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Table 1 Kinetic constants ( K m , μM; k cat , s -1 ; and k cat / K m , s -1 .mM -1 ) for the nine PODs from the P. ostreatus genome a

From: Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability

Substrate

Kinetic constants

VP1

VP2

VP3

MnP1b

MnP2

MnP3

MnP4

MnP5

MnP6

VA

K m

5,500 ± 46

10,400 ± 133

5,500 ± 100

-c

-

-

-

-

-

k cat

12.7 ± 0.5

4.4 ± 0.2

1.7 ± 0.1

0

0

0

0

0

0

kcat/Km

2.3 ± 0.2

0.4 ± 0

0.3 ± 0

0

0

0

0

0

0

RB5

K m

5.4 ± 0.2

9.6 ± 1.8

1.2 ± 0.2

-

-

-

-

-

-

k cat

12.9 ± 0.3

20.3 ± 2

1.2 ± 0.1

0

0

0

0

0

0

kcat/Km

2,380 ± 50

2,120 ± 175

990 ± 150

0

0

0

0

0

0

ABTS e

K m

605 ± 81 (4.0 ± 0.4)

3,260 ± 363 (12 ± 1.6)

726 ± 30 (nsd)

111 ± 18

1,150 ± 38

778 ± 103

1,560 ± 76

455 ± 69

1,020 ± 80

k cat

126 ± 5 (14.4 ± 0.4)

209 ± 12 (8.7 ± 0.4)

328 ± 17 (ns)

90 ± 8

175 ± 3

222 ± 15

128 ± 3

53 ± 3

115 ± 5

kcat/Km

209 ± 21 (3,600 ± 20)

64 ± 4 (725 ± 36)

452 ± 10 (407 ± 12)

803 ± 7

152 ± 3

285 ± 19

82 ± 3

110 ± 10

112 ± 4

DMP e

K m

45,100 ± 3,600 (54 ± 4)

18,900 ± 2,070 (607 ± 57)

108,000 ± 13,000 (51 ± 14)

-

63,300 ± 12,800

59,100 ± 6,800

ns

ns

117,000 ± 18,000

k cat

98 ± 4 (6.6 ± 0.1)

92 ± 5 (17 ± 0.6)

311 ± 0.4 (2.9 ± 0.2)

0

109 ± 14

101 ± 7.2

ns

ns

56 ± 6

kcat/Km

2.2 ± 0.1 (122 ± 7)

4.9 ± 0 (28 ± 1)

2.9 ± 0.1 (57 ± 2)

0

1.7 ± 0.1

1.7 ± 0

0.4 ± 0

0.4 ± 0

0.5 ± 0

Mn 2+

K m

98 ± 5.6

18 ± 2

45 ± 3

7 ± 1

92 ± 5

101 ± 12

88 ± 4

22 ± 2

73 ± 9

k cat

185 ± 2.6

79 ± 2

172 ± 2

9 ± 0

159 ± 3

163 ± 5

125 ± 2

41 ± 1

109 ± 3

kcat/Km

1,900 ± 90

4,510 ± 412

3,930 ± 210

1,200 ± 80

1,730 ± 71

1,610 ± 170

1,410 ± 60

1,930 ± 170

1,500 ± 100

H 2 O 2

K m

64.6 ± 6.7

42.5 ± 1.4

220 ± 16

530 ± 92

66.7 ± 11.7

136 ± 7.5

85.6 ± 7.6

27.6 ± 1.2

22.8 ± 4.4

kcat/Km

1,750 ± 150

1,880 ± 40

2,410 ± 140

372 ± 54

3,680 ± 470

3,070 ± 130

3,040 ± 210

3,130 ± 110

3,280 ± 490

  1. aMeans and 95% confidence limits are shown; bdescribed as MnP [21], changed to VP because of the putative catalytic tryptophan [17], and renamed now as MnP1 because of its inability to oxidize high redox potential substrates; cdashes correspond to undetermined Km values when no activity was detected (kcat 0); dns, Km, and kcat not determined because of non-saturation (but kcat/Km determined from slope of observed activity versus concentration); eABTS and DMP oxidation by VPs showed biphasic kinetics providing a second set of constants (parenthesis) characterized by lower Km values (see Materials and methods section of Kinetic constants on selected substrates). ABTS, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate; DMP, 2,6-dimethoxyphenol; MnP, manganese peroxidase; POD, class II peroxidase from the superfamily of non-animal (plant-fungal-prokaryotic) peroxidases; RB5, Reactive Black 5; VA, veratryl alcohol; VP, versatile peroxidase.
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Biotechnology for Biofuels and Bioproducts

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