EC Number |
Protein Variants |
Reference |
---|
3.2.1.80 | E201Q |
inactive |
682143 |
3.2.1.80 | more |
a D239A mutant of cell wall invertase 1 acts as a 1-FEH, preferentially degrading 1-kestose |
682426 |
3.2.1.80 | more |
immobilisation of the purified recombinant N-glycosylated enzyme designed to incorporate the optimal amount of protein/activity per surface area of aldehyde-activated glyoxyl-resin at pH 8.0-10.0, method overview |
731850 |
3.2.1.80 | more |
the internal region D' encoding the 157-amino-acid sequence in the Penicillium exoinulinase gene inuD cDNA is inserted into the site between the nucleotides 897 and 898 of the Aspergillus niger exoinulinase gene inuE cDNA. The resultant inuE:D' fusion is expressed in Pichia pastoris. The Km-value of the secreted hybrid enzyme InuE:D' for inulin hydrolysis is about 1/15 that of the Aspergillus niger InuE, whereas its kcat value does not differ greatly from that of the InuE |
-, 680950 |
3.2.1.80 | P294N |
mutant with an introduced N-glycosylation site near the inulin-binding cleft, shows highly decreased activity against higher DP inulin. The introduction of a glycosyl chain most probably blocks the cleft and prevents inulin binding and degradation |
682145 |
3.2.1.80 | P294N |
shows highly decreased activity against inulin |
682145 |
3.2.1.80 | S101L |
inactive |
682143 |
3.2.1.80 | S101L |
no inhibition by sucrose |
682143 |
3.2.1.80 | S101L |
strongly increased sucrose-hydrolysing activity compared with the wild-type enzym at high sucrose concentrations. At a very low substrate concentration (5 mm), the introduced sucrose hydrolysing activity is small compared with the activities towards the preferential 1-FEH IIa substrates 1-kestose and inulin |
682147 |
3.2.1.80 | W82L |
inactive |
682143 |