Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. L
Our findings reveal that pyruvic acid content is generally higher in Allium fistulosum than in A. cepa. In A. fistulosum, the bulbs contain more pyruvic acid than the leaves, while in A. cepa, the inner bulb layers exhibit higher levels compared to the outer layers. We demonstrate that A. fistulosum...
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Elsevier
2025-06-01
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| Series: | Food Chemistry: Molecular Sciences |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666566225000164 |
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| author | Mingzhao Zhu Huanhuan Xu Zhili Deng Menglu Hou Lecheng Liu Yongqin Wang |
| author_facet | Mingzhao Zhu Huanhuan Xu Zhili Deng Menglu Hou Lecheng Liu Yongqin Wang |
| author_sort | Mingzhao Zhu |
| collection | DOAJ |
| description | Our findings reveal that pyruvic acid content is generally higher in Allium fistulosum than in A. cepa. In A. fistulosum, the bulbs contain more pyruvic acid than the leaves, while in A. cepa, the inner bulb layers exhibit higher levels compared to the outer layers. We demonstrate that A. fistulosum γ-glutamyl transpeptidase 1 (AfGGT1) catalyzes the production of S-1-propenyl-L-cysteine from γ-glutamyl-S-1-propenylcysteine, whereas AfGGT2 and AfGGT3 lack catalytic activity. In natural populations of A. fistulosum, AfGGT1 expression shows a strong positive correlation with pyruvic acid content (R2 = 0.6976). The optimal catalytic conditions for AfGGT1 are pH 7 and 37 °C, with a Km value of 0.2686 mM under these conditions. Molecular docking studies further reveal distinct substrate-binding conformations among AfGGT1, AfGGT2, and AfGGT3, highlighting functional divergence within the enzyme family. |
| format | Article |
| id | doaj-art-c8c0e13a0a274eacb95eaeba9f9551fa |
| institution | DOAJ |
| issn | 2666-5662 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: Molecular Sciences |
| spelling | doaj-art-c8c0e13a0a274eacb95eaeba9f9551fa2025-08-20T02:39:38ZengElsevierFood Chemistry: Molecular Sciences2666-56622025-06-011010025510.1016/j.fochms.2025.100255Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. LMingzhao Zhu0Huanhuan Xu1Zhili Deng2Menglu Hou3Lecheng Liu4Yongqin Wang5State Key Laboratory of Vegetable Biobreeding, National Engineering Research Center for Vegetables, Beijing Key Laboratory of Vegetable Germplasms Improvement, Key Laboratory of Biology and Genetics Improvement of Horticultural Crops (North China), Beijing Vegetable Research Center, Beijing Academy of Agricultural and Forestry Sciences, Beijing 100097, ChinaCollege of Horticulture and Gardening, Yangtze University, Jingzhou 434025, ChinaCollege of Horticulture and Gardening, Yangtze University, Jingzhou 434025, ChinaCollege of Horticulture and Gardening, Yangtze University, Jingzhou 434025, ChinaCollege of Horticulture and Gardening, Yangtze University, Jingzhou 434025, China; Corresponding authors.State Key Laboratory of Vegetable Biobreeding, National Engineering Research Center for Vegetables, Beijing Key Laboratory of Vegetable Germplasms Improvement, Key Laboratory of Biology and Genetics Improvement of Horticultural Crops (North China), Beijing Vegetable Research Center, Beijing Academy of Agricultural and Forestry Sciences, Beijing 100097, China; Corresponding authors.Our findings reveal that pyruvic acid content is generally higher in Allium fistulosum than in A. cepa. In A. fistulosum, the bulbs contain more pyruvic acid than the leaves, while in A. cepa, the inner bulb layers exhibit higher levels compared to the outer layers. We demonstrate that A. fistulosum γ-glutamyl transpeptidase 1 (AfGGT1) catalyzes the production of S-1-propenyl-L-cysteine from γ-glutamyl-S-1-propenylcysteine, whereas AfGGT2 and AfGGT3 lack catalytic activity. In natural populations of A. fistulosum, AfGGT1 expression shows a strong positive correlation with pyruvic acid content (R2 = 0.6976). The optimal catalytic conditions for AfGGT1 are pH 7 and 37 °C, with a Km value of 0.2686 mM under these conditions. Molecular docking studies further reveal distinct substrate-binding conformations among AfGGT1, AfGGT2, and AfGGT3, highlighting functional divergence within the enzyme family.http://www.sciencedirect.com/science/article/pii/S2666566225000164Allium cropsPungencyγ-Glutamyl transpeptidaseCatalysisS-1-propenyl-L-cysteine |
| spellingShingle | Mingzhao Zhu Huanhuan Xu Zhili Deng Menglu Hou Lecheng Liu Yongqin Wang Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. L Food Chemistry: Molecular Sciences Allium crops Pungency γ-Glutamyl transpeptidase Catalysis S-1-propenyl-L-cysteine |
| title | Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. L |
| title_full | Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. L |
| title_fullStr | Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. L |
| title_full_unstemmed | Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. L |
| title_short | Identification of S-1-propenyl-L-cysteine as the catalytic product of AfGGT1 and a key intermediate in isoalliin biosynthesis in Allium fistulosum. L |
| title_sort | identification of s 1 propenyl l cysteine as the catalytic product of afggt1 and a key intermediate in isoalliin biosynthesis in allium fistulosum l |
| topic | Allium crops Pungency γ-Glutamyl transpeptidase Catalysis S-1-propenyl-L-cysteine |
| url | http://www.sciencedirect.com/science/article/pii/S2666566225000164 |
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