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Prediction of substrate‐specific pockets in cyclosporin synthetase
Author(s) -
Husi Holger,
Schörgendorfer Kurt,
Stempfer Günter,
Taylor Paul,
Walkinshaw Malcolm D
Publication year - 1997
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/s0014-5793(97)01064-8
Subject(s) - amino acid , luciferase , biochemistry , peptide sequence , mutant , binding site , biology , binding pocket , homology (biology) , sequence homology , amino acid residue , adenylylation , chemistry , enzyme , gene , biosynthesis , transfection
Amino acid sequence comparisons between domains of cyclosporin synthetase have been used to identify regions of the sequence which are responsible for the recognition and binding of the individual amino acids. Using a limited set of selection rules it was possible to identify three amino acid positions in the subdomain sequences which are responsible for amino acid specificity. Homology with the firefly luciferase protein shows that these three key residues are close to each other and line the surface of a putative specific substrate binding pocket located on the amino acyl‐adenylation subdomain. These results allow us to predict a large number of cyclosporin synthetase mutants which could be used to synthesise alternative cyclosporin‐like peptides.