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Characterization of three chalcone synthase-like genes from apple (Malus x domestica Borkh.)
Year:
2017
Source of publication :
Phytochemistry
Authors :
Ali, Samah
;
.
Davidovich-Rikanati, Rachel
;
.
Eyal, Yoram
;
.
Ibdah, Mwafaq
;
.
Lewinsohn, Efraim
;
.
Shachtier, Alona
;
.
Yahyaa, Mosaab
;
.
Volume :
140
Co-Authors:
Yahyaa, M., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Ali, S., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Davidovich-Rikanati, R., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Ibdah, M., Sakhnin College Academic College for Teacher Education, Sakhnin, Israel
Shachtier, A., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Eyal, Y., Institute of Plant Science, The Volcani Center, ARO, P.O. Box 6, Bet Dagan, Israel
Lewinsohn, E., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Ibdah, M., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Facilitators :
From page:
125
To page:
133
(
Total pages:
9
)
Abstract:
Apple (Malus x domestica Brokh.) is a widely cultivated deciduous tree species of significant economic importance. Apple leaves accumulate high levels of flavonoids and dihydrochalcones, and their formation is dependent on enzymes of the chalcone synthase family. Three CHS genes were cloned from apple leaves and expressed in Escherichia coli. The encoded recombinant enzymes were purified and functionally characterized. In-vitro activity assays indicated that MdCHS1, MdCHS2 and MdCHS3 code for proteins exhibiting polyketide synthase activity that accepted either p-dihydrocoumaroyl-CoA, p-coumaroyl-CoA, or cinnamoyl-CoA as starter CoA substrates in the presence of malonyl-CoA, leading to production of phloretin, naringenin chalcone, and pinocembrin chalcone. MdCHS3 coded a chalcone-dihydrochalcone synthase enzyme with narrower substrate specificity than the previous ones. The apparent Km values of MdCHS3 for p-dihydrocoumaryl-CoA and p-coumaryl-CoA were both 5.0 μM. Expression analyses of MdCHS genes varied according to tissue type. MdCHS1, MdCHS2 and MdCHS3 expression levels were associated with the levels of phloretin accumulate in the respective tissues. © 2017 Elsevier Ltd
Note:
Related Files :
Acyltransferases
Apple
biosynthesis
chalcone derivative
Dihydrochalcone
Genetics
metabolism
Show More
Related Content
More details
DOI :
10.1016/j.phytochem.2017.04.022
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
31497
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:03
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Scientific Publication
Characterization of three chalcone synthase-like genes from apple (Malus x domestica Borkh.)
140
Yahyaa, M., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Ali, S., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Davidovich-Rikanati, R., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Ibdah, M., Sakhnin College Academic College for Teacher Education, Sakhnin, Israel
Shachtier, A., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Eyal, Y., Institute of Plant Science, The Volcani Center, ARO, P.O. Box 6, Bet Dagan, Israel
Lewinsohn, E., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Ibdah, M., Newe Yaar Research Center, Agriculture Research Organization, P.O.Box 1021, Ramat Yishay, Israel
Characterization of three chalcone synthase-like genes from apple (Malus x domestica Borkh.)
Apple (Malus x domestica Brokh.) is a widely cultivated deciduous tree species of significant economic importance. Apple leaves accumulate high levels of flavonoids and dihydrochalcones, and their formation is dependent on enzymes of the chalcone synthase family. Three CHS genes were cloned from apple leaves and expressed in Escherichia coli. The encoded recombinant enzymes were purified and functionally characterized. In-vitro activity assays indicated that MdCHS1, MdCHS2 and MdCHS3 code for proteins exhibiting polyketide synthase activity that accepted either p-dihydrocoumaroyl-CoA, p-coumaroyl-CoA, or cinnamoyl-CoA as starter CoA substrates in the presence of malonyl-CoA, leading to production of phloretin, naringenin chalcone, and pinocembrin chalcone. MdCHS3 coded a chalcone-dihydrochalcone synthase enzyme with narrower substrate specificity than the previous ones. The apparent Km values of MdCHS3 for p-dihydrocoumaryl-CoA and p-coumaryl-CoA were both 5.0 μM. Expression analyses of MdCHS genes varied according to tissue type. MdCHS1, MdCHS2 and MdCHS3 expression levels were associated with the levels of phloretin accumulate in the respective tissues. © 2017 Elsevier Ltd
Scientific Publication
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