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Exopeptidases
(Exoproteases)


A sub-subclass of peptide hydrolases that act only near the ends of polypeptide chains. exopeptidases are further divided into aminopeptidases; EC 3.4.11; dipeptidases; EC 3.4.13; dipeptidyl peptidases & tripeptidyl peptidases, EC 3.4.14; peptidyl-dipeptidases, EC 3.4.15; carboxypeptidases; EC 3.4.16 - EC 3.4.18, and omega peptidases, EC 3.4.19. EC 3.4.-.

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substrates that enter the
substrates that enter the
www.cellinteractive.com

cleavage by <b>exopeptidases</b>
cleavage by exopeptidases
www.nature.com

<b>exopeptidases</b>
exopeptidases
faculty.pasadena.edu

<b>exopeptidases</b> and
exopeptidases and
www.liv.ac.uk

Fig. 2.
Fig. 2.
www.pnas.org

<b>exopeptidases</b> cleave exterior
exopeptidases cleave exterior
www.studyblue.com

Detecting protease enzymes
Detecting protease enzymes
camel.arizona.edu

OF ENDO-AND <b>EXOPEPTIDASES</b> Protein Quaternary Structure: HETERO TRIMERIC
OF ENDO-AND EXOPEPTIDASES Protein Quaternary Structure: HETERO TRIMERIC
swissmodel.expasy.org

Therapeutic use


Symptoms:

    

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Wikipedia


  • Exopeptidases: A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.
  • Glutamyl Aminopeptidase: A ZINC-dependent membrane-bound aminopeptidase that catalyzes the N-terminal peptide cleavage of GLUTAMATE (and to a lesser extent ASPARTATE). The enzyme appears to play a role in the catabolic pathway of the RENIN-ANGIOTENSIN SYSTEM.
  • Aminopeptidases: A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.
  • Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
  • Humans: Members of the species Homo sapiens.
  • Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
  • Kinetics: The rate dynamics in chemical or physical systems.
  • Animals: Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.
  • Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.


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  • MeSH - Medical Subject Headings.
  • DeCS - Health Sciences Descriptors.

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Last update: April 2009
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