INU point mutation: catalytic activity under acidic pH (N158S)
Positive AI-extracted, curator-verified MARXBASE-R000596
| Gene | INU Enzyme or protein label, not a gene symbol |
|---|---|
| Gene from | K. marxianus |
| Change | point mutation |
| Effect | increases |
| Phenotype | catalytic activity under acidic pH (N158S) (enzyme activity) |
| Class | Positive |
| Host | Pichia pastoris |
| Strain | GS115 |
| Product | Secreted enzyme (Enzymes) |
Measured
| Value | 464.06 |
|---|---|
| Size as written | maximum 464.06 ± 14.06 s-1 on inulin at pH 4.5 |
| Metric | activity |
Conditions
| pH | 4.5 |
|---|---|
| Carbon source | inulin |
Evidence
Evidence sentences are not included in this release.
Paper
Engineering better catalytic activity and acidic adaptation into Kluyveromyces marxianus exoinulinase using site-directed mutagenesis.
Wang CH; Xiong WP; Huang C; Li XM; Wang QY; Huang RB
Journal of the science of food and agriculture 2021 · PubMed · DOI
Cite as: MarxBase result MARXBASE-R000596, release 1.0.