Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8305842 | Biochimie | 2014 | 7 Pages |
Abstract
Human matriptase-2 is an enzyme that belongs to the family of type II transmembrane serine proteases. So far there is a limited knowledge regarding its specificity and protein substrate(s). One of the identified natural substrates is hemojuvelin, a protein involved in the control of iron homeostasis. In this work, we describe the synthesis and evaluation of internal quenched substrates using a combinatorial approach. The iterative deconvolution of two libraries to define the specificity of matriptase-2 yielded to the identification of the substrate ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2 with a kcat/Km value of 4.5Â ÃÂ 105Â Mâ1Â ÃÂ sâ1, i.e. the highest specificity constant reported so far for matriptase-2.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
M. Wysocka, N. Gruba, A. Miecznikowska, J. Popow-Stellmaszyk, M. Gütschow, M. Stirnberg, N. Furtmann, J. Bajorath, A. Lesner, K. Rolka,