1.13.11.88: isoeugenol monooxygenase

the mutation results in a 1.3fold increase in specific activity

H167A

mutation of conserved His residue, involved in binding of Fe2+. Loss of catalytic activity

H205A

mutation of conserved His residue, 6.8% residual catalytic activity

H218A

mutation of conserved His residue, involved in binding of Fe2+. Loss of catalytic activity

H282A

mutation of conserved His residue, involved in binding of Fe2+. Loss of catalytic activity

I352R

the mutant with 99.7% activity shows better thermostability than the wild type enzyme (70.4% residual activity after 15 min at 35°C)

K83R

the mutant with 103.9% activity shows better thermostability than the wild type enzyme (84.2% residual activity after 15 min at 35°C)

K83R/I352R

the mutant with 99.2% activity shows better thermostability than the wild type enzyme (87.8% residual activity after 15 min at 35°C)

K83R/K95R

the mutant with 104.8% activity shows better thermostability than the wild type enzyme (92.1% residual activity after 15 min at 35°C)

K83R/K95R/G398A

the mutant with 130.1% activity shows better thermostability than the wild type enzyme (94.1% residual activity after 15 min at 35°C)

K83R/K95R/I352R

the mutant with 114.3% activity shows better thermostability than the wild type enzyme (90.1% residual activity after 15 min at 35°C)

K83R/K95R/L273F

compared with the wild type enzyme, the thermal inactivation half-lives (t1/2) of the mutant at 25°C, 30°C, and 35°C increase 2.9fold, 11.9fold, and 24.7fold, respectively. Simultaneously, it also exhibits a 4.8fold increase in kcat, leading to a 1.2fold increase in catalytic efficiency. The tolerance of the mutant to metal ions is also improved

K95R

the mutant with 106.6% activity shows better thermostability than the wild type enzyme (68% residual activity after 15 min at 35°C)

L273F

the mutant exhibits 1.17fold increase in specific activity compared to the wild type enzyme

G398A

the mutation results in a 1.3fold increase in specific activity

I352R

the mutant with 99.7% activity shows better thermostability than the wild type enzyme (70.4% residual activity after 15 min at 35°C)

K83R

the mutant with 103.9% activity shows better thermostability than the wild type enzyme (84.2% residual activity after 15 min at 35°C)

K95R

the mutant with 106.6% activity shows better thermostability than the wild type enzyme (68% residual activity after 15 min at 35°C)

L273F