2024
DOI: 10.1021/acs.jafc.3c09589
|View full text |Cite
|
Sign up to set email alerts
|

Enhancing the Thermal Stability and Enzyme Activity of Ketopantoate Hydroxymethyltransferase through Interface Modification Engineering

Xue Cai,
Xue Shi,
Jia-Ying Wang
et al.

Abstract: Ketopantoate hydroxymethyltransferase (KPHMT) plays a pivotal role in D-pantothenic acid biosynthesis. Most KPHMTs are homodecamers with low thermal stability, posing challenges for protein engineering and limiting output enhancement. Previously, a high-enzyme activity KPHMT mutant (K25A/E189S) from Corynebacterium glutamicum was screened as mother strain (M0). Building upon this strain, our study focused on interface engineering modifications, employing a multifaceted approach including integrating folding-fr… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

0
0
0

Publication Types

Select...

Relationship

0
0

Authors

Journals

citations
Cited by 0 publications
references
References 48 publications
0
0
0
Order By: Relevance

No citations

Set email alert for when this publication receives citations?