DynLib

DynLib compiles LC-MS spectral metadata for 5,420 maize metabolites to support structural characterization and metabolic network analysis.

Key Features:

• Extensive compound characterization: Contains LC-MS spectral metadata for 5,420 compounds and enabled structural characterization of 427 compounds, including phenylpropanoids, flavonoids, benzoxazinoids, and auxin-related compounds, of which 75 were previously documented in maize.
• Organ-resolved profiling: Profiles metabolites from five distinct maize organs using various reversed-phase LC-MS methods.
• Candidate substrate-product pair (CSPP) networks: Integrates CSPP networks to reveal metabolic relationships and organ-specific metabolite enrichment.
• Reaction-level mass-difference analysis: Identifies frequent mass differences corresponding to glycosyl- and acyltransferase reactions leading to diverse mixed glycosides with substructures from multiple biochemical classes.
• Organ-specific molecular patterns: Reveals examples such as maize tassel glycosides that combine phenylpropanoid, flavonoid, and auxin-derived moieties.

Scientific Applications:

• Metabolic pathway discovery: Supports identification of candidate biochemical transformations and pathway relationships via CSPP networks and mass-difference analysis.
• Specialized metabolism mapping: Enables organ-specific mapping of phenylpropanoid, flavonoid, benzoxazinoid, and auxin-related metabolite distributions.
• Systems biology and metabolic engineering: Provides spectral evidence for enzyme-associated modifications (glycosylation, acylation) useful for modeling and engineering plant metabolic networks.
• Compound identification in plant biochemistry and genetics: Facilitates discovery and structural annotation of novel maize metabolites for biochemical and genetic studies.

Methodology:

Profiling of five maize organs using various reversed-phase LC-MS methods, structural characterization of compounds, integration of candidate substrate-product pair (CSPP) networks, and mass-difference analysis to infer glycosyl- and acyltransferase reactions.