Functional characterization of Narc 1, a novel proteinase related to proteinase K.
Arch Biochem Biophys
; 420(1): 55-67, 2003 Dec 01.
Article
en En
| MEDLINE
| ID: mdl-14622975
ABSTRACT
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.
Buscar en Google
Banco de datos:
MEDLINE
Asunto principal:
Serina Endopeptidasas
/
Alineación de Secuencia
/
Endopeptidasa K
/
Análisis de Secuencia de Proteína
/
Modelos Químicos
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Año:
2003
Tipo del documento:
Article