- PII
- 10.31857/S0023476124060075-1
- DOI
- 10.31857/S0023476124060075
- Publication type
- Article
- Status
- Published
- Authors
- Volume/ Edition
- Volume 69 / Issue number 6
- Pages
- 981-986
- Abstract
- Pyridoxal-5'-phosphate (PLP)-dependent enzymes are one of the most widely represented groups of enzymes in organisms, performing more than 150 different catalytic functions. Based on the three-dimensional structure, members of this group are divided into seven (I-VII) different fold types. Cofactor binding in these enzymes occurs due to the formation of a Schiff base with a conserved lysine residue located in the active site. A recently discovered protein from the bacterium Variovorax paradoxus (VAPA), which belongs to the IV fold type and has significant structural similarity to transaminases, contains an asparagine residue at the catalytic lysine position in the transaminases and, as a result, cannot form a Schiff base with PLP and does not have aminotransferase activity. In this research, a point mutant of VAPA protein with the N174K substitution was obtained and its 3D structure was determined. Analysis of the structural data showed that the introduced mutation restores the ability of VAPAN174K to form a Schiff base with a cofactor.
- Keywords
- Date of publication
- 15.09.2025
- Year of publication
- 2025
- Number of purchasers
- 0
- Views
- 14
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