Reference to 1.1.1.168; Id = 761008 - BRENDA Enzyme Database

expressed in Escherichia coli BL21(DE3) cells

Candida dubliniensis

H128A

the mutant shows strongly reduced activity compared to the wild type enzyme

Candida dubliniensis

T30A

the mutant shows reduced activity compared to the wild type enzyme

Candida dubliniensis

Y66A

inactive

Candida dubliniensis

Ag+

complete inhibition at 1 mM

Candida dubliniensis

Ca2+

94.6% residual activity at 1 mM

Candida dubliniensis

Co2+

75.3% residual activity at 1 mM

Candida dubliniensis

Cu2+

29.7% residual activity at 1 mM

Candida dubliniensis

EDTA

85.7% residual activity at 1 mM

Candida dubliniensis

Fe2+

66.8% residual activity at 1 mM

Candida dubliniensis

Mg2+

77.6% residual activity at 1 mM

Candida dubliniensis

Mn2+

56.8% residual activity at 1 mM

Candida dubliniensis

Ni2+

88.5% residual activity at 1 mM

Candida dubliniensis

Pb2+

complete inhibition at 1 mM

Candida dubliniensis

Zn2+

10.8% residual activity at 1 mM

Candida dubliniensis

0.484

-

2-dehydropantolactone

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

3.5

-

2-dehydropantolactone

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

20.4

-

2-dehydropantolactone

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

2-dehydropantolactone + NADPH + H+

Candida dubliniensis

98% conversion and 99% enantiomeric excess within 2 h

(R)-pantolactone + NADP+

-

?

2-dehydropantolactone + NADPH + H+

Candida dubliniensis CD36

98% conversion and 99% enantiomeric excess within 2 h

(R)-pantolactone + NADP+

-

?

Candida dubliniensis

B9WJQ5

-

Candida dubliniensis CD36

B9WJQ5

-

Ni-NTA column chromatography

Candida dubliniensis

10.3

-

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

26.5

-

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

49.1

-

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

2-dehydropantolactone + NADPH + H+

98% conversion and 99% enantiomeric excess within 2 h

761008

Candida dubliniensis

(R)-pantolactone + NADP+

-

?

2-dehydropantolactone + NADPH + H+

98% conversion and 99% enantiomeric excess within 2 h

761008

Candida dubliniensis CD36

(R)-pantolactone + NADP+

-

?

x * 37000, SDS-PAGE

Candida dubliniensis

CPR

-

Candida dubliniensis

NADPH-dependent conjugated polyketone reductase

-

Candida dubliniensis

40

-

Candida dubliniensis

35

55

between 35 and 55Â°C, the enzyme activity remains above 70% of the maximal activity

Candida dubliniensis

30

50

the residual activity of recombinant enzyme maintains above 90% of the initial activity after 7 h at 30Â°C. When the enzyme is incubated at 50Â°C, above 30% of the initial activity still retains after 2 h. The recombinant enzyme exhibits adequate thermal stability, and its half-lives are 45.6, 8.6 and 1.7 h at 30, 40 and 50Â°C, respectively

Candida dubliniensis

6.01

-

2-dehydropantolactone

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

15.5

-

2-dehydropantolactone

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

59

-

2-dehydropantolactone

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

6.5

-

Candida dubliniensis

6.5

7

the half-lives of the enzyme are 12.8 and 8.9 h at pH 6.5 and pH 7.0, respectively

Candida dubliniensis

NADP+

-

Candida dubliniensis

expressed in Escherichia coli BL21(DE3) cells

Candida dubliniensis

NADP+

-

Candida dubliniensis

H128A

the mutant shows strongly reduced activity compared to the wild type enzyme

Candida dubliniensis

T30A

the mutant shows reduced activity compared to the wild type enzyme

Candida dubliniensis

Y66A

inactive

Candida dubliniensis

Ag+

complete inhibition at 1 mM

Candida dubliniensis

Ca2+

94.6% residual activity at 1 mM

Candida dubliniensis

Co2+

75.3% residual activity at 1 mM

Candida dubliniensis

Cu2+

29.7% residual activity at 1 mM

Candida dubliniensis

EDTA

85.7% residual activity at 1 mM

Candida dubliniensis

Fe2+

66.8% residual activity at 1 mM

Candida dubliniensis

Mg2+

77.6% residual activity at 1 mM

Candida dubliniensis

Mn2+

56.8% residual activity at 1 mM

Candida dubliniensis

Ni2+

88.5% residual activity at 1 mM

Candida dubliniensis

Pb2+

complete inhibition at 1 mM

Candida dubliniensis

Zn2+

10.8% residual activity at 1 mM

Candida dubliniensis

0.484

-

2-dehydropantolactone

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

3.5

-

2-dehydropantolactone

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

20.4

-

2-dehydropantolactone

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

2-dehydropantolactone + NADPH + H+

Candida dubliniensis

98% conversion and 99% enantiomeric excess within 2 h

(R)-pantolactone + NADP+

-

?

2-dehydropantolactone + NADPH + H+

Candida dubliniensis CD36

98% conversion and 99% enantiomeric excess within 2 h

(R)-pantolactone + NADP+

-

?

Ni-NTA column chromatography

Candida dubliniensis

10.3

-

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

26.5

-

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

49.1

-

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

2-dehydropantolactone + NADPH + H+

98% conversion and 99% enantiomeric excess within 2 h

761008

Candida dubliniensis

(R)-pantolactone + NADP+

-

?

2-dehydropantolactone + NADPH + H+

98% conversion and 99% enantiomeric excess within 2 h

761008

Candida dubliniensis CD36

(R)-pantolactone + NADP+

-

?

x * 37000, SDS-PAGE

Candida dubliniensis

40

-

Candida dubliniensis

35

55

between 35 and 55Â°C, the enzyme activity remains above 70% of the maximal activity

Candida dubliniensis

30

50

the residual activity of recombinant enzyme maintains above 90% of the initial activity after 7 h at 30Â°C. When the enzyme is incubated at 50Â°C, above 30% of the initial activity still retains after 2 h. The recombinant enzyme exhibits adequate thermal stability, and its half-lives are 45.6, 8.6 and 1.7 h at 30, 40 and 50Â°C, respectively

Candida dubliniensis

6.01

-

2-dehydropantolactone

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

15.5

-

2-dehydropantolactone

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

59

-

2-dehydropantolactone

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

6.5

-

Candida dubliniensis

6.5

7

the half-lives of the enzyme are 12.8 and 8.9 h at pH 6.5 and pH 7.0, respectively

Candida dubliniensis

0.295

-

2-dehydropantolactone

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

4.43

-

2-dehydropantolactone

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

122

-

2-dehydropantolactone

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

0.295

-

2-dehydropantolactone

mutant enzyme H128A, at pH 7.0 and 30Â°C

Candida dubliniensis

4.43

-

2-dehydropantolactone

mutant enzyme T30A, at pH 7.0 and 30Â°C

Candida dubliniensis

122

-

2-dehydropantolactone

wild type enzyme, at pH 7.0 and 30Â°C

Candida dubliniensis

761008

Cheng

Recombinant expression and mo ...

Candida dubliniensis, Candida dubliniensis CD36

Enzyme Microb. Technol.

126

77-85

2019

-

1

-

3

-

11

3

-

2

-

12

-

1

-

3

-

2

1

2

1

3

1

-

1

-

1

-

3

-

11

-

3

-

2

-

1

-

3

-

2

1

3

1

-

1

-

3

761570

Wang

Discovery of a new NADPH-depe ...

Candida orthopsilosis, Candida orthopsilosis 90-125

J. Biotechnol.

291

26-34

2019

-

1

-

9

1

-

1

-

2

-

6

-

1

-

13

1

2

1

-

1

-

1

-

1

-

9

-

1

-

1

-

2

-

1

-

13

1

-

1

-

347731

Julliard

-

Purification and characterizat ...

Spinacia oleracea

Bot. Acta

107

191-200

1994

-

3

4

-

1

-

1

-

1

-

1

6

1

-

1

-

1

-

1

-

1

-

3

1

4

-

1

-

1

-

1

6

1

-

1

-

1

-

347730

Kataoka

Enzymes involved in the NADPH ...

Saccharomyces cerevisiae, Candida parapsilosis, Mucor ambiguus, Mucor ambiguus AKU 3006

Biosci. Biotechnol. Biochem.

56

820-821

1992

-

5

-

7

-

2

-

7

-

2

-

347723

Hata

Ketopantoyl-lactone reductase ...

Saccharomyces cerevisiae

FEMS Microbiol. Lett.

58

87-90

1989

-

3

16

-

1

-

4

-

21

-

4

-

16

-

1

-

21

-

347724

Hata

Ketopantoyl-lactone reductase ...

Candida parapsilosis

Biochim. Biophys. Acta

990

175-181

1989

-

1

-

11

4

-

2

-

10

-

1

-

2

-

12

1

-

1

-

2

-

2

-

1

-

12

-

4

-

2

-

1

-

2

-

12

1

-

2

-

2

-

347726

Wilken

Ketopantoyl lactone reductases ...

Saccharomyces cerevisiae

Methods Enzymol.

62

209-215

1979

-

1

5

-

1

-

1

-

1

-

1

4

-

1

-

2

-

1

-

5

-

1

-

1

-

1

4

-

1

-

2

-

347725

Wilken

Stereospecificity of pantoyl l ...

Saccharomyces cerevisiae

Arch. Biochem. Biophys.

189

251-255

1978

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

286105

Wilken

Ketopantoic acid and ketopanto ...

Saccharomyces cerevisiae

J. Biol. Chem.

250

2311-2314

1975

-

1

-

1

-

4

-

1

-

4

-

347727

King

Ketopantoyl lactone and ketopa ...

Saccharomyces cerevisiae

J. Biol. Chem.

249

4689-4695

1974

-

4

-

1

-

1

-

1

-

2

-

1

-

4

-

1

-

1

-

2

-

1

-

286104

King

-

Separation and preliminary stu ...

Saccharomyces cerevisiae

J. Biol. Chem.

247

4096-4098

1972

-

2

-

1

-

4

-

1

-

2

-

4

-

1

-

Recombinant expression and molecular insights into the catalytic mechanism of an NADPH-dependent conjugated polyketone reductase for the asymmetric synthesis of (R)-pantolactone

Data extracted from this reference: