Literature summary extracted from
Lewis, R.A.; Nunns, L.; Thirlway, J.; Carroll, K.; Smith, C.P.; Micklefield, J.
Active site modification of the beta-ketoacyl-ACP synthase FabF3 of Streptomyces coelicolor affects the fatty acid chain length of the CDA lipopeptides (2011), Chem. Commun. (Camb. ), 47, 1860-1862.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.3.1.179 |
expressed in Escherichia coli BL21(DE3) |
Streptomyces coelicolor |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.3.1.179 |
F107I |
less efficient than wild type protein |
Streptomyces coelicolor |
2.3.1.179 |
F107L |
less efficient than wild type protein |
Streptomyces coelicolor |
2.3.1.179 |
F107S |
suggested that the Ser residue has less significant effects than the Ile and Leu mutations |
Streptomyces coelicolor |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.3.1.179 |
Streptomyces coelicolor |
- |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.3.1.179 |
beta-ketoacyl-ACP synthase FabF3 |
KAS-II homologue |
Streptomyces coelicolor |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.3.1.179 |
physiological function |
encoded in the gene cluster required for biosynthesis of the calcium dependent antibiotics |
Streptomyces coelicolor |