Exopeptidase

exopeptidases
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide chain.wikipedia
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Endopeptidase

endopeptidasesendoproteaseendopeptidase clp
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids.

Protease

proteasespeptidaseproteinase
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide chain.
Some detach the terminal amino acids from the protein chain (exopeptidases, such as aminopeptidases, carboxypeptidase A); others attack internal peptide bonds of a protein (endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase).

Catalysis

catalyzescatalysescatalyst
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide chain.

Peptide bond

peptide bondsamide bondprotein backbone
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide chain.

Amino acid

amino acidsresiduesresidue
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide chain.

Dipeptide

dipeptidesdipeptide bondglorin
An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide chain.

Aminopeptidase

aminopeptidasesaminopeptidase P.
Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.

Brush border

brush-border membranebrush-borderstriated border
Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.

Small intestine

small bowelsmall intestinessmall
Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.

Carboxypeptidase

Carboxypeptidasescarboxypeptidase bcarboxypeptidase h
Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.

Digestive enzyme

digestive enzymespancreatic enzymepancreatic enzymes
Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.

Pancreatic juice

digestive juicespancreatic fluidspancreatic juices
Thus, an aminopeptidase, an enzyme in the brush border of the small intestine, will cleave a single amino acid from the amino terminal, whereas carboxypeptidase, which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.

Carboxypeptidase A

carboxypeptidaseAcarboxypeptidases a
Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains.

Endopeptidase inhibitor

Endopeptidases are one of two types of proteases (enzymes that break down proteins and peptides), the other being exopeptidases.

Angiotensin-converting enzyme 2

ACE2angiontensin-converting enzyme 2angiotensin converting enzyme 2
Angiotensin converting enzyme 2 (ACE 2) is an exopeptidase that catalyses the conversion of angiotensin I to the nonapeptide angiotensin[1-9], or the conversion of angiotensin II to angiotensin 1-7.

Exopeptidase inhibitor

An exopeptidase inhibitor is a drug that inhibits one or more exopeptidase enzymes.

Metalloexopeptidase

metallocarboxypeptidasemetallo-carboxypeptidase
A metalloexopeptidase is a type of enzyme that acts as a metalloproteinase exopeptidase.

Polyhistidine-tag

His-tagHis tag6x His-Tag
This extra sequence is not necessary if exopeptidases are used to remove N-terminal His-tags (e.g., Qiagen TAGZyme).

Ham

dry-cured hamsmoked hamdry-cured
The enzymes involved are proteinases (cathepsins – B, D, H & L, and calpains) and exopeptidases (peptidase and aminopeptidase).

Dipeptidyl peptidase-4

DPP4CD26DPP-4
DPP-4 is a serine exopeptidase that cleaves X-proline or X-alanine dipeptides from the N-terminus of polypeptides.

PA clan of proteases

PA clanPAPA superfamily
The majority are endopeptidases, with the exception being the S46 family of exopeptidases.