ThYme

ThYme catalogs amino acid sequences and three-dimensional structures of thioester-active enzymes involved in fatty acid and polyketide synthesis cycles.

Key Features:

• Enzyme Coverage: Includes enzymes that act on thioester-containing substrates, specifically acyl-CoA synthase, acyl-CoA carboxylase, acyl transferase, ketoacyl synthase, ketoacyl reductase, hydroxyacyl dehydratase, enoyl reductase, and thioesterase.
• Classification: Organizes enzymes into families based on amino acid sequence similarity, tertiary-structure similarity, and catalytic mechanism, indicating common protein ancestry within families.
• Data Integration: Integrates amino acid sequence data with three-dimensional tertiary-structure information for enzyme entries.
• Continual Updates: Is dynamically updated to incorporate newly available sequences and tertiary structures.

Scientific Applications:

• Structural Biology: Provides 3D structures to support analyses of enzyme mechanisms and interactions with substrates or inhibitors.
• Bioinformatics and Computational Biology: Supports sequence alignment, phylogenetic analysis, and modeling of enzyme function using sequence and structural data.
• Drug Discovery and Development: Supplies structural and functional enzyme data to aid identification of potential targets within fatty acid and polyketide synthesis pathways.
• Evolutionary Studies: Enables tracing of enzyme family development and diversification across organisms through family classification.

Methodology:

Classification is based on amino acid sequence similarity, tertiary-structure similarity, and catalytic mechanism; the resource integrates sequence and 3D structural data and is applied using sequence alignment, phylogenetic analysis, and modeling.