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Direct evidence for the participation of pyruvate in N ‐hydroxylation of lysine
Author(s) -
Szczepan Edward W.,
Kaller Damon,
Honek John F.,
Viswanatha Thammaiah
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)81444-8
Subject(s) - chemistry , hydroxylation , lysine , thiamine pyrophosphate , decarboxylation , biochemistry , oxidative decarboxylation , thiamine , pyruvate dehydrogenase complex , stereochemistry , amino acid , enzyme , cofactor , catalysis
The contribution of pyruvate to the formation of N 6 ‐acetyl‐ N 6 ‐hydroxylysine by a cell‐free system of Aerobacter aerogenes 62‐1 involved in the production of the dihydroxamate siderophore, aerobactin, has been assessed by a study of the influence of its analogs as well as of inhibitors of thiamine pyrophosphate‐dependent decarboxylation reactions. These studies have provided unequivocal evidence for pyruvate functioning not only as a source of reducing equivalents in the initial step of N ‐hydroxylation of lysine but also as a precursor of the acetyl moiety in the subsequent conversion of the N ‐hydroxy amino to its N 6 ‐acetyl derivative.