Literature summary for 1.14.13.22 extracted from

Fuerst, M.J.L.J.; Boonstra, M.; Bandstra, S.; Fraaije, M.W.
Stabilization of cyclohexanone monooxygenase by computational and experimental library design (2019), Biotechnol. Bioeng., 116, 2167-2177 .

Search for more literature for 1.14.13.22

Protein Variants

Protein Variants	Comment	Organism
E91Q/A115V/R280Y/N431Y/Q439P/A455V/S534R	most stable mutant found, increase in unfolding temperature of 13 K and an approximately 33fold increase in half-life at 30°C	Rhodococcus sp. HI-31
E91Q/D95H/A115V/Q191M/R280Y/N431Y/Q439P/A455V/S534R	increase in melting temperature of 15 K, highly diminished activity	Rhodococcus sp. HI-31
E91Q/D95H/A115V/R280Y/N431Y/Q439P/A455V/S534R	increase in melting temperature of 13 K, highly active	Rhodococcus sp. HI-31
Q409P/N431Y/A115V/A455V	increase in melting temperature of 6.3 K	Rhodococcus sp. HI-31

Organism

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
cyclohexanone + NADPH + H+ + O2	-	Rhodococcus sp. HI-31	hexano-6-lactone + NADP+ + H2O	-	?

Synonyms

Synonyms	Comment	Organism
ChnB	-	Rhodococcus sp. HI-31

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
36	-	melting temperature of wild-type	Rhodococcus sp. HI-31
48.8	-	melting temperature of mutant E91Q/D95H/A115V/R280Y/N431Y/Q439P/A455V/S534R	Rhodococcus sp. HI-31

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
4.9	-	cyclohexanone	mutant E91Q/D95H/A115V/R280Y/N431Y/Q439P/A455V/S534R, pH 7.5, temperature not specified in the publication	Rhodococcus sp. HI-31
9.2	-	cyclohexanone	wild-type, pH 7.5, temperature not specified in the publication	Rhodococcus sp. HI-31

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Release 2023.1 (January 2023)