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Background  Durian ( Durio zibethinus  L.) is a highly popular fruit in Thailand and several other Southeast Asian countries. It is abundant in essential nutrients and sulphur-containing compounds such as glutathione (GSH) and γ-glutamylcysteine (γ-EC). Cysteinylglycine (Cys-Gly) is produced by GSH catabolism and occurs in durian fruit pulp. Cysteine (Cys) is a precursor of sulphur-containing volatiles generated during fruit ripening. The aforementioned substances contribute to the strong odour and flavour of the ripe fruit. However, the genes encoding plant Cys-Gly dipeptidases are unknown. The aim of this study was to measure leucylaminopeptidase (LAP) activity in durian fruit pulp.    Results  We identified DzLAP1 and DzLAP2, which the former was highly expressed in the fruit pulp.  DzLAP1  was expressed at various ripening stages and in response to ethephon/1-MCP treatment. Hence,  DzLAP1  is active at the early stages of fruit ripening. DzLAP1 is a metalloenzyme ~ 63 kDa in size. It is activated by Mg 2+  or Mn 2+  and, like other LAPs, its optimal alkaline pH is 9.5. Kinetic studies revealed that DzLAP1 has K m  = 1.62 mM for its preferred substrate Cys-Gly. DzLAP1-GFP was localised to the cytosol and targeted the plastids.  In planta  Cys-Gly hydrolysis was confirmed for  Nicotiana benthamiana  leaves co-infiltrated with Cys-Gly and expressing  DzLAP1 .    Conclusions  DzLAP1 has Cys-Gly dipeptidase activity in the γ-glutamyl cycle. The present study revealed that the LAPs account for the high sulphur-containing compound levels identified in fully ripened durian fruit pulp.    Supplementary Information  The online version contains supplementary material available at 10.1186/s12870-021-02845-6.

bmc plant biology

Fruit ripening-associated leucylaminopeptidase with cysteinylglycine dipeptidase activity from durian suggests its involvement in glutathione recycling