Dipeptidyl-peptidase I

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Dipeptidyl peptidase I
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Cathepsin C, heterododekamer, Human
Identifiers
EC no. 3.4.14.1
CAS no. 9032-68-2
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Dipeptidyl peptidase I (EC 3.4.14.1, cathepsin C , dipeptidyl aminopeptidase I, dipeptidyl transferase, dipeptide arylamidase I, DAP I) is an enzyme. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

Release of an N-terminal dipeptide, Xaa-Yaa!Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro

This Cl-dependent, lysosomal cysteine-type peptidase is maximally active at acidic pH.

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<span class="mw-page-title-main">Dipeptidyl peptidase-4</span> Mammalian protein found in Homo sapiens

Dipeptidyl peptidase-4 (DPP4), also known as adenosine deaminase complexing protein 2 or CD26 is a protein that, in humans, is encoded by the DPP4 gene. DPP4 is related to FAP, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner, and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV].

<span class="mw-page-title-main">PEPD</span> Protein-coding gene in the species Homo sapiens

Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the PEPD gene.

<span class="mw-page-title-main">DPP3</span> Protein-coding gene in the species Homo sapiens

Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene.

<span class="mw-page-title-main">DPP7</span> Protein-coding gene in the species Homo sapiens

Dipeptidyl-peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene.

<span class="mw-page-title-main">DPP8</span> Protein-coding gene in the species Homo sapiens

Dipeptidyl peptidase 8 is an enzyme that in humans is encoded by the DPP8 gene.

<span class="mw-page-title-main">DPP9</span> Protein-coding gene in the species Homo sapiens

Dipeptidyl peptidase 9 is an enzyme that in humans is encoded by the DPP9 gene.

Cathepsin X is an enzyme. This enzyme catalyses the following chemical reaction

Dipeptidyl-peptidase III is an enzyme. This enzyme catalyses the following chemical reaction

Xaa-Pro aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Bacterial leucyl aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Xaa-Trp aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">X-Pro dipeptidase</span>

Xaa-Pro dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Dipeptidyl-peptidase II is an enzyme. This enzyme catalyses the following chemical reaction:

Xaa-Pro dipeptidyl-peptidase (EC 3.4.14.11, X-prolyl dipeptidyl aminopeptidase, PepX, X-prolyl dipeptidyl peptidase is an enzyme. It catalyses the following chemical reaction

Xaa-Xaa-Pro tripeptidyl-peptidase is an enzyme. It catalyses the following chemical reaction

Pyroglutamyl-peptidase II is an enzyme. This enzyme catalyses the following chemical reaction

C-terminal processing peptidase is an enzyme. This enzyme catalyses the following chemical reaction

Signal peptidase II is an enzyme.

References

  1. ↑ Planta RJ, Gorter J, Gruber M (September 1964). "The catalytic properties of cathepsin C". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 89 (3): 511–9. doi:10.1016/0926-6569(64)90077-x. PMID   14209333.
  2. ↑ Metroione RM, Neves AG, Fruton JS (May 1966). "Purification and properties of dipeptidyl transferase (Cathepsin C)". Biochemistry. 5 (5): 1597–604. doi:10.1021/bi00869a021. PMID   5961281.
  3. ↑ McDonald JK, Zeitman BB, Reilly TJ, Ellis S (May 1969). "New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones". The Journal of Biological Chemistry. 244 (10): 2693–709. doi: 10.1016/S0021-9258(18)83453-6 . PMID   4306035.
  4. ↑ McDonald, J.K.; Schwabe, C. (1977). "Intracellular exopeptidases". In Barrett, A.J. (ed.). Proteinases in Mammalian Cells and Tissues. Amsterdam: North-Holland Publishing Co. pp. 311–391.


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