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Group specific antibodies against the putative AMP‐binding domain signature SGTTGXPKG in peptide synthetases and related enzymes
Author(s) -
Etchegaray Augusto,
Dieckmann Ralf,
Engel Paul C.,
Turner Geoffrey,
Döhren Hans
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201262
Subject(s) - biochemistry , biology , gramicidin s , enzyme , peptide , peptide sequence , adenylate kinase , gene , gramicidin , membrane
Abstract The superfamily of adenylate forming enzymes including peptide synthetases, acyl‐CoA synthetases and insect luciferases is readily identified by the signature sequence SGTTGXPKG. This sequence including an invariant lysyl residue is located in a disordered loop region and was predicted to be of significant antigenicity. Antibodies were generated employing YTSGTTGRPKGC attached to bovine serum albumin and have been successfully used to identify respective enzymes and adenylate forming domains in multienzyme systems. These include the δ‐(L‐α‐aminoadipyl)‐L‐cysteinyl‐D‐valine synthetases of Aspergillus nidulans and Acremonium chrysogenum, gramicidin S synthetase 1 and tyrocidine synthetase 1 from Bacillus brevis, acetyl‐CoA synthetase from Alcaligenes eutrophus and a putative peptide synthetase from Metarhizium anisopliae. Weaker or no reactions are observed when the amino acid in position X in the protein is non‐basic or hydrophobic, which is respectively the case for gramicidin S synthetase 1 and luciferase.