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Sequence identity between a lysine‐containing peptide from Leuconostoc mesenteroides glucose‐6‐phosphate dehydrogenase and an active site peptide from human erythrocyte glucose‐6‐phosphate dehydrogenase
Author(s) -
Bhadbhade Mohan M.,
Adams Margaret J.,
Flynno T.Geoffrey,
Richard Levy H.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81445-x
Subject(s) - leuconostoc mesenteroides , biochemistry , glucose 6 phosphate dehydrogenase , dehydrogenase , enzyme , peptide , peptide sequence , lysine , biology , active site , leuconostoc , amino acid , chemistry , bacteria , lactic acid , genetics , gene , fermentation , lactobacillus
Peptides recently isolated and sequenced from a bacterial ( Leuconostoc mesenteroides ) glucose‐6‐phosphate dehydrogenase are remarkably homologous to an active site region of the human erythrocyte enzyme, although the enzymes differ in their overall amino acid composition and kinetic properties. The computer program ALIGN, used to determine the bestalignment between the two enzyme sequences, gives matchscores which are statistically highly significant.