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Literature summary extracted from

  • Rossini, E.; Gajewski, J.; Klaus, M.; Hummer, G.; Grininger, M.
    Analysis and engineering of substrate shuttling by the acyl carrier protein (ACP) in fatty acid synthases (FASs) (2018), Chem. Commun. (Camb.), 54, 11606-11609 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.85 structure-based homology modeling based on PDB entry 2uv8 Corynebacterium ammoniagenes

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.85 D2553A/G2559S/M2600W in addition to G2559S/M2600W, mutation in ketoacyl synthase domain KS, mutation increases the fraction of long chain acyl-CoA produced Corynebacterium ammoniagenes
2.3.1.85 D2553N/G2559S/M2600W in addition to G2559S/M2600W, mutation in ketoacyl synthase domain KS, mutation increases the fraction of long chain acyl-CoA produced Corynebacterium ammoniagenes
2.3.1.85 D2556A/G2559S/M2600W in addition to G2559S/M2600W, mutation in ketoacyl synthase domain KS, mutation increases the fraction of long chain acyl-CoA produced Corynebacterium ammoniagenes
2.3.1.85 G2559S/D2622A/M2600W in addition to G2559S/M2600W, mutation in ketoacyl synthase domain KS, mutant is most efficient in C8-CoA production but impaired in activity Corynebacterium ammoniagenes
2.3.1.85 G2559S/M2600W mutant produces produces a bimodal spectrum of C8- and C14/C16-CoA in vitro Corynebacterium ammoniagenes
2.3.1.85 G2559S/N2621D/M2600W in addition to G2559S/M2600W, mutation in ketoacyl synthase domain KS, mutant is most efficient in C8-CoA production but impaired in activity Corynebacterium ammoniagenes
2.3.1.85 N2557E/G2559S/M2600W in addition to G2559S/M2600W, mutation in ketoacyl synthase domain KS, mutant is most efficient in C8-CoA production but impaired in activity Corynebacterium ammoniagenes

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.85 Corynebacterium ammoniagenes
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