Table 4. Residues from the active sites of β-glucosidases in direct contact with sector A positions.
Sector A position | Active site residues | |||||||
SfβGly | 1UG6 | 1E4I | 1E56 | 1V03 | 1E6S | 2ZOX | 3AHY | |
54 | K201abr, M453abr | H178abr, A394abr | H179, A407 | F205abr, F466abr | L203abr, S462abr | D201, N466 | F179abr, N426 | F179, A426 |
98 | R97p | R75 | R77 | R96 | R97 | R95 | R75 | R73 |
143 | H142bg, E187*, E190abr, K201abr | H119bg, E164*, C167, H178abr | H121bg, E166*, C168, H179 | H142bg, D191*, T194, F205abr | H143bg, D189*, T192, L203abr | H141bg, Q187, S190abr, D201 | H120bg, Q165*, F179abr | H119bg, E165*, C168, F179 |
188 | E187*, E190abr | E164*, C167 | E166*, C168 | D191*, T194 | D189*, T192 | Q187, S190abr | Q165*, V168abr | E165*, C168 |
195 | E194abr | C167, L171abr, H178 | C168, L172, H179 | T194, F198abr, F205abr | T192, V196abr, L203abr | S190abr, R194abr, D201 | M172abr, F179abr | C168, P172, F179 |
196 | E194abr | L171abr | L172 | F198abr | V196abr | R194abr | M172abr | P172 |
203 | E194abr, K201abr | H178abr | H179 | F205abr | L203abr | D201 | F179abr | F179 |
398 | R97p, E399* | R75, E338* | R77, E352* | R96, E406* | R97, E404* | R95, E409* | E373* | R73, E367* |
451 | Q39bg, W444bg, M453abr | Q18bg, W385bg, A394abr | Q20bg, W398bg, A407 | Q38bg, W457bg, F466abr | Q39bg, W453, S462abr | Q39bg, W457bg, N466 | Q17, W417bg, N426 | Q16bg, W417bg, N426 |
452 | Q39bg, H142bg, K201abr, M453abr | Q18bg, H119bg, H178abr, A394abr | Q20bg, H121bg, H180, A407 | Q38bg, H142bg, F205abr, F466abr | Q39bg, H143bg, L203abr, S462abr | Q39bg, H141bg, N466 | Q17, H120bg, F179abr, N426 | Q16bg, H119bg, F179, N426 |
460 | Y331p, W444bg | Y284, W385bg | Y296, W398bg | Y333, W457bg | Y331, W453bg | W457bg | Y309, W417bg | Y298, W417bg |
The numbering of the sector A positions was based on the Sfβgly sequence. * identifies catalytic glutamic acids; p – indicates residues involved in the modulation of the pK a of the catalytic glutamic acids; bg – shows residues involved in the binding of the substrate glycone; abr – indicates residues that form the aglycone binding region. Data regarding the role of individual residues in substrate binding and catalysis were retrieved from the literature [5], [27], [28], [29], [9], [30]. β-Glucosidase from Spodoptera frugiperda Sfβgly; β-glucosidase from Thermus thermophilus (1UG6); β-glucosidase A from Paenibacillus polymyxa (1E4I); β-glucosidase Zmglu from Zea mays (1E56); β-glucosidase SbDhr from Sorghum bicolor (1V03); myrosinase from Sinapis alba (1E6S); Human cytosolic β-glucosidase (2ZOX);β-glucosidase from Trichoderma reesei (3AHY).