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Endopeptidase or
endoproteinase are
proteolytic peptidases that
break peptide bonds of
nonterminal amino acids (i.e.
within the molecule), in contrast...
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Serine proteases (or
serine endopeptidases) are
enzymes that
cleave peptide bonds in proteins.
Serine serves as the
nucleophilic amino acid at the (enzyme's)...
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catalyzes the
addition of a
farnesyl moiety to the cysteine. Second, an
endoprotease that
recognizes the
farnesylated protein catalyzes the
peptide bond's...
- endopeptidase, Kex2
endoprotease, Kex2 endoproteinase, Kex2 protease,
proteinase Kex2p, Kex2-like
precursor protein processing endoprotease, prohormone-processing...
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acidic pH or at a
slightly basic pH (4.5 and 8.0, respectively)
using the
endoprotease, Glu-C. The
rates of
deamidation depend on
multiple factors, including...
- 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...
-
exopeptidase cleavage may
solve the
unspecific cleavage observed when
using endoprotease-based tag removal. Polyhistidine-tags are
often used for
affinity purification...
- 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...
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active products. This
encoded protein is a calcium-dependent
serine endoprotease that can
efficiently cleave precursor proteins at
their paired basic...
- 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...
