التفاصيل البيبلوغرافية
| العنوان: |
Functional characterization of Narc 1, a novel proteinase related to proteinase K |
| المؤلفون: |
Naureckiene, Saule1, Ma, Linh1, Sreekumar, Kodangattil2, Purandare, Urmila1, Frederick Lo, C.1, Huang, Ying3, Chiang, Lillian W.4, Grenier, Jill M.4, Ozenberger, Bradley A.1, Steven Jacobsen, J.1, Kennedy, Jeffrey D.1, DiStefano, Peter S.4, Wood, Andrew1, Bingham, Brendan1 binghab@wyeth.com |
| المصدر: |
Archives of Biochemistry & Biophysics. Dec2003, Vol. 420 Issue 1, p55. 13p. |
| مصطلحات موضوعية: |
*PROTEINASES, *GENETIC code, *SUBTILISINS, *PROTEOLYTIC enzymes |
| مستخلص: |
The NARC 1 gene encodes a novel proteinase K family proteinase. The domain structure of rat Narc 1 resembles that of the subtilisin-like proprotein convertases (SPCs), except that rNarc 1 lacks the canonical P-domain of SPCs, retaining only the RGD motif as part of what might be a cryptically functioning P-domain. Narc 1 undergoes autocatalytic intramolecular processing at the site LVFAQ↓, resulting in the cleavage of its prosegment and the generation of an active proteinase with a broad alkaline pH optimum and no apparent calcium requirement for activity. Both primary and secondary structural determinants influence Narc 1 substrate recognition. Our functional characterization of Narc 1 reinforces the inference drawn from the analysis of its predicted structure that this enzyme is most closely related to representatives of the proteinase K family, but that it is also sufficiently different to warrant its possible classification in a separate sub-family. [Copyright &y& Elsevier] |
| قاعدة البيانات: |
Academic Search Index |
