Structural and functional characterisation of the cytochrome P450 enzyme CYP268A2 from Mycobacterium marinum
Stromal cell-derived factor-1 (CXCL12) activates integrins by direct binding to an allosteric ligand-binding site (site 2) of integrins without CXCR4
Structural insights into the catalytic mechanism of cysteine (hydroxyl) lyase from the hydrogen sulfide-producing oral pathogen, Fusobacterium nucleatum
Propionate enters GABAergic neurons, inhibits GABA transaminase, causes GABA accumulation and lethargy in a model of propionic acidemia
CMS-G from Beta vulgaris ssp. maritima is maintained in natural populations despite containing an atypical cytochrome c oxidase
Crystal structure of thermospermine synthase from Medicago truncatula and substrate discriminatory features of plant aminopropyltransferases
Methionine sulfoxide reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase
The X-ray crystal structure of the substrate binding pocket of cytochrome P450 enzyme CYP268A2, from Mycobacterium marinum, with the molecule pseudoionone bound in the active site. In this issue of the Biochemical Journal, Bell et al. show how the substrate becomes completely enclosed by the active site of the enzyme; for details see pages 705–722.