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Using an improved purification and derivatization procedure, the endogenous gibberellin-O-glucosides in mature runner beans (Phaseolus coccineus) were analysed by combined gas chromatography-mass spectrometry. In addition to the previously characterized GA1-3-O-glucoside and GA8-2-O-glucoside, from runner beans, the following GA-O-glucosides were identified as endogenously occurring compounds by comparison of their full scan mass spectra and Kovats retention indices with those of standards: GA1-13-O-glucoside, 3-epiGA1-3-O-glucoside, GA5-13-O-glucoside and GA29-2-O-glucoside. The first three are reported in higher plants for the first time. The physiological relevance of the detected GA-O-glucosides is discussed.

Data on the occurrence of free and conjugated gibberellins in different tribes of Gramineae are compiled and discussed with regard to their biosynthetic pathways. From the gibberellins detected so far the functioning of both the early 13-hydroxylation and the non-3,13-hydroxylation pathway of GA biosynthesis in gramineous plants can be deduced and the discovery of further gibberellin conjugates may be expected.

Acridone synthase was isolated from cell suspension cultures of Ruta graveolens which catalysed the formation of 1,3-dihydroxy-N- methylacridone from N-methylanthraniloyl-CoA and malonyl-CoA. No cofactors were required for this enzyme reaction. Potassium phosphate buffer was superior compared to Tris-HCl. Sodium ascorbate instead of mercaptoethanol as oxidation protectant showed an advantageous effect on acridone synthase activity. The enzyme was strongly inhibited by 1,3-dihydroxy-N-methylacridone and by the antibiotic cerulenin. Microsomal preparations from Ruta graveolens cell suspension cultures catalysed an NADPH- and oxygen-dependent condensation of 1,3-dihydroxy-N- methylacridone and isopentenyl pyrophosphate. The reaction product was identified as rutacridone. Mg2+ or Mn2+ ions were necessary for optimal rutacridone synthase activity. The enzyme was inhibited by a number of inhibitors of cytochrome P-450 enzymes. A prenylated acridone, viz. glycocitrine-II was identified as an essential intermediate. Under in vivo conditions glycocitrine-II is incorporated into rutacridone, but a clear-cut conversion of glycocitrine-II by microsomal preparations (cyclase) was not observed. Microsomes converted rutacridone into furofoline-I. A number of detergents was used for solubilization of membrane-bound proteins of Ruta microsomes. Highest specific glycocitrine -II synthase (prenyltransferase) activity was obtained after solubilization with dodecylmaltoside.

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Coenzyme A thioesters of anthranilic acid and N‐methylanthranilic acid were synthesized. The corresponding N‐hydroxysuccinimidyl esters proved to be useful as activated intermediates to prepare anthraniloyl‐CoA and N‐methylanthraniloyl‐CoA. These compounds were characterized by positive and negative ion liquid secondary ion mass spectrometry. Acridone synthase from suspension cultures of Ruta graveolens catalyses the condensation of N‐methylanthraniloyl‐CoA and malonyl‐CoA. The reaction product 1,3‐dihydroxy‐N‐methylacridone was directly identified after the extraction of the assay mixture by electron impact mass spectrometry and capillary gas chromatography.

(Diphenylmethylene)amine [benzophenone imine, DPMA-H] cleanly reacts with a variety of α,β-unsaturated esters, nitriles, ketones, and aldehydes 1a-q to give Michael type adducts 2a-q, generally, in respectable to excellent yields. Sterically congested and donor-substituted Michael acceptors do not react. The β-amino-substituted products can be further transformed in their protected form, or selectively deprotected under mild conditions, e.g. by catalytic hydrogenation.

Cyclopropane amino acids have attracted the attention of synthetically and biologically oriented chemists throughout the last decade. Most efforts have been directed towards 1-aminocyclopropane carboxyclic acid (ACC), the natural precursor of the phytohormone ethylene,1 and its derivatives. Other natural cyclopropane amino acids as well as artificial ones were used as enzyme inhibitors for receptor and metabolism studies.2 We report here a new synthetic approach to a wide variety of cyclopropyl-substituted amino acids including the natural products cleonin (1) (1-hydroxycyclopropyl-glycin)3 and 1-methylcyclopropyl- glycin (2).4