Literature DB >> 12729016

Synthesis of hydroxymethylglutathione from glutathione and L-serine catalyzed by carboxypeptidase Y.

Ryosuke Okumura1, Yukio Koizumi, Jiro Sekiya.   

Abstract

Hydroxymethylglutathione (gamma-L-glutamyl-L-cysteinyl-L-serine; hmGSH) occurs in many species belonging to the family Gramineae, but the biosynthetic pathway for hmGSH has not been identified. We found that carboxypeptidase Y (CPY), but not carboxypeptidase A, catalyzed hmGSH synthesis from glutathione and L-serine in vitro at acidic pH. CPY also catalyzed methylglutathione synthesis from glutathione and L-alanine. These findings suggested that a carboxypeptidase-like enzyme may be involved in hmGSH synthesis in vivo.

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Year:  2003        PMID: 12729016     DOI: 10.1271/bbb.67.434

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  3 in total

1.  Glutathione.

Authors:  Graham Noctor; Guillaume Queval; Amna Mhamdi; Sejir Chaouch; Christine H Foyer
Journal:  Arabidopsis Book       Date:  2011-02-18

2.  Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays).

Authors:  Mark Skipsey; Benjamin G Davis; Robert Edwards
Journal:  Biochem J       Date:  2005-11-01       Impact factor: 3.857

3.  Site directed mutagenesis of Schizosaccharomyces pombe glutathione synthetase produces an enzyme with homoglutathione synthetase activity.

Authors:  Tamara Dworeck; Martin Zimmermann
Journal:  PLoS One       Date:  2012-10-16       Impact factor: 3.240

  3 in total

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