Literature summary 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 .

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.13.22	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

EC Number	Organism	UniProt	Comment	Textmining
1.14.13.22	Rhodococcus sp. HI-31	C0STX7	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.14.13.22	-	Rhodococcus sp. HI-31

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Release 2023.1 (January 2023)