-
Endopeptidase or
endoproteinase are
proteolytic peptidases that
break peptide bonds of
nonterminal amino acids (i.e.
within the molecule), in contrast...
-
Serine proteases (or
serine endopeptidases) are
enzymes that
cleave peptide bonds in proteins.
Serine serves as the
nucleophilic amino acid at the (enzyme's)...
- the aid of two
endoproteases. Type I
endoproteases, PC1 and PC3,
disrupt the C peptide-B
chain connection. PC2, a type II
endoprotease,
cleaves the C...
- yeast,
insulin may be
engineered as a single-chain
protein with a
KexII endoprotease (a
yeast homolog of PCI/PCII) site that
separates the
insulin A chain...
-
After budding,
insulin secretory granules are acidified,
activating endoproteases PC1/3 and PC2 to
convert proinsulin into insulin. The
clatherin coating...
-
catalyzes the
addition of a
farnesyl moiety to the cysteine. Second, an
endoprotease that
recognizes the
farnesylated protein catalyzes the
peptide bond's...
- (2001). "Maturation of HIV
envelope glycoprotein precursors by
cellular endoproteases". Biochim. Biophys. Acta. 1469 (3): 121–32. doi:10.1016/S0304-4157(00)00014-9...
- then
cleaved from the C-terminus by a
specific prenyl-protein
specific endoprotease and the new C-terminus is
methylated by a methyltransferase. KRas processing...
-
active products. This
encoded protein is a calcium-dependent
serine endoprotease that can
efficiently cleave precursor proteins at
their paired basic...
-
generated from the
precursor at a ****tive
cleavage site for a furin-like
endoprotease. In
contrast to
smaller LEAP-2 variants, this
peptide exhibits dose-dependent...
