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Table 1 Catalytic efficiencies of the investigated CE15 enzymes on model substrates

From: Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion

Enzyme/substrate

kcat/Km (s−1M−1)a

BnzGlcA

AllylGlcA

MeGlcA

MeGalA

pNp-Ac

OtCE15A

4.64 × 103

8.80 × 103

6.85 × 103

4.85 × 103

3.23 × 101

OtCE15B

1.86 × 101

2.82

1.14

8.68

2.56

OtCE15C

1.16 × 104

2.49 × 103

8.98 × 102

1.19 × 103

3.97 × 101

OtCE15D

1.11 × 104

3.45 × 103

5.19 × 102

1.95 × 10−6

9.51

SlCE15A

1.88 × 103

1.00 × 103

1.55 × 103

3.82 × 101

3.09 × 101

SlCE15B

2.60 × 103

9.08 × 102

4.57 × 102

3.66 × 10−7

NDb

SlCE15C

9.69 × 101

1.11 × 102

1.03 × 102

3.73 × 10−6

NDb

SuCE15A

2.20 × 104

5.47 × 103

2.32 × 103

1.62 × 103

5.09

SuCE15B

1.49 × 103

3.65 × 102

6.00 × 10−2

9.00 × 10−3

1.82 × 101

SuCE15C

2.27 × 104

1.57 × 104

1.66 × 104

1.59 × 103

1.09 × 101

  1. Benzyl (Bnz), allyl (Allyl) and methyl (Me) esters of glucuronoate (GlcA) and galacturonoate (GalA), and 4-nitrophenol acetate (pNP-Ac)
  2. aSEM of duplicate measurements are presented in Additional files 1
  3. bNot determined due to activities below the detection limit