The C-terminal sequence encodes function in serine proteases

Citation
Mm. Krem et al., The C-terminal sequence encodes function in serine proteases, J BIOL CHEM, 274(40), 1999, pp. 28063-28066
Citations number
41
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
0021-9258 → ACNP
Volume
274
Issue
40
Year of publication
1999
Pages
28063 - 28066
Database
ISI
SICI code
0021-9258(19991001)274:40<28063:TCSEFI>2.0.ZU;2-K
Abstract
Serine proteases of the chymotrypsin family have maintained a common fold o ver an evolutionary span of more than one billion years. Notwithstanding mo dest changes in sequence, this class of enzymes has developed a wide variet y of substrate specificities and important biological functions. Remarkably , the C-terminal portion of the sequence in the protease domain accounts fu lly for this functional diversity. This portion is often encoded by a singl e exon and contains most of the residues forming the contact surface in the active site for the P1-P3 residues of the substrate, as well as domains re sponsible for the modulation of catalytic activity. The evolution of serine proteases was therefore driven by optimization of contacts made with the u nprimed subsites of the substrate and targeted a relatively short portion o f the sequence toward the C-terminal end. The dominant role of the C-termin al sequence should facilitate the identification of function in newly disco vered genes belonging to this class of enzymes.