Excavating the functionally crucial active-site residues of the DXS protein of Bacillus subtilis by exploring its closest homologues.

ABSTRACT:

Background

To achieve a high yield of terpenoid-based therapeutics, 1-deoxy-d-xylulose-5-phosphate (DXP) pathway has been significantly exploited for the production of downstream enzymes. The DXP synthase (DXS) enzyme, the initiator of this pathway, is pivotal for the convergence of carbon flux, and is computationally studied well for the industrially utilized generally regarded as safe (GRAS) bacterium Bacillus subtilis to decode its vital regions for aiding the construction of a functionally improved mutant library.

Results

For the 546 sequence dataset of DXS sequences, a representative set of 108 sequences is created, and it shows a significant evolutionary divergence across different species clubbed into 37 clades, whereas three clades are observed for the 76 sequence da

SUBMITTER: Runthala A 

PROVIDER: S-EPMC7691408 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature