A Molecular Model of the Active Site of Dipeptidyl Peptidase IV

Explanation of the Substrate Specificity and Interaction with Inhibitors
  • Wolfgang Brandt
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 421)


The ectoenzyme dipeptidyl peptidase IV (DPP IV) is an integral plasma membrane glycoprotein abundantly expressed on a variety of cell surfaces.1 It is a serine peptidase of broad medical and biochemical significance. It plays a role in the degradations and post translational processing of bioactive peptides such as substance P, ß-casomorphins, growth hormone-releasing hormone and promelittin.2–9 DPP IV has been identified as CD26.10 Recently, it could be demonstrated that it is not only a surface differentiation marker involved in the transduction of mitogenic signals in thymocytes and T lymphocytes in human but also a cofactor in AIDS expression.10–13


Catalytic Triad Dipeptidyl Peptidase Surface Differentiation Marker Scissile Bond Calculated Interaction Energy 
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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Wolfgang Brandt
    • 1
  1. 1.Fachbereich Biochemie/BiotechnologieMartin-Luther-Universität Halle-WittenbergHalleGermany

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