Biochemistry of the Mevalonic Acid Pathway to Terpenoids 1990
DOI: 10.1007/978-1-4684-8789-3_1
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Some Properties of Enzymes Involved in the Biosynthesis and Metabolism of 3-Hydroxy-3-Methylglutaryl-CoA in Plants

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Cited by 36 publications
(41 citation statements)
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“…Both intermediates are products of pyruvate decarboxylase-dehydrogenase reactions. This system appears to differ from the acetoacetyl-CoA synthase/3-hydroxy-3-methylglutaryl-CoA synthase complex described for the ER and/or mitochondrion by Bach et al (3).…”
contrasting
confidence: 59%
See 1 more Smart Citation
“…Both intermediates are products of pyruvate decarboxylase-dehydrogenase reactions. This system appears to differ from the acetoacetyl-CoA synthase/3-hydroxy-3-methylglutaryl-CoA synthase complex described for the ER and/or mitochondrion by Bach et al (3).…”
contrasting
confidence: 59%
“…The metabolically autonomic system of the developing chloroplast with prokaryotic organization is evidently capable of synthesizing the introductory intermediate of isoprenoid synthesis, presumably acetoacetylCoA, starting from two different C2-compounds. This reaction seems to differ from most eukaryotic systems known so far (3,4).…”
Section: -14c]dl-mevalonate In Light By Different Regions Of Leavesmentioning
confidence: 65%
“…They were also confirmed by incorporation of 13 C-labeled glucose into isoprenoids from bacteria utilizing glucose via the Embden-Meyerhof-Parnas pathway and by studies in other isoprenoid series such as the ubiquitous ubiquinones and menaquinones [16]. Incorporation of doubly labeled [4,[5][6][7][8][9][10][11][12][13] C 2 ]glucose into the hopanoids and ubiquinone of Methylobacterium fujisawaense and of uniformly labeled [U- 13 C 6 ]glucose into the hopanoids from Z. mobilis afforded a definitive proof for the formation of the isoprene units via a C 2 and a C 3 subunit and shed light on a rearrangement reaction allowing the insertion of the C 2 subunit derived from pyruvate 11 between two carbon atoms from the triose phosphate-derived C 3 subunit [16,17]. This triose phosphate was identified as glyceraldehyde phosphate 10 by feeding E. coli mutants lacking each enzymes of the triose phosphate metabolism with either 13 C-labeled glycerol in the presence of unlabeled pyruvate, or 13 C-labeled pyruvate in the presence of unlabeled glycerol [17].…”
Section: © 2003 Iupac Pure and Applied Chemistry 75 375-387mentioning
confidence: 92%
“…Mev (6a-methylcompactin), also referred to as lovastatin, competitively inhibits the binding of the HMG-CoA substrate to the active site of the HMGR enzyme and consequently, blocks the synthesis of cytosolic IPP (Bach and Lichtenthaler, 1982) and phytosterol biosynthesis (Bach and Lichtenthaler, 1987;Bach et al, 1990). Mev treatment for 1 d in 4-week-old adventitious roots significantly decreased the total contents of major ginsenosides by about 34% compared with the control plants ( Fig.…”
Section: Activity Of Hmgr Is Positively Correlated With Ginsenoside Pmentioning
confidence: 99%