Mutant Genes of Gramicidin S Synthetase 1 Defective in Phenylalanine Racemization Have the Same Sequence as the Wild Gene

• Published in: Journal of biochemistry (Tokyo) 1994-12, Vol.116 (6), p.1202-1204
• Main Authors: Hori, Kazuko, Saito, Fumihiko, Tokita, Kazuhiko, Kurotsu, Toshitsugu, Kanda, Masayuki, Saito, Yoshitaka
• Format: Article
• Language: English
• Subjects: 4′ -phosphopantetheine; acyl carrier protein; Amino Acid Isomerases - chemistry; Amino Acid Isomerases - genetics; Amino Acid Isomerases - metabolism; Amino Acid Sequence; Bacillus - enzymology; Bacillus - genetics; Bacillus brevis; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Cloning, Molecular; gramicidin S synthetase 1; Molecular Sequence Data; Multienzyme Complexes - chemistry; Multienzyme Complexes - genetics; Multienzyme Complexes - metabolism; Mutation - genetics; Peptide Synthases - chemistry; Peptide Synthases - genetics; Peptide Synthases - metabolism; Phenylalanine - chemistry; Phenylalanine - metabolism; phenylalanine racemase; Racemases and Epimerases - genetics; Racemases and Epimerases - metabolism; Stereoisomerism; Structure-Activity Relationship
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a124663

Mutant grs1 genes were cloned and sequenced from the Bacillus brevis Nagano BI-4, C-3, E-l, and E-2 strains, which produce defective gramicidin S synthetase 1 (GS1), lacking racemase activity. Surprisingly, these mutant genes had entirely the same sequence as that of the wild type gene. These mutant strains also produce defective gramicidin S synthetase 2 (GS2), lacking 4′ -phosphopantetheine, a prosthetic group of this enzyme. The participation of this group in phenylalanine racemization is suggested.