SEARCHGTr

SEARCHGTr: Glycosyltransferase Sequence–Structure Analysis and Specificity Prediction

SEARCHGTr analyzes glycosyltransferases (GTrs) by correlating enzyme sequences with substrate chemical structures to predict donor/acceptor specificities and substrate-binding residues involved in the biosynthesis of compounds including adriamycin, erythromycin, and vancomycin.

Key Features:

• Sequence–Structure Correlation: Correlates glycosyltransferase amino acid sequences with corresponding substrate chemical structures to infer enzyme specificity and functional determinants.
• Specificity Prediction: Predicts donor and acceptor substrate specificities and identifies potential substrate-binding residues.
• Homology-Based Annotation: Retrieves and analyzes homologous glycosyltransferases using data from GENBANK, SWISS-PROT, CAZY, PDB, PDBSum, and PUBMED.
• Integration with NRPS-PKS: Enables combined computational analysis of glycosyltransferases with NRPS-PKS for coordinated evaluation of aglycone core biosynthesis and glycosylation processes.

Scientific Applications:

• Natural Product Biosynthesis: Supports prediction of enzyme specificity and substrate interactions for rational design of novel natural products and identification of secondary metabolite gene cluster products in newly sequenced genomes.

Methodology:

Developed through analysis of sequence and structural characteristics from 102 experimentally characterized glycosyltransferases across 52 natural product biosynthetic gene clusters, enabling predictive modeling of substrate specificity and functional residues.