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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