B. S. Moore

Molecular Forecasting of Domoic Acid during a Pervasive Toxic Diatom Bloom

The paper identifies molecular predictors of domoic acid production during a harmful algal bloom and links iron and silica co-limitation to bloom dynamics and toxicity.

Oxidative rearrangement of tryptophan to indole nitrile by a single diiron enzyme

This study identifies a novel diiron enzyme, AetD, that catalyzes the oxidative rearrangement of tryptophan to indole nitrile, revealing a new pathway for nitrile biosynthesis.

Mechanistic and structural insights into a divergent PLP-dependent L-enduracididine cyclase from a toxic cyanobacterium

This study characterizes the biosynthesis of L-enduracididine, a cyclic arginine noncanonical amino acid, by analyzing the enzyme GntC from a cyanobacterium using structural and biochemical methods.

Extreme genome diversity and cryptic speciation in a harmful algal bloom forming eukaryote

This study presents genome assemblies of fifteen Prymnesium parvum strains, revealing extreme genome diversity, cryptic speciation, and hybridization, with implications for understanding harmful algal blooms.

Phylogenetic analysis of the salinipostin γ-butyrolactone gene cluster uncovers new potential for bacterial signaling-molecule diversity

The paper identifies spt-like gene clusters in diverse bacteria, suggesting broader distribution of γ-butyrolactone production and potential for new signaling molecules.

Expansion of gamma-butyrolactone signaling molecule biosynthesis to phosphotriester natural products

The paper identifies the spt operon in Salinispora species as responsible for producing both saliniphostins and A-factor-like gamma-butyrolactones, revealing its broad distribution across actinomycete genera.

Co-Occurrence of Enzyme Domains Guides the Discovery of an Oxazolone Synthetase

The paper introduces CO-ED, a genome mining approach that identifies novel multifunctional enzymes by analyzing co-occurring enzyme domains, leading to the discovery of an oxazolone synthetase.

Algal Neurotoxin Biosynthesis Repurposes the Terpene Cyclase Structural Fold Into an N-prenyltransferase

The paper reports the structure and function of prenyltransferases from marine algae that repurpose the terpene cyclase fold for N-prenylation of glutamic acid, enabling the biosynthesis of neurotoxins like domoic acid.