Abstract
Metal-binding peptides derived from glutathione and having the structure (γGlu-Cys)nGly[(γEC)nG] were first described by Murasugi et al. [1] in studies of Schizosaccharomyces pombe growing in the presence of added cadmium ions. These peptides were subsequently found to be synthesized in a wide variety of plant species [2] and have been designated as phytochelatins, gamma-glutamyl peptides, and class III metallothioneins. The enzyme responsible for the step-wise addition of the γEC moiety to γECG (glutathione) or an already formed (γEC)nG has been isolated from Silene cucubalis and partially characterized. The enzyme is a dipeptidyl transferase that has been given the trivial name phytochelatin synthase and has been reported to be constitutive in plants [3].
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References
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© 1999 Springer Basel AG
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Lauro, M.M., Plocke, D.J. (1999). Synthesis and properties of class III metallothioneins of Schizosaccharomyces pombe in response to cadmium and zinc. In: Klaassen, C.D. (eds) Metallothionein IV. Advances in Life Sciences. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8847-9_25
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DOI: https://doi.org/10.1007/978-3-0348-8847-9_25
Publisher Name: Birkhäuser, Basel
Print ISBN: 978-3-0348-9799-0
Online ISBN: 978-3-0348-8847-9
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