Literature summary for 1.14.13.22 extracted from

Latham, J.A.; Walsh, C.
Mechanism-based in activation of the flavoenzyme cyclohexanone oxygenase during oxygenation of cyclic thiol ester substrates (1987), J. Am. Chem. Soc., 109, 3421-3427.

No PubMed abstract available

Search for more literature for 1.14.13.22

Inhibitors

Inhibitors	Comment	Organism	Structure
2-Thiacyclohexanone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
2-Thiocyclohexanone	-	Acinetobacter sp.
delta-thiovalerolactone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
ethylene monothiocarbonate	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
additional information	inactivation mechanism	Acinetobacter sp.
S-gamma-Thiobutyrolactone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.006	-	cyclohexanone	-	Acinetobacter sp.
0.01	-	3-thiacyclohexanone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
0.016	-	4-methylcyclohexanone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
0.021	-	4-thiacyclohexanone	-	Acinetobacter sp.
0.024	-	Thiane	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter sp.	-	NCIB 9871	-

Purification (Commentary)

Purification (Comment)	Organism
partially	Acinetobacter sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
8	10	partially purified enzyme, substrate 4-methylcyclohexanone	Acinetobacter sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-thiacyclohexanone + NADPH + O2	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.	1-oxa-2-oxo-3-thiacycloheptane + NADP+ + H2O	-	?
3-thiacyclohexanone + NADPH + H+ + O2	-	Acinetobacter sp.	?	-	r
4-methylcyclohexanone + NADPH + O2	-	Acinetobacter sp.	1-oxa-2-oxo-5-methylcycloheptane + NADP+ + H2O	-	?
4-thiacyclohexanone + NADPH + H+ + O2	-	Acinetobacter sp.	?	-	r
cyclohexanone + NADPH + O2	-	Acinetobacter sp.	6-hexanolide + NADP+ + H2O	-	?
delta-thiovalerolactone + NADPH + O2	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.	?	-	ir
epsilon-thiocaprolactone + NADPH + O2	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.	?	-	ir
ethylene monothiocarbonate + NADPH + O2	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.	?	-	?
ethylene monothiocarbonate + NADPH + O2	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.	?	-	ir
gamma-thiobutyrolactone + NADPH + O2	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.	?	-	ir
S-gamma-thiobutyrolactone + NADPH + O2	substrate irreversibly inactivates enzyme after a few turnovers	Acinetobacter sp.	?	-	?
thiane + NADPH + O2	-	Acinetobacter sp.	?	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.227	-	epsilon-thiocaprolactone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
0.24	-	delta-thiovalerolactone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
0.683	-	gamma-thiobutyrolactone	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.
2.38	-	ethylene monothiocarbonate	substrate inactivates enzyme after a few turnovers	Acinetobacter sp.

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Acinetobacter sp.

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
2	-	ethylene monothiocarbonate	-	Acinetobacter sp.
2	-	S-gamma-Thiobutyrolactone	-	Acinetobacter sp.
2	-	2-Thiocyclohexanone	-	Acinetobacter sp.
2.9	-	delta-thiovalerolactone	-	Acinetobacter sp.

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Release 2023.1 (January 2023)