Lipase Engineering Database

Lipase Engineering Database catalogs and classifies α/β-hydrolases by integrating protein sequence and structural data to enable analysis of sequence-structure-function relationships and evolutionary networks.

Key Features:

• Comprehensive Data Collection: Contains 280,638 protein sequences and 1,557 protein structures of α/β-hydrolases.
• Structural Classification: Classifies enzymes into 12 architectures including core domain only, lids at three positions, three cap types, N- or C-terminal domains, and combinations of these modules.
• Oxyanion Hole Signatures: Distinguishes oxyanion hole types as GX-, GGGX-, and Y-types relevant to catalytic mechanism.
• Domain Folds: Identifies N-terminal domains with Rossmann or β-propeller folds and C-terminal domains with β-sandwich folds, noting structural resemblance to lectins.
• Application to Novel Enzymes: Assigns PETases and MHETases as core-domain α/β-hydrolases of the GX- and GGGX-types, respectively.
• Evolutionary Network Analysis: Analyzes sequence networks that exhibit a power-law degree distribution with scaling exponent γ = 1.4, indicating hub-dominated connectivity and functional robustness of hubs.
• Cluster Analysis: Reports a cluster size distribution following a power law with extrapolated scaling exponent τ = 2.6.

Scientific Applications:

• Sequence-structure-function analysis: Provides a framework to relate protein sequences and structural architectures to biochemical function.
• Evolutionary dynamics and robustness: Enables study of evolutionary relationships and the functional robustness of hub sequences in sequence networks.
• Analogue identification: Supports identification of potential structural and functional analogs among α/β-hydrolases.

Methodology:

Integrates sequence and structural data and applies sequence-network analysis to classify and analyze α/β-hydrolases.