-
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....
-
involved are
proteinases (cathepsins – B, D, H & L, and calpains) and
exopeptidases (peptidase and aminopeptidase).
These enzymes cause proteolysis of muscle...
- peptides.
Exopeptidases are
enzymes that can
cleave the end of an
amino acid side
chain mostly through the
addition of water.
Exopeptidase enzymes exist...
- An
exopeptidase inhibitor is a drug that
inhibits one or more
exopeptidase enzymes.
Exopeptidases are one of two
types of
proteases (enzymes that break...
-
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...
-
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...
- orthophenanthroline.
There are two
subgroups of metalloproteinases:
Exopeptidases,
metalloexopeptidases (EC number: 3.4.17). Endopeptidases, metalloendopeptidases...
- system, the
other two
being chymotrypsin and trypsin.
There are also
exopeptidases which remove individual amino acids at both ends of
proteins (carboxypeptidases...
