptidases.
These proteases allow T.
rubrum to
digest human...
-
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...
- food
proteins into
polypeptides that are then
broken down by
various exopeptidases and
dipeptidases into
amino acids. The
digestive enzymes however are...
