Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.85 extracted from

  • Asturias, F.J.; Chadick, J.Z.; Cheung, I.K.; Stark, H.; Witkowski, A.; Joshi, A.K.; Smith, S.
    Structure and molecular organization of mammalian fatty acid synthase (2005), Nat. Struct. Mol. Biol., 12, 225-232.
    View publication on PubMed
Search for more literature for 2.3.1.85

Protein Variants

Protein Variants Comment Organism
C161Q mutation of ketoacyl synthase, less conformational variability than wild-type Rattus norvegicus
G1888A mutation of beta-ketoacyl reductase, less conformational variability than wild-type Rattus norvegicus
K326A mutation of ketoacyl synthase, less conformational variability than wild-type Rattus norvegicus
S2302A mutation of thioesterase, less conformational variability than wild-type Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Subunits

Subunits Comment Organism
More structural analysis by electron microscopy, enzyme monomers in the dimeric form adopt a coiled conformation that allows for a variety of intra- and intermonomer functional domain interactions Rattus norvegicus