EC Number   |
Protein Variants |
Reference |
|---|
   3.2.1.25 | E555A |
low activity |
680752 |
| 3.2.1.25 | E555Q |
molecular modeling and electron densitiy studies of the Michaelis complex |
708104 |
| 3.2.1.25 | more |
mutation associated with caprine beta-mannosidosis: single-base deletion at position 1398 of the coding sequence results in a shift in the reading frame, yielding a deduced peptide of 481 amino acids |
136037 |
| 3.2.1.25 | N461A |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | N461A |
low activity |
680752 |
| 3.2.1.25 | Q646A |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | Q646A |
low activity |
680752 |
| 3.2.1.25 | Q77R |
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 2fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.1fold higher than that for 4-nitrophenyl beta-D-mannopyranoside |
-, 654641 |
| 3.2.1.25 | Q77R |
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides |
750443 |
| 3.2.1.25 | Q77R/D206N |
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 8fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.4fold higher than that for 4-nitrophenyl beta-D-mannopyranoside |
-, 654641 |
