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Aspects related to mevalonate biosynthesis in plants

  • Plant and Fungal Sterols: Biosynthesis, Metabolism and Function Papers Presented at a Symposium Held at the AOCS Annual Meeting. Baltimore, MD, April 1990
  • Article
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Lipids

Abstract

We purified and characterized a membrane-associated enzyme system from radish (Raphanus sativus L.) that is capable of converting acetyl-CoA into 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA). The enzyme system apparently comprises acetoacetyl-CoA thiolase (EC 2.3.1.9) and HMG-CoA synthase (EC 4.1.3.5). Its activityin vitro can be strongly stimulated by FeII. When ferrous ions are applied chelated with ethylenediaminetetraacetate, citrate or adenosine 5′-triphosphate (ATP), the stimulation is further increased. Stimulation is due to a higher catalytic efficiency as indicated by an increase in Vmax, whereas the affinity of the enzyme towards acetyl-CoA remains constant (Km=6 μM). A considerable portion of HMG-CoA lyase activity is associated with the same membranes. HMG-CoA lyase (EC 4.1.3.4) is also solubilized and partially co-purified. Its activity requires comparatively high concentrations of Mg2+. The conversion of HMG-CoA to mevalonic acid is catalyzed by HMG-CoA reductase (EC 1.1.1.34) that is associated with the same membranes. By cDNA encoding theArabidopsis HMG-CoA reductase, we isolated a corresponding gene from a cDNA library newly established from etiolated radish seedlings. This full-length cDNA, referred to as λcRS3, encodes a polypeptide of 583 amino acids with a molecular mass of about 63 kDa. The hydropathy profile suggests the presence of two hydrophobic membrane-spanning domains within the N-terminal 165 amino acids. The carboxy-terminal part, where the catalytic site resides, is highly conserved in all eukaryotic HMG-CoA reductase genes sequenced so far.

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Abbreviations

AACT:

acetoacetyl-CoA thiolase

ATP:

adenosine 5-triphosphate

Brij W-1:

polyoxyethylene ether Brij W-1

CoA:

coenzyme A

DTE:

dithioerythritol

EDTA:

ethylenediaminetetraacetate

FPLC:

fast-performance liquid chromatography

HMG-CoA:

3-hydroxy-3-methylglutaryl-coenzyme A

HMGL:

HMG-CoA lyase

HMGR:

HMG-CoA reductase

HMGS:

HMG-CoA synthase

HPLC:

high-performance liquid chromatography

MVA:

mevalonic acid

PAGE:

polyacrylamide gel electrophoresis

SDS:

sodium dodecylsulfate

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Authors and Affiliations

  1. Botanisches Institut (Pflanzenphysiologie und Pflanzenbiochemie), Universität Karisruhe, Kaiserstrasse 12, D-7500, Karlsruhe 1, Germany

    Thomas J. Bach, Thomas Weber & Annette Wettstein

  2. Facultat de Famàcia, Unitat de Bioquimica, Universitat de Barcelona, E-08028, Barcelona, Spain

    Albert Boronat, Carmé Caelles & Albert Ferrer

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  1. Thomas J. Bach
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  2. Albert Boronat
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  3. Carmé Caelles
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  4. Albert Ferrer
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  5. Thomas Weber
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  6. Annette Wettstein
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Bach, T.J., Boronat, A., Caelles, C. et al. Aspects related to mevalonate biosynthesis in plants. Lipids 26, 637–648 (1991). https://doi.org/10.1007/BF02536429

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