Literature summary for 2.3.1.85 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 .

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Crystallization (Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
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
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
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
G2559S/M2600W	mutant produces produces a bimodal spectrum of C8- and C14/C16-CoA in vitro	Corynebacterium ammoniagenes
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
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

Organism	UniProt	Comment	Textmining
Corynebacterium ammoniagenes	-	-	-

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Release 2023.1 (January 2023)