Elsevier

Phytochemistry

Volume 31, Issue 6, June 1992, Pages 1991-1996
Phytochemistry

Biosynthesis of neuroactive amino acids by cysteine synthases in Lathyrus latifolius

https://doi.org/10.1016/0031-9422(92)80347-HGet rights and content

Abstract

Two cysteine syntheses (CSases) purified from the aerial parts of Lathyrus latifolius could catalyse the formation of some heterocyclic β-substituted alanines such as β-(pyrazol-1-yl)-l-alanine from O-acetyl-l-serine (OAS) as additional catalytic activities. CSase isoenzyme A synthesized the neuroexcitatory amino acid l-quisqualic acid in the same manner as the formation of l-quisqualic acid by CSase in Quisqualis indica var. villosa. Both CSase isoenzymes also catalysed the formation of the neurotoxic amino acid β-cyano-l-alanine from OAS and CN. This activity is different from the biosynthesis of β-cyano-l-alanine from l-cysteine and CN as catalysed by β-eyano-alanine synthase. Several properties, including the amino acid compositions of the purified CSases, and the physiological role of these enzymes in higher plants are also described.

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    Cysteine is one of the substrates in the β-ODAP synthesis pathway. Ikegami et al. (1992) reported that biosynthesis of β-ODAP is connected to the sulfur amino acid biosynthetic pathway. Selenium and sulfur are congeners, and selenocysteine is formed when selenium replaces the sulfur position in amino acids during cysteine synthesis (Brown and Shrift, 2010).

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Parts of this work were reported at the 109th Annual Meeting of the Pharmaceutical Society of Japan at Nagoya, 5 April 1989 (Abstracts III-186) and also at the 1st Biennial International Conference on Amino Acid Research in Kyoto, 15 August 1991 (Abstracts, p. 19).

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