Identification of the active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis
The active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis (PepX) was identified. The enzyme was labeled by [ 3H]DFP, treated by CNBr and the resulting peptides were separated by reverse-phase-HPLC. The main radiolabeled peptide was sequenced. Ser-348, in the following...
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Published in | FEBS letters Vol. 314; no. 2; pp. 139 - 142 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
14.12.1992
Elsevier Wiley |
Subjects | |
Online Access | Get full text |
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Summary: | The active site serine of the X-prolyl dipeptidyl aminopeptidase from
Lactococcus lactis (PepX) was identified. The enzyme was labeled by [
3H]DFP, treated by CNBr and the resulting peptides were separated by reverse-phase-HPLC. The main radiolabeled peptide was sequenced. Ser-348, in the following sequence, Gly-Lys-Ser-Tyr-Leu-Gly, was identified as the active site serine. A sequence comparison between the active site of PepX and other serine proteases was made, showing only limited sequence homologies in this area. The consensus sequence surrounding the active site serine in the three known X-prolyl dipeptidyl aminopeptidases (mammalian DPPIV, yeast DPAB and PepX) is G-X-S-Y-X-G, where X is a non-conserved amino acid. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(92)80960-O |