Active site determination of novel plant versatile peroxidase extracted from Citrus sinensis and bioconversion of β-naphthol.

ABSTRACT: A ligninolytic peroxidase called versatile peroxidase, VP, (EC 1.11.1.16) is an iron-containing metalloenzyme. The most distinctive feature of this enzyme is its composite molecular framework, which combines lignin peroxidase's capacity to oxidize compounds with high-redox potential with manganese peroxidase's capacity to oxidize Mn²⁺ to Mn³⁺. In this study, we have extracted amino acid sequences from the Citrus sinensis source and subjected them to various computation tools to visualize the insight secondary and 3D structure, physicochemical properties, and validation of the structure which have not been studied so far to further investigate the catalytic efficiency and effectiveness of VP. The binding energies of HEME and HEME C (HEC) ligands with produced PD

SUBMITTER: Hoque RA 

PROVIDER: S-EPMC10501043 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature