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. 2020 Jan 9;21(2):417. doi: 10.3390/ijms21020417

Table 1.

Kinetic parameters of PhNah20A and β-NAHAs from the literature on pNPGlcNAc and pNPGalNAc. SmS. marcescens; AhA. hydrophila; BbB. bifidum; CfC. fimi; VfV. furnissii; EhE. histolytica; TrTrichoderma reesei.

Enzyme Substrate KM (mM) Vmax (µmoL·mg−1·min−1) kcat (s−1) kcat/KM (mM−1·s−1)
PhNah20A pNPGlcNAc 0.43 ± 0.07 93.7 ± 5.0 146.8 341
pNPGalNAc 0.56 ± 0.11 123.0 ± 7.0 192.7 344
SmChb 1 pNPGlcNAc 56.7 ± 4.3 NI 111.0 1.95
AhNag20A 2 pNPGlcNAc 0.52 115 NI NI
pNPGalNAc 0.5 7.6 NI NI
AhNagB 2 pNPGlcNAc 8.57 25 NI NI
pNPGalNAc 11.1 11 NI NI
BbhI of Bb 3 pNPGlcNAc 120.0 ± 0.2 NI 213 178
pNPGalNAc NA NA NA NA
CfHex20 4 pNPGlcNAc 0.053 NI 482.3 9090
pNPGalNAc 0.066 NI 129.1 1950
VfExoI 5 pNPGlcNAc 0.09 270 NI NI
pNPGalNAc 0.33 130 NI NI
Hex2 6 pNPGlcNAc 0.48 NI 60.0 ± 1.7 NI
EhHexA 7 pNPGlcNAc 0.1 3.8 NI NI
TrNag1 pNPGlcNAc 69.4 ± 4.0 NI NI 1023 ± 23

Data from 1 [69], 2 [36] and [34], 3 [40], 4 [39], 5 [33], 6 [18], 7 [67]. NI—not indicated; NA—no detected activity.