Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops

Judith Pfeiffer; Christiane Kühnel; Jeannette Brandt; Daniela Duy; P. A.Nimal Punyasiri; Gert Forkmann; Thilo C. Fischer

doi:10.1016/j.plaphy.2006.06.001

Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops

Judith Pfeiffer
, Christiane Kühnel
, Jeannette Brandt
, Daniela Duy
, P. A.Nimal Punyasiri
, Gert Forkmann
, Thilo C. Fischer

Life Sciences

Technical University of Munich
Tea Research Institute of Sri Lanka

Research output: Contribution to journal › Article › peer-review

87 Scopus citations

Abstract

Catechin and epicatechin biosyntheses were studied of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crop leaves, since these monomers and the derived proanthocyanidins are important disease resistance factors. Grape and apple leucoanthocyanidin 4-reductase (LAR; EC 1.17.1.3) enzymes were characterized on basis of plant and recombinant enzymes. In case of grape, two LAR cDNAs were cloned by assembling available EST sequences. Grape and apple leaf anthocyanidin reductase (ANR; EC 1.3.1.77) cDNAs were also obtained and the respective plant and recombinant enzymes were characterized. Despite general low substrate specificity, within the respective flavonoid biosyntheses of grape and apple leaves, both enzyme types deliver differently hydroxylated catechins and epicatechins, due to substrate availability in vivo. Furthermore, for LAR enzymes conversion of 3-deoxyleucocyanidin was shown. Beside relevance for plant protection, this restricts the number of possible reaction mechanisms of LAR. ANR enzyme activity was demonstrated for a number of other crop plants and its correlation with (-)-epicatechin and obvious competition with UDP-glycosyl:flavonoid-3-O-glycosyltransferases was considered.

Original language	English
Pages (from-to)	323-334
Number of pages	12
Journal	Plant Physiology and Biochemistry
Volume	44
Issue number	5-6
DOIs	https://doi.org/10.1016/j.plaphy.2006.06.001
State	Published - May 2006

Keywords

Apple
Catechin biosynthesis
Epicatechin biosynthesis
Flavonoids
Grape
Plant resistance
Proanthocyanidins

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10.1016/j.plaphy.2006.06.001

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Pfeiffer, J., Kühnel, C., Brandt, J., Duy, D., Punyasiri, P. A. N., Forkmann, G., & Fischer, T. C. (2006). Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops. Plant Physiology and Biochemistry, 44(5-6), 323-334. https://doi.org/10.1016/j.plaphy.2006.06.001

@article{04cf8b67683245eca995297029f58f1d,

title = "Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops",

abstract = "Catechin and epicatechin biosyntheses were studied of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crop leaves, since these monomers and the derived proanthocyanidins are important disease resistance factors. Grape and apple leucoanthocyanidin 4-reductase (LAR; EC 1.17.1.3) enzymes were characterized on basis of plant and recombinant enzymes. In case of grape, two LAR cDNAs were cloned by assembling available EST sequences. Grape and apple leaf anthocyanidin reductase (ANR; EC 1.3.1.77) cDNAs were also obtained and the respective plant and recombinant enzymes were characterized. Despite general low substrate specificity, within the respective flavonoid biosyntheses of grape and apple leaves, both enzyme types deliver differently hydroxylated catechins and epicatechins, due to substrate availability in vivo. Furthermore, for LAR enzymes conversion of 3-deoxyleucocyanidin was shown. Beside relevance for plant protection, this restricts the number of possible reaction mechanisms of LAR. ANR enzyme activity was demonstrated for a number of other crop plants and its correlation with (-)-epicatechin and obvious competition with UDP-glycosyl:flavonoid-3-O-glycosyltransferases was considered.",

keywords = "Apple, Catechin biosynthesis, Epicatechin biosynthesis, Flavonoids, Grape, Plant resistance, Proanthocyanidins",

author = "Judith Pfeiffer and Christiane K{\"u}hnel and Jeannette Brandt and Daniela Duy and Punyasiri, \{P. A.Nimal\} and Gert Forkmann and Fischer, \{Thilo C.\}",

note = "Funding Information: The “Bayerisches Staatsministerium f{\"u}r Landesentwicklung und Umweltfragen” is acknowledged for the financial support of the project “Induzierte Pathogenabwehr”, the Department of Research Cooperation (SAREC) of the Swedish International Development Cooperation, Sida, for financial support through Biochemical Pest Control Project for P.A.N. Punyasiri to carry out work at the Technical University of Munich, Germany. Dr. Thorsten Strissel and Professor Dr. Dieter Treutter (Fruit Science, Technical University Munich) are acknowledged for help with HPLC analyses performed in their lab, Professor Dr. Iris Szankowski (Vegetable and Fruit Science, University of Hannover) and Dr. Henryk Flachowsky (Federal Centre for Breeding Research on Cultivated Plants (BAZ), Dresden/Pillnitz) for providing us with frozen apple leaf material of various cultivars. Bettina Deiml is thanked for manifold support. Dr. Christian Seitz (Floriculture, TU Munich) is acknowledged for providing a flavonoid-3′5′-hydroxylase expression clone for substrate synthesis. We are grateful to Dr. Henriette A. Remmer (University of Michigan) and Dr. Uta von Rad (BIOP, Neuherberg) for proofreading the manuscript.",

year = "2006",

month = may,

doi = "10.1016/j.plaphy.2006.06.001",

language = "English",

volume = "44",

pages = "323--334",

journal = "Plant Physiology and Biochemistry",

issn = "0981-9428",

publisher = "Elsevier Masson s.r.l.",

number = "5-6",

}

Pfeiffer, J, Kühnel, C, Brandt, J, Duy, D, Punyasiri, PAN, Forkmann, G & Fischer, TC 2006, 'Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops', Plant Physiology and Biochemistry, vol. 44, no. 5-6, pp. 323-334. https://doi.org/10.1016/j.plaphy.2006.06.001

Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops. / Pfeiffer, Judith; Kühnel, Christiane; Brandt, Jeannette et al.
In: Plant Physiology and Biochemistry, Vol. 44, No. 5-6, 05.2006, p. 323-334.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops

AU - Pfeiffer, Judith

AU - Kühnel, Christiane

AU - Brandt, Jeannette

AU - Duy, Daniela

AU - Punyasiri, P. A.Nimal

AU - Forkmann, Gert

AU - Fischer, Thilo C.

N1 - Funding Information: The “Bayerisches Staatsministerium für Landesentwicklung und Umweltfragen” is acknowledged for the financial support of the project “Induzierte Pathogenabwehr”, the Department of Research Cooperation (SAREC) of the Swedish International Development Cooperation, Sida, for financial support through Biochemical Pest Control Project for P.A.N. Punyasiri to carry out work at the Technical University of Munich, Germany. Dr. Thorsten Strissel and Professor Dr. Dieter Treutter (Fruit Science, Technical University Munich) are acknowledged for help with HPLC analyses performed in their lab, Professor Dr. Iris Szankowski (Vegetable and Fruit Science, University of Hannover) and Dr. Henryk Flachowsky (Federal Centre for Breeding Research on Cultivated Plants (BAZ), Dresden/Pillnitz) for providing us with frozen apple leaf material of various cultivars. Bettina Deiml is thanked for manifold support. Dr. Christian Seitz (Floriculture, TU Munich) is acknowledged for providing a flavonoid-3′5′-hydroxylase expression clone for substrate synthesis. We are grateful to Dr. Henriette A. Remmer (University of Michigan) and Dr. Uta von Rad (BIOP, Neuherberg) for proofreading the manuscript.

PY - 2006/5

Y1 - 2006/5

N2 - Catechin and epicatechin biosyntheses were studied of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crop leaves, since these monomers and the derived proanthocyanidins are important disease resistance factors. Grape and apple leucoanthocyanidin 4-reductase (LAR; EC 1.17.1.3) enzymes were characterized on basis of plant and recombinant enzymes. In case of grape, two LAR cDNAs were cloned by assembling available EST sequences. Grape and apple leaf anthocyanidin reductase (ANR; EC 1.3.1.77) cDNAs were also obtained and the respective plant and recombinant enzymes were characterized. Despite general low substrate specificity, within the respective flavonoid biosyntheses of grape and apple leaves, both enzyme types deliver differently hydroxylated catechins and epicatechins, due to substrate availability in vivo. Furthermore, for LAR enzymes conversion of 3-deoxyleucocyanidin was shown. Beside relevance for plant protection, this restricts the number of possible reaction mechanisms of LAR. ANR enzyme activity was demonstrated for a number of other crop plants and its correlation with (-)-epicatechin and obvious competition with UDP-glycosyl:flavonoid-3-O-glycosyltransferases was considered.

AB - Catechin and epicatechin biosyntheses were studied of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crop leaves, since these monomers and the derived proanthocyanidins are important disease resistance factors. Grape and apple leucoanthocyanidin 4-reductase (LAR; EC 1.17.1.3) enzymes were characterized on basis of plant and recombinant enzymes. In case of grape, two LAR cDNAs were cloned by assembling available EST sequences. Grape and apple leaf anthocyanidin reductase (ANR; EC 1.3.1.77) cDNAs were also obtained and the respective plant and recombinant enzymes were characterized. Despite general low substrate specificity, within the respective flavonoid biosyntheses of grape and apple leaves, both enzyme types deliver differently hydroxylated catechins and epicatechins, due to substrate availability in vivo. Furthermore, for LAR enzymes conversion of 3-deoxyleucocyanidin was shown. Beside relevance for plant protection, this restricts the number of possible reaction mechanisms of LAR. ANR enzyme activity was demonstrated for a number of other crop plants and its correlation with (-)-epicatechin and obvious competition with UDP-glycosyl:flavonoid-3-O-glycosyltransferases was considered.

KW - Apple

KW - Catechin biosynthesis

KW - Epicatechin biosynthesis

KW - Flavonoids

KW - Grape

KW - Plant resistance

KW - Proanthocyanidins

UR - https://www.scopus.com/pages/publications/33748060964

U2 - 10.1016/j.plaphy.2006.06.001

DO - 10.1016/j.plaphy.2006.06.001

M3 - Article

C2 - 16806954

AN - SCOPUS:33748060964

SN - 0981-9428

VL - 44

SP - 323

EP - 334

JO - Plant Physiology and Biochemistry

JF - Plant Physiology and Biochemistry

IS - 5-6

ER -

Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops

Abstract

Keywords

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