-
peptide bonds from end-pieces of
terminal amino acids. For this reason,
endopeptidases cannot break down
peptides into monomers,
while exopeptidases can break...
-
Aspartic endopeptidases EC 3.4.23. of vertebrate,
fungal and
retroviral origin have been characterised. More recently,
aspartic endopeptidases ****ociated...
-
Serine proteases (or
serine endopeptidases) are
enzymes that
cleave peptide bonds in proteins.
Serine serves as the
nucleophilic amino acid at the (enzyme's)...
- An
endopeptidase inhibitor is a drug that
inhibits one or more
endopeptidase enzymes.
Endopeptidases are one of two
types of
proteases (enzymes that break...
-
Cysteine (/ˈsɪstɪiːn/;
symbol Cys or C) is a
semiessential proteinogenic amino acid with the
formula HOOC−CH(−NH2)−CH2−SH. The
thiol side
chain in cysteine...
- are
metalloproteinases that are calcium-dependent zinc-containing
endopeptidases;
other family members are adamalysins, serralysins, and astacins. The...
-
necessary for
proper folding but not for
hormonal activity.
Specific endopeptidases cleave the
prohormone before secretion,
producing the mature, biologically...
- ISBN 9780123822192. Birktoft, Jens J.; Breddam,
Klaus (1994). "[8]
Glutamyl endopeptidases".
Proteolytic Enzymes:
Serine and
Cysteine Peptidases.
Methods in Enzymology...
- modifications.
Endopeptidases are
enzymes that add
water to an
internal peptide bond in a
peptide chain and
break that bond.
Three common endopeptidases that come...
- GPR
endopeptidase (EC 3.4.24.78,
germination proteinase) is an enzyme. This
enzyme catalyses the
following chemical reaction:
Endopeptidase action with...
