Reciprocal mutations of two multifunctional β-amyrin synthases from Barbarea vulgaris shift α/β-amyrin ratios
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Reciprocal mutations of two multifunctional β-amyrin synthases from Barbarea vulgaris shift α/β-amyrin ratios. / Günther, Jan; Erthmann, Pernille Osterbye; Khakimov, Bekzod; Bak, Søren.
I: Plant Physiology, Bind 188, Nr. 3, 2022, s. 1483-1495.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Reciprocal mutations of two multifunctional β-amyrin synthases from Barbarea vulgaris shift α/β-amyrin ratios
AU - Günther, Jan
AU - Erthmann, Pernille Osterbye
AU - Khakimov, Bekzod
AU - Bak, Søren
N1 - Funding Information: We thank the European Community’s Seventh Framework Programme (FP7/2007-2013; grant no. 613692 to TriForC) for supporting this work. We thank Pablo D. Cárdenas and Nils Agerbirk for thorough reading and constructive input during writing of this manuscript. Funding Information: This work was funded by The Danish Council for Independent Research, Technology and Production Sciences (grant no. 1335-00151), the Novo Nordisk Foundation, Distinguished Investigator (grant no. NNF20OC0060298), and Department of Plant and Environmental Sciences, University of Copenhagen (PhD stipend to PØE). Publisher Copyright: © 2022 American Society of Plant Biologists. All rights reserved.
PY - 2022
Y1 - 2022
N2 - In the wild cruciferous wintercress (Barbarea vulgaris), β-amyrin-derived saponins are involved in resistance against insect herbivores like the major agricultural pest diamondback moth (Plutella xylostella). Enzymes belonging to the 2,3-oxidosqualene cyclase family have been identified and characterized in B. vulgaris G-type and P-type plants that differ in their natural habitat, insect resistance and saponin content. Both G-type and P-type plants possess highly similar 2,3-oxidosqualene cyclase enzymes that mainly produce β-amyrin (Barbarea vulgaris Lupeol synthase 5 G-Type; BvLUP5-G) or a-amyrin (Barbarea vulgaris Lupeol synthase 5 P-Type; BvLUP5-P), respectively. Despite the difference in product formation, the two BvLUP5 enzymes are 98% identical at the amino acid level. This provides a unique opportunity to investigate determinants of product formation, using the B. vulgaris 2,3-oxidosqualene cyclase enzymes as a model for studying amino acid residues that determine differences in product formation. In this study, we identified two amino acid residues at position 121 and 735 that are responsible for the dominant changes in generated product ratios of β-amyrin and a-amyrin in both BvLUP5 enzymes. These amino acid residues have not previously been highlighted as directly involved in 2,3-oxidosqualene cyclase product specificity. Our results highlight the functional diversity and promiscuity of 2,3-oxidosqualene cyclase enzymes. These enzymes serve as important mediators of metabolic plasticity throughout plant evolution.
AB - In the wild cruciferous wintercress (Barbarea vulgaris), β-amyrin-derived saponins are involved in resistance against insect herbivores like the major agricultural pest diamondback moth (Plutella xylostella). Enzymes belonging to the 2,3-oxidosqualene cyclase family have been identified and characterized in B. vulgaris G-type and P-type plants that differ in their natural habitat, insect resistance and saponin content. Both G-type and P-type plants possess highly similar 2,3-oxidosqualene cyclase enzymes that mainly produce β-amyrin (Barbarea vulgaris Lupeol synthase 5 G-Type; BvLUP5-G) or a-amyrin (Barbarea vulgaris Lupeol synthase 5 P-Type; BvLUP5-P), respectively. Despite the difference in product formation, the two BvLUP5 enzymes are 98% identical at the amino acid level. This provides a unique opportunity to investigate determinants of product formation, using the B. vulgaris 2,3-oxidosqualene cyclase enzymes as a model for studying amino acid residues that determine differences in product formation. In this study, we identified two amino acid residues at position 121 and 735 that are responsible for the dominant changes in generated product ratios of β-amyrin and a-amyrin in both BvLUP5 enzymes. These amino acid residues have not previously been highlighted as directly involved in 2,3-oxidosqualene cyclase product specificity. Our results highlight the functional diversity and promiscuity of 2,3-oxidosqualene cyclase enzymes. These enzymes serve as important mediators of metabolic plasticity throughout plant evolution.
U2 - 10.1093/plphys/kiab545
DO - 10.1093/plphys/kiab545
M3 - Journal article
C2 - 34865155
AN - SCOPUS:85125882258
VL - 188
SP - 1483
EP - 1495
JO - Plant Physiology
JF - Plant Physiology
SN - 0032-0889
IS - 3
ER -
ID: 300443946