Comparative modeling and enzymatic affinity of novel haloacid dehalogenase from strain BHS1 isolated from alkaline Blue Lake in Turkey.

This study presents the initial structural model of L-haloacid dehalogenase (DehLBHS1) from BHS1, an alkalotolerant bacterium known for its ability to degrade halogenated environmental pollutants. The model provides insights into the structural features of DehLBHS1 and expands our understanding of the enzymatic mechanisms involved in the degradation of these hazardous pollutants. Key amino acid residues (Arg40, Phe59, Asn118, Asn176, and Trp178) in DehLBHS1 were identified to play critical roles in catalysis and molecular recognition of haloalkanoic acid, essential for efficient binding and transformation of haloalkanoic acid molecules.

Molecular interactions of trichoderma β-1,4-glucosidase (ThBglT12) with mycelial cell wall components of phytopathogenic .

Efficacy of a β-1,4-glucosidase from T12 (ThBglT12) in disrupting the cell wall of the phytopathogenic fungus () was studied, as the underlying molecular mechanisms of cell wall recognition remains elusive. In this study, the binding location identified by a consensus of residues predicted by COACH tool, blind docking, and multiple sequence alignment revealed that molecular recognition by ThBglT12 occurred through interactions between the α-1,3-glucan, β-1,3-glucan, β-1,3/1,4-glucan, and chitin components of , with corresponding binding energies of -7.4, -7.

Molecular docking and molecular dynamics simulations of a mutant alkaline-stable lipase against tributyrin.

We previously reported on a mutant lipase KV1 (Mut-LipKV1) from which optimal pH was raised from 8.0 to 11.0 after triple substitutions of surface aspartic acid (Asp) with lysine (Lys).