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Literature summary for 1.14.13.22 extracted from

  • Yachnin, B.J.; McEvoy, M.B.; MacCuish, R.J.; Morley, K.L.; Lau, P.C.; Berghuis, A.M.
    Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis (2014), ACS Chem. Biol., 9, 2843-2851 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rhodococcus sp. HI-31

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method. Two crystal structures of cyclohexanone monooxygenase with its product, epsilon-caprolactone, bound: the CHMO(Tight) and CHMO(Loose) structures. The CHMO(Tight) structure represents the enzyme state in which substrate acceptance and stereospecificity is determined, providing a foundation for engineering BVMOs with altered substrate spectra and/or stereospecificity. The CHMO(Loose) structure is the first structure where the product is solvent accessible. This structure represents the enzyme state upon binding and release of the substrate and product Rhodococcus sp. HI-31

Organism

Organism UniProt Comment Textmining
Rhodococcus sp. HI-31 C0STX7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rhodococcus sp. HI-31