2017
DOI: 10.1007/s10265-017-0986-5
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Molecular characterization of cytosolic cysteine synthase in Mimosa pudica

Abstract: In the cysteine and mimosine biosynthesis process, O-acetyl-L-serine (OAS) is the common substrate. In the presence of O-acetylserine (thiol) lyase (OASTL, cysteine synthase) the reaction of OAS with sulfide produces cysteine, while with 3-hydroxy-4-pyridone (3H4P) produces mimosine. The enzyme OASTL can either catalyze Cys synthesis or both Cys and mimosine. A cDNA for cytosolic OASTL was cloned from M. pudica for the first time containing 1,410 bp nucleotides. The purified protein product from overexpressed … Show more

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Cited by 5 publications
(2 citation statements)
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“…In legumes, biosynthesis of several secondary metabolites including β-cyanoalanine in Vicia sativa (common vetch), β-ODAP in Lathyrus species, and mimosine in Mimosa pudica is related to sulfur metabolism. ,, Generally, SAT that catalyzes the production of OAS from serine and acetyl-CoA is the rate-limiting enzyme in sulfur metabolism for its lower expression level . Three LsSATs were found in L.…”
Section: Discussionmentioning
confidence: 99%
“…In legumes, biosynthesis of several secondary metabolites including β-cyanoalanine in Vicia sativa (common vetch), β-ODAP in Lathyrus species, and mimosine in Mimosa pudica is related to sulfur metabolism. ,, Generally, SAT that catalyzes the production of OAS from serine and acetyl-CoA is the rate-limiting enzyme in sulfur metabolism for its lower expression level . Three LsSATs were found in L.…”
Section: Discussionmentioning
confidence: 99%
“…However, it turned out that cytosolic OAS-TL is specific for only cysteine synthesis and does not catalyze mimosine formation. The Mimosa pudica Mill enzyme has similar properties: the cloned cytosolic OASTL 1275 bp long cDNA expressed in E. coli , but enzyme produced cystein only [270]. Harun-Ur-Rashid et al [271] was the first to obtain the enzyme involved in the synthesis of mimosine.…”
Section: Biosynthesis Of Allelochemicalsmentioning
confidence: 99%