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September 10, 2025International Journal of Molecular SciencesOpen Access

Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase from Desulfomonile tiedjei

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Authors

ABAlina K. BakunovaRussian Academy of Sciences IRIuliia V. RudinaA N Bach Institute of Biochemistry VPVladimir O. PopovRussian Academy of Sciences

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Implication

Functional characterization of a novel plp-dependent transaminase from Desulfomonile tiedjei reveals key second-shell interactions affecting stability and activity.

Key Points

The T199Q variant shows a fivefold increase in PLP affinity, enhancing catalytic activity under alkaline conditions.
PLP-dependent transaminases are essential for industrial enzyme applications, yet engineering them remains challenging.
Site-directed mutagenesis identified critical second-shell residues impacting cofactor binding and enzyme efficiency.
Understanding second-shell interactions can guide the design of more stable and versatile biocatalysts.

Cite This Study

Bakunova et al. (2025) studied this question.

synapsesocial.com/papers/68c1824b9b7b07f3a060ea7d https://doi.org/10.3390/ijms26178536

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Implication

Functional characterization of a novel plp-dependent transaminase from Desulfomonile tiedjei reveals key second-shell interactions affecting stability and activity.

Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase from Desulfomonile tiedjei

Discussion

Member takes

Implication

Key Points

Cite This Study

Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase from Desulfomonile tiedjei

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Implication

Key Points

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