Reprint of: 1-Aminocyclopropanecarboxylate Synthase, a Key Enzyme in Ethylene Biosynthesis.

1-Aminocyclopropanecarboxylate (ACC) synthase, which catalyzes the conversion of S-adenosylmethionine (SAM) to ACC and methylthioadenosine, was demonstrated in tomato extract. Methylthioadenosine was then rapidly hydrolyzed to methylthioribose by a nucleosidase present in the extract. ACC synthase had an optimum pH of 8.

Tracing phenolic metabolism in Vitis vinifera berries with 13C6-phenylalanine: implication of an unidentified intermediate reservoir.

Understanding the regulation of phenolic compounds in agricultural products has been a topic of great interest. In V. vinifera berries, phenolics are responsible for important sensory and functional characteristics.

Tracing phenolic biosynthesis in Vitis vinifera via in situ C-13 labeling and liquid chromatography-diode-array detector-mass spectrometer/mass spectrometer detection.

Phenolic compounds in Vitis vinifera contribute important flavor, functionality, and health qualities to both table and wine grapes. The plant phenolic metabolic pathway has been well characterized, however many important questions remain regarding the influence of environmental conditions on pathway regulation. As a diagnostic for this pathway's regulation, we present a technique to incorporate a stable-isotopic tracer, L-phenyl-(13)C(6)-alanine (Phe(13)), into grape berries in situ and the accompanying high throughput analytical method based on LC-DAD-MS/MS to quantify and track the label into phenylalanine metabolites.

Aviglycine and propargylglycine inhibit conidial germination and mycelial growth of Fusarium oxysporumf. sp. luffae.

Two inhibitors, aviglycine and propargylglycine, were tested for their ability to suppress methionine synthesis thus inhibit conidial germination and mycelial growth of Czapek-Dox liquid medium grown Fusarium oxysporum f. sp. luffaemuM.