Structural dynamics studies of wild-type and mutant candida boidinii nad+-dependent formate dehydrogenase

Candida boidinii NAD+-dependent formate dehydrogenase (cbFDH) is a biotechnologically invaluable enzyme that recently gained more attention on biosynthetic applications for biofuel production. Structure-based mutants of this enzyme performed highly promising results of enhanced catalytic activity and thermal stability. In this study, we aimed to employ a holistic approach and combine X-ray crystallographic analysis of NAD+-dependent cboFDH with Gaussian Network Model analysis to determine the underpinnings of the cboFDH catalytic mechanism and allostery. Additionally, Alphafold2 predictions of a mutant form of cbFDH enzyme were discussed for mutation-based structure prediction efficiency. The 1.4 A resolution X-ray crystallography data of NAD+-dependent cbFDH revealed the structural dynamics of the enzyme with the help of the computational approach. This understanding of enzymatic dynamics and the effect of mutations on structure and function may provide new insight for future biotechnology studies.