Plasma membrane bound high pI peroxidase isoenzymes convert tryptophan to indole-3-acetaldoxime

Phytochemistry

Volumn 29, Issue 5, 1990, Pages 1397-1400

  Ludwig Müller, Jutta ^a   Rausch, Thomas ^a   Lang, Siegfried ^a,b   Hilgenberg, Willy ^a  

^a GOETHE UNIVERSITY   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

Brassica campestris subsp. pekinensis; Brassicaceae; Chinese cabbage; indole 3 acetaldoxime peroxidase isoenzymes; l tryptophan.

Indexed keywords

EID: 0000913870     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/0031-9422(90)80088-X     Document Type: Article

References (21)

1. Role of Oximes in Nitrogen Metabolism in Plants
2. An Intermediate in the Synthesis of Glucobrassicins from 3-Indoleacetaldoxime by Woad Leaves
3. Localization of newly synthesized indoIe-3-methylglucosinolate (= glucobrassicin) in vacuoles from horseradish (Armoracia rusticana)
4. Indole-3-methylglucosinolate biosynthesis and metabolism in clubroot diseased plants
5. Biosynthesis and conjugation of indole-3-acetic acid in tobacco crown gall
6. A plasma membrane-bound enzyme oxidizes l-tryptophan to indole-3-acetaldoxime
7. The biosynthesis of cyanogenic glucosides in higher plants. Channeling of intermediates in dhurrin biosynthesis by a microsomal system from Sorghum bicolor (linn) Moench.