HIGHLIGHTS
- who: Yu Yang from the (UNIVERSITY) have published the research work: Adapting to oxygen: 3-Hydroxyanthrinilate 3,4-dioxygenase employs loop dynamics to accommodate two substrates with disparate polarities, in the Journal: (JOURNAL) of May/18,/2018
- what: Using O2 saturated buffer, the kcat of N27A reached the same level of wtHAO, indicating that the primary reason for a substantial negative impact of the N27A mutation in catalysis with the regular buffer is a decreased oxygen-binding affinity.
- how: The authors chose 3-hydroxyanthranilate 34-dioxygenase (HAO)3 a ring-cleaving dioxygenase as . . .
If you want to have access to all the content you need to log in!
Thanks :)
If you don't have an account, you can create one here.