|Protein Name||Dipeptidyl peptidase 1|
|Ref Sequence ID||NP_001028789.1|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Protein Function||cystein cathepsin; involved in a normal cellular protein degradation and turnover; aminodipeptidase|
|Biochemical Properties||Cysteine cathepsins are optimally active in a slightly acidic pH and are mostly unstable at neutral pH; exhibit broad specificity, cleave substrates preferentially after basic or hydrophobic residues; E-64 is a non-selective inhibitor of all the cysteine cathepsins, with the exception of cathepsin C, which is only weakly inhibited|
|Significance in milk||DPP4 is a key enzyme in intermediary metabolism by regulating important glycemic pathways; expression of DPP4 decreases with the onset of lactation|
|PTMs||Glycosylated: four glycans|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||No TM helices|
|Bibliography||1. Schulz, K. et al. (2015) ‘Effects of Inhibiting Dipeptidyl Peptidase-4 (DPP4) in Cows with Subclinical Ketosis.’, PloS one. Edited by M. Bader, 10(8), p. e0136078. doi: 10.1371/journal.pone.0136078. |
2. Turk, B., Turk, D. and Turk, V. (2000) ‘Lysosomal cysteine proteases: more than scavengers.’, Biochimica et biophysica acta, 1477(1–2), pp. 98–111. doi: 10.1016/s0167-4838(99)00263-0.
3. Turk, D. et al. (2001) ‘Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases’, The EMBO Journal, 20(23), pp. 6570–6582. doi: 10.1093/emboj/20.23.6570.