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3.5.1.77: N-carbamoyl-D-amino-acid hydrolase

This is an abbreviated version!
For detailed information about N-carbamoyl-D-amino-acid hydrolase, go to the full flat file.

Word Map on EC 3.5.1.77

Reaction

an N-carbamoyl-D-amino acid
+
H2O
=
a D-amino acid
 +
NH3
 +
CO2

Synonyms

AcHyuC, Amidase, N-carbamoyl-D-amino acid, BJS_06659, carbamoylase, D-carbamoylase, D-N-alpha-Carbamoylase, D-N-carbamoylase, D-NCAase, Dcase, DCase-M3, DCHase, hyuD, N-carbamoyl D-amino acid amidohydrolase, N-Carbamoyl-D-amino acid amidase, N-carbamoyl-D-amino acid amidohydrolase, N-Carbamyl amino acid amidohydrolase, N-Carbamyl-D-amino acid amidohydrolase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.77 N-carbamoyl-D-amino-acid hydrolase

Engineering

Engineering on EC 3.5.1.77 - N-carbamoyl-D-amino-acid hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H57L
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
H57Y
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
P203A
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203H
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203I
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203L
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
P203N
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203S
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
P203T
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
V236A
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
V236S
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
V236T
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
H57Y
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
-
P203L
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
-
P203S
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
-
A222C
-
crystal structure is nearly identical to wild-type enzyme, half-life at 50°C is 1.1fold higher than that of wild-type enzyme
A302C
-
crystal structure is nearly identical to wild-type enzyme, 123.9% of wild-type activity, temperature-optimum is 10°C higher than that of wild-type enzyme, half-life at 50°C is 2.5fold higher than that of wild-type enzyme, 4.2fold increase in kcat/Km at 65°C, 1.5fold increase at 55°C and 1.15fold increase at 37°C
C172A
C172S
G75S
-
96% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 42.5% compared to 5% for the wild-type enzyme
G75S/V237A
-
mutant, thermal stability 55.6%, wild-type 3.0%, oxidative stability 42.8%, wild-type 5.0%
H129A
-
inactive mutant enzyme
H129N
-
inactive mutant enzyme
H129R
-
inactive mutant enzyme
H144A
-
5% of the activity of wild-type enzyme
H215A
-
17% of the activity of wild-type enzyme
H58Y
-
80% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 20.6% compared to 5% for the wild-type enzyme
I286V/F287A
-
mutant, thermal stability 4.5%, wild-type 3.0%, oxidative stability 4.8%, wild-type 5.0%
M167L/M169L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 37% for mutant enzyme, compared to 21% for wild-type enzyme
M184L
M184L/T262A
-
46% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 54.8% compared to 5% for the wild-type enzyme. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 58.6% of the wild-type ratio
M220L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 62% for mutant enzyme, compared to 21% for wild-type enzyme
M239L
-
mutant enzyme is stable after treatment with 0.5 mM H2O2 for 15 min compared to 79% loss of wild-type activity
M239L/M244L
-
mutant enzyme is stable after treatment with 0.5 mM H2O2 for 15 min compared to 79% loss of wild-type activity
M244L
-
mutant enzyme is stable after treatment with 0.5 mM H2O2 for 15 min compared to 79% loss of wild-type activity
M31L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 8% for mutant enzyme, compared to 21% for wild-type enzyme
M5L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 51% for mutant enzyme, compared to 21% for wild-type enzyme
M73L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 84% for mutant enzyme, compared to 21% for wild-type enzyme
N173A
-
KM-value for N-carbamoyl-D-p-hydroxyphenylglycine is 40% of the wild-type value. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 5.5fold lower than wild-type ratio. Tm is 68°C compared to 63° for wild-type enzyme
P178C
-
half-life at 50°C is nearly identical to wild-type enzyme
P295C/F304C
-
107.3% of wild-type activity, temperature-optimum is 5°C higher than that of wild-type enzyme, half-life at 50°C is 2fold higher than that of wild-type enzyme. 2.5fold increase in kcat/Km at 65°C, 1.1fold increase at 55°C and at 37°C
Q23L
-
81% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 63.9% compared to 5% for the wild-type enzyme
Q23L/V40A/H58Y/G75S/M184L/T262A
-
mutant enzyme with improved oxidative and thermostability, 79.3% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 72.4% of the wild-type ratio
R175A
-
inactive mutant enzyme
R175K
-
KM-value for N-carbamoyl-D-p-hydroxyphenylglycine is 2.5fold higher than the wild-type value. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 4706fold lower than wild-type ratio. Tm is 65°C compared to 63° for wild-type enzyme
R176A
-
inactive mutant enzyme
R176K
-
KM-value for N-carbamoyl-D-p-hydroxyphenylglycine is 4.2fold higher than the wild-type value. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 364fold lower than wild-type ratio. Tm is 65°C compared to 63° for wild-type enzyme
T262A
V237A/C279S
-
mutant, thermal stability 22.4%, wild-type 3.0%, oxidative stability 31.2%, wild-type 5.0%
V40A/G75S/V237A
-
mutant, thermal stability 68.4%, wild-type 3.0%, oxidative stability 80.3%, wild-type 5.0%
V40A/G75S/V237A/I286V/F287A
-
mutant, thermal stability 72.3%, wild-type 3.0%, oxidative stability 83.1%, wild-type 5.0%
M184L
-
80% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 20% compared to 5% for the wild-type enzyme
-
M184L/T262A
-
46% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 54.8% compared to 5% for the wild-type enzyme. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 58.6% of the wild-type ratio
-
Q23L
-
81% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 63.9% compared to 5% for the wild-type enzyme
-
T262A
C172A
-
mutant enzyme Cys172Ala or Cys172Ser is completely inactive. Substitution of any of the other Cys has no effect on enzyme activity
-
C172S
-
mutant enzyme Cys172Ala or Cys172Ser is completely inactive. Substitution of any of the other Cys has no effect on enzyme activity
-
A164T
-
mutant, screening for thermostable enzyme
A18T/Y30N/K34E
-
kinetic properties and thermodynamic parameters of the mutant enzyme are identical with those of the wild-type enzyme. More than 80% improve in solubility compared to wild-type enzyme
A36E
-
mutant, screening for thermostable enzyme
A36V
-
mutant, screening for thermostable enzyme
H248Q
-
mutant, screening for thermostable enzyme
H248Q/T262A
-
the mutant displays a T50 value of 65°C and a DELTAT50 enhancement of 8°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
H58Y
-
mutant, screening for thermostable enzyme
K34D
-
mutant has higher solubility than wild-type enzyme
K34E
-
mutant has higher solubility than wild-type enzyme
Q12A
-
saturation mutagenesis at position Gln12, thermostability 13.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12C
-
saturation mutagenesis at position Gln12, thermostability 9.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12D
-
saturation mutagenesis at position Gln12, thermostability 8.9%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12E
-
saturation mutagenesis at position Gln12, thermostability 9.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12F
-
saturation mutagenesis at position Gln12, thermostability 14.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12G
-
saturation mutagenesis at position Gln12, thermostability 20.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12H
-
saturation mutagenesis at position Gln12, thermostability 12.8%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12I
-
saturation mutagenesis at position Gln12, thermostability 14.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12K
-
saturation mutagenesis at position Gln12, thermostability 11.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12L/Q23L/H248Q/T262A/T263S
-
the mutant exhibits an increase of 10°C in thermostability compared with the parental enzyme M3
Q12L/Q23L/H248Q/T262A/T263S/A273K
-
the mutant displays a T50 value of 69°C and a DELTAT50 enhancement of 12°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/E266D
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/M31L
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/M31L/N242G
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/M31L/Q207E
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N242G
-
the mutant displays a T50 value of 69°C and a DELTAT50 enhancement of 12°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N242G/A273P
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N242G/T271I/A273P
-
the mutant displays a T50 value of 72°C and a DELTAT50 enhancement of 15°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N93Y
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/Q207E
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/Q207E/N242G
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/T271I
-
the mutant displays a T50 value of 69°C and a DELTAT50 enhancement of 12°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/T271I/A273K
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/Q207E/N242G/H248Q/T262A/T263S/E266D/T271I/A273P
-
the mutant displays a T50 value of 73°C and a DELTAT50 enhancement of 16°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%). The mutant retains over 50% of its initial activity after heat treatment at 57°C for at least 100 min
Q12M
-
saturation mutagenesis at position Gln12, thermostability 9.2%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12N
-
saturation mutagenesis at position Gln12, thermostability 15.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12P
-
saturation mutagenesis at position Gln12, thermostability 12.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12R
-
saturation mutagenesis at position Gln12, thermostability 9.2%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12S
-
saturation mutagenesis at position Gln12, thermostability 12.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12T
-
saturation mutagenesis at position Gln12, thermostability 14.8%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12V
-
saturation mutagenesis at position Gln12, thermostability 20.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12W
-
saturation mutagenesis at position Gln12, thermostability 16.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12Y
-
saturation mutagenesis at position Gln12, thermostability 11.9%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T262A
-
mutant, screening for thermostable enzyme
T263A
-
saturation mutagenesis at position Thr263, thermostability 8.6%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263C
-
saturation mutagenesis at position Thr263, thermostability 13.2%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263D
-
saturation mutagenesis at position Thr263, thermostability 10.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263E
-
saturation mutagenesis at position Thr263, thermostability 12.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263F
-
saturation mutagenesis at position Thr263, thermostability 13.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263G
-
saturation mutagenesis at position Thr263, thermostability 15.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263H
-
saturation mutagenesis at position Thr263, thermostability 15.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263I
-
saturation mutagenesis at position Thr263, thermostability 14.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263K
-
saturation mutagenesis at position Thr263, thermostability 11.8%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263L
-
saturation mutagenesis at position Thr263, thermostability 10.4%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263M
-
saturation mutagenesis at position Thr263, thermostability 23.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263N
-
saturation mutagenesis at position Thr263, thermostability 14.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263P
-
saturation mutagenesis at position Thr263, thermostability 14.6%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263Q
-
saturation mutagenesis at position Thr263, thermostability 10.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263R
-
saturation mutagenesis at position Thr263, thermostability 9.6%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263S
T263V
-
saturation mutagenesis at position Thr263, thermostability 8.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263W
-
saturation mutagenesis at position Thr263, thermostability 9.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263Y
-
saturation mutagenesis at position Thr263, thermostability 12.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
V237A
-
mutant, screening for thermostable enzyme
H248Q/T262A
-
the mutant displays a T50 value of 65°C and a DELTAT50 enhancement of 8°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
-
Q12L
-
the mutant displays a T50 value of 63°C and a DELTAT50 enhancement of 6°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
-
Q12L/Q23L/H248Q/T262A/T263S
-
the mutant exhibits an increase of 10°C in thermostability compared with the parental enzyme M3
-
Q12L/Q23L/H248Q/T262A/T263S/M31L
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
-
Q12L/Q23L/Q207E/N242G/H248Q/T262A/T263S/E266D/T271I/A273P
-
the mutant displays a T50 value of 73°C and a DELTAT50 enhancement of 16°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%). The mutant retains over 50% of its initial activity after heat treatment at 57°C for at least 100 min
-
additional information