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C1622

Sigma-Aldrich

Cyclohexanone Monooxygenase from Acinetobacter sp.

≥12 U/mL, ammonium sulfate suspension, recombinant, expressed in E. coli

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CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

ammonium sulfate suspension

concentration

≥12 U/mL

storage temp.

−20°C

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This Item
P2621G6278G6637
Glycerokinase from Escherichia coli 300-600 units/mL, ammonium sulfate suspension

G6278

Glycerokinase from Escherichia coli

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

-

Quality Level

-

Quality Level

-

Application

Cyclohexanone monooxygenase has been used in a study that cloned and overexpressed the 2-oxo-Δ(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (OTEMO) in Escherichia coli. Cyclohexanone monooxygenase has also been used in a study that investigated the effects of structural modification of the cell wall on the biotransformation capability by recombinant Corynebacterium glutamicum cells.

Biochem/physiol Actions

Purified cyclohexanone monooxygenase has a molecular weight of 59,000 Da. It is a versatile oxygenation catalyst. The enzyme uses the bound FAD-4a-OOH oxygenating intermediate to initiate transfer of oxygen to electrophilic substrate sites. The reaction consequently yields the corresponding sulfoxide and selenoxide products. This enzyme is also capable of oxygenating at nitrogen, trivalent phosphorus, and boron sites in boronic acids. Hence, it is one of the most broad-based flavoprotein oxygenases known.

Unit Definition

1 unit corresponds to the amount of enzyme which catalyzes the cyclohexanone-stimulated oxidation of 1 μmol of NADPH per minute at pH 9.0 and 30 °C

Physical form

Suspension in 80% saturated ammonium sulfate, 20 mM K-Na-phosphate buffer pH 7, 3.5 mM 1,4-Dithioerythritol (DTE)

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Ji-Yeong Yun et al.
Bioprocess and biosystems engineering, 35(1-2), 211-216 (2011-09-13)
The effects of structural modification of cell wall on the biotransformation capability by recombinant Corynebacterium glutamicum cells, expressing the chnB gene encoding cyclohexanone monooxygenase of Acinetobacter calcoaceticus NCIMB 9871, were investigated. Baeyer-Villiger oxygenation of 2-(2'-acetoxyethyl) cyclohexanone (MW 170 Da) into
Iakov Polyak et al.
Journal of the American Chemical Society, 134(5), 2732-2741 (2012-01-14)
We report a combined quantum mechanical/molecular mechanical (QM/MM) study on the mechanism of the enzymatic Baeyer-Villiger reaction catalyzed by cyclohexanone monooxygenase (CHMO). In QM/MM geometry optimizations and reaction path calculations, density functional theory (B3LYP/TZVP) is used to describe the QM
D Sheng et al.
Biochemistry, 40(37), 11156-11167 (2001-09-12)
Cyclohexanone monooxygenase (CHMO), a bacterial flavoenzyme, carries out an oxygen insertion reaction on cyclohexanone to form a seven-membered cyclic product, epsilon-caprolactone. The reaction catalyzed involves the four-electron reduction of O2 at the expense of a two-electron oxidation of NADPH and
Hannes Leisch et al.
Applied and environmental microbiology, 78(7), 2200-2212 (2012-01-24)
A dimeric Baeyer-Villiger monooxygenase (BVMO) catalyzing the lactonization of 2-oxo-Δ(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A (CoA), a key intermediate in the metabolism of camphor by Pseudomonas putida ATCC 17453, had been initially characterized in 1983 by Ougham and coworkers (H. J. Ougham, D. G.
Y C Chen et al.
Journal of bacteriology, 170(2), 781-789 (1988-02-01)
The gene coding for cyclohexanone monooxygenase from Acinetobacter sp. strain NCIB 9871 was isolated by immunological screening methods. We located and determined the nucleotide sequence of the gene. The structural gene is 1,626 nucleotides long and codes for a polypeptide

Articles

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