Details
| Original language | English |
|---|---|
| Pages (from-to) | 529-546 |
| Number of pages | 18 |
| Journal | Molecular microbiology |
| Volume | 6 |
| Issue number | 4 |
| Publication status | Published - Feb 1992 |
| Externally published | Yes |
Abstract
The entire nucleotide sequence of the Bacillus brevis grsB gene encoding the gramicidin S synthetase 2, which activates and condenses the four amino acids proline, valine, ornithine and leucine has been determined. The gene contains an open reading frame of 13359bp which encodes a protein of 4453 amino acids with a predicted Mr of 510287. The gene is located within the gramicidin S biosynthetic operon, also containing the genes grsT and grsA, whose nucleotide sequences have been determined previously. Within the GrsB amino acid sequence four conserved and repeated domains of about 600 amino acids (45–50% identity) have been identified. The four domains are separated by non‐homologous sequences of about 500 amino acids. The domains also share a high degree of similarity (20–70%) with eight peptide synthetases of bacterial and fungal origin as well as with conserved sequences of nine other adenylate‐forming enzymes of diverse origin. On the basis of sequence homology and functional similarities, we infer that those enzymes share a common evolutionary origin and present a phylogenetic tree for this superfamily of domain‐bearing enzymes.
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Molecular microbiology, Vol. 6, No. 4, 02.1992, p. 529-546.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate‐forming enzymes
AU - Turgay, K.
AU - Krause, Michael
AU - Marahiel, M. A.
N1 - Copyright: Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1992/2
Y1 - 1992/2
N2 - The entire nucleotide sequence of the Bacillus brevis grsB gene encoding the gramicidin S synthetase 2, which activates and condenses the four amino acids proline, valine, ornithine and leucine has been determined. The gene contains an open reading frame of 13359bp which encodes a protein of 4453 amino acids with a predicted Mr of 510287. The gene is located within the gramicidin S biosynthetic operon, also containing the genes grsT and grsA, whose nucleotide sequences have been determined previously. Within the GrsB amino acid sequence four conserved and repeated domains of about 600 amino acids (45–50% identity) have been identified. The four domains are separated by non‐homologous sequences of about 500 amino acids. The domains also share a high degree of similarity (20–70%) with eight peptide synthetases of bacterial and fungal origin as well as with conserved sequences of nine other adenylate‐forming enzymes of diverse origin. On the basis of sequence homology and functional similarities, we infer that those enzymes share a common evolutionary origin and present a phylogenetic tree for this superfamily of domain‐bearing enzymes.
AB - The entire nucleotide sequence of the Bacillus brevis grsB gene encoding the gramicidin S synthetase 2, which activates and condenses the four amino acids proline, valine, ornithine and leucine has been determined. The gene contains an open reading frame of 13359bp which encodes a protein of 4453 amino acids with a predicted Mr of 510287. The gene is located within the gramicidin S biosynthetic operon, also containing the genes grsT and grsA, whose nucleotide sequences have been determined previously. Within the GrsB amino acid sequence four conserved and repeated domains of about 600 amino acids (45–50% identity) have been identified. The four domains are separated by non‐homologous sequences of about 500 amino acids. The domains also share a high degree of similarity (20–70%) with eight peptide synthetases of bacterial and fungal origin as well as with conserved sequences of nine other adenylate‐forming enzymes of diverse origin. On the basis of sequence homology and functional similarities, we infer that those enzymes share a common evolutionary origin and present a phylogenetic tree for this superfamily of domain‐bearing enzymes.
UR - http://www.scopus.com/inward/record.url?scp=0026588298&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2958.1992.tb01498.x
DO - 10.1111/j.1365-2958.1992.tb01498.x
M3 - Article
C2 - 1560782
AN - SCOPUS:0026588298
VL - 6
SP - 529
EP - 546
JO - Molecular microbiology
JF - Molecular microbiology
SN - 0950-382X
IS - 4
ER -