Background: Bis(monoacylglycero)phosphate (BMP) plays a key role in the degradation and sorting of lipids in acidic organelles.Results: ABHD6 degrades BMP and co-localizes with late endosomes/lysosomes. Knockdown of ABHD6 increases hepatic BMP levels.Conclusion: ABHD6 controls BMP catabolism.Significance: ABHD6 is part of the late endosomal/lysosomal lipid-sorting machinery.

S2General. All reactions were carried out under Ar in glassware dried with a heat gun under vacuum (Schlenk line). The solvents were purified by distillation over the indicated drying agents and were transferred under Ar: THF, Et 2 O (Mg/anthracene), acetone (B 2 O 3 ), toluene (Na/K), CH 2 Cl 2 (CaH 2 ), MeOH (Mg, stored over 3Å MS); DMSO, DMF, CH 3 CN, NEt 3 and pyridine were dried by an adsorption solvent purification system based on molecular sieves. Unless stated otherwise, all commercially available compounds (ABCR, Acros, Aldrich, Strem, TCI) were used as received. [(Cp*RuCl) 4 ] was prepared according to a literature procedure and was stored under Argon. 1 Thin layer chromatography (TLC): Macherey-Nagel precoated plates (POLYGRAM® SIL/UV254); Flash chromatography: Merck silica gel 60 (40-63 μm) with predistilled or HPLC grade solvents; IR: ALPHA spectrometer (Bruker), wavenumbers (ṽ) in cm -1 . MS (EI): Finnigan MAT 8200 (70 eV), ESIMS: ESQ 3000 (Bruker), accurate mass determinations: Bruker APEX III FT-MS (7 T magnet) or MAT 95 (Finnigan); Optical rotations ([ ] ) were measured with a Perkin-Elmer Model 343 polarimeter.NMR: Spectra were recorded on a Bruker AV 400, AV 500 or AV 600 spectrometer in the solvents indicated; chemical shifts (δ) are given in ppm relative to TMS, coupling constants (J) in Hz. The solvent signals were used as references and the chemical shifts converted to the TMS scale (CDCl 3 at 7.26 and 77.16 ppm, CD 3 OD at 3.31 ppm and 49.00 ppm for 1 H and 13 C NMR spectroscopy, respectively).Where indicated, the signal assignments in the NMR spectra are unambiguous; the numbering scheme is arbitrary as shown in the inserts.(R)-Oct-1-en-3-ol (4). Novozyme (300 mg) was added to a solution of (±)-oct-1-en-3-ol (8.0 mL, 6.6 g, 52 mmol) and vinyl acetate (18.0 mL, 194 mmol) in hexane (70 mL) and the resulting suspension was gently stirred (~ 50 rpm) at ambient temperature. The progress of the reaction was monitored by GC-MS. After 42 h the immobilized enzyme was filtered off and rinsed with hexane (4 x 10 mL) and the combined filtrates were concentrated under reduced pressure. Purification of the residue by flash chromatography (hexane/tert-butyl methyl ether, 9:1 → 1:1) yielded the product as colorless liquid with a mushroom-like odor (2.27 g, 34%). The physical properties of the product were in full accordance with the literature; 2 the enantiomeric excess (> 99% ee) was determined by gas chromatography using a chiral stationary phase, cf: 1 P.

The assigned structure of the dinoflagellate-derived toxin belizentrin was prepared by total synthesis in form of the corresponding methyl ester for stability reasons. The successful route features an unusual solution for the preparation of a recalcitrant ylide on a C-glycosidic segment; moreover, it involves an asymmetric hetero-Diels-Alder reaction en route to the tertiary hemiacetal substructure, a Negishi cross-coupling of two elaborate building blocks, and a macrocyclization based on an intramolecular aminolysis of a spirolactone. A modified Kocienski olefination ultimately allowed the polyol side chain to be attached to the macrocycle although this transformation faced the exceptional base sensitivity of this polyunsaturated target compound.

A set of S‐adenosyl‐l‐methionine (SAM) dependent methyltransferases has been characterized as versatile catalysts for the enzymatic Friedel–Crafts (alkylation) reaction. Although the substrate specificity of the enzymes range from high (in the case of SfmM2, SacF, and ORF19) to moderate (in the case of NovO and CouO), the cofactor spectrum is broad. Modified cofactors decorated with alkyl groups other than methyl were used for biocatalytic Friedel–Crafts alkylation, and conversions up to 99 % were achieved. In contrast to the classical chemical reaction the biotransformation is very selective and environmentally compatible.

We report the synthesis of diverse β‐hydroxy‐α,α‐dialkyl‐α‐amino acids with perfect stereoselectivity for the α‐quaternary center through the action of l‐ and d‐specific threonine aldolases. A wide variety of aliphatic and aromatic aldehydes were accepted by the enzymes and conversions up to >80 % were obtained. In the case of d‐selective threonine aldolase from Pseudomonas sp., generally higher diastereoselectivities were observed. The applicability of the protocol was demonstrated by performing enzymatic reactions on preparative scale. Using the d‐threonine aldolase from Pseudomonas sp., (2R,3S)‐2‐amino‐3‐(2‐fluorophenyl)‐3‐hydroxy‐2‐methylpropanoic acid was generated in preparative amounts in one step with a diastereomeric ratio >100 favoring the syn‐product. A Birch‐type reduction enabled the reductive removal of the β‐hydroxy group from (2S)‐2‐amino‐3‐hydroxy‐2‐methyl‐3‐phenylpropanoic acid to generate enantiopure l‐α‐methyl‐phenylalanine via a two‐step chemo‐enzymatic transformation.