Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae.

Shi, Zheng Zheng; Buntel, Christopher J.; Griffin, John H.

doi:10.1073/pnas.91.15.7370

Cited by 102 publications

(56 citation statements)

References 41 publications

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“…It was assumed that the aromatic rings of the conserved tryptophan residues of this motif could stabilize the intermediary carbocations (72,102). This would be in agreement with other models of active centers with carbocation intermediates (21,41,88). However, the SHC structure revealed that all QW motifs are located at the C terminus of an exposed ␣-helix, with the eponymous part of the motif (Q-X 3 -G-X-W) generating the loop structure (see Fig.…”

Section: Structure-function Relationships Of Shcsmentioning

confidence: 50%

Squalene-Hopene Cyclases

Siedenburg

Jendrossek

2011

Appl Environ Microbiol

123

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Hopanoids and sterols are members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms. They are biochemically synthesized from linear precursors (squalene, 2,3-oxidosqualene) in only one enzymatic step that is catalyzed by squalene-hopene cyclase (SHC) or oxidosqualene cyclase (OSC). SHCs and OSCs are related in amino acid sequences and probably are derived from a common ancestor. The SHC reaction requires the formation of five ring structures, 13 covalent bonds, and nine stereo centers and therefore is one of the most complex one-step enzymatic reactions. We summarize the knowledge of the properties of triterpene cyclases and details of the reaction mechanism of Alicyclobacillus acidocaldarius SHC. Properties of other SHCs are included.

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Section: Structure-function Relationships Of Shcsmentioning

confidence: 50%

Squalene-Hopene Cyclases

Siedenburg

Jendrossek

2011

Appl Environ Microbiol

123

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“…2,3-Oxidosqualene cyclase or lanosterol synthase, the product of the ERG7 gene, performs several ring closures and bond cleavages in this very complex reaction. 50 The ERG7 gene from yeast has been cloned by two laboratories 50,237 which should allow for characterization of this gene and the encoded enzyme. The pathway has now reached the point where a sterol molecule is present and the question to be asked from here to the end of the pathway is whether the intermediate produced at each step is able to meet both the bulk and sparking requirements and thus permit growth.…”

Section: Sterol Biosynthesis In Yeast: Farnesyl Pyrophosphate To Ergomentioning

confidence: 99%

Biochemistry, cell biology and molecular biology of lipids ofSaccharomyces cerevisiae

Daum

Lees

Bard

et al. 1998

Yeast

579

380

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The yeast Saccharomyces cerevisiae is a powerful experimental system to study biochemical, cell biological and molecular biological aspects of lipid synthesis. Most but not all genes encoding enzymes involved in fatty acid, phospholipid, sterol or sphingolipid biosynthesis of this unicellular eukaryote have been cloned, and many gene products have been functionally characterized. Less information is available about genes and gene products governing the transport of lipids between organelles and within membranes, turnover and degradation of complex lipids, regulation of lipid biosynthesis, and linkage of lipid metabolism to other cellular processes. Here we summarize current knowledge about lipid biosynthetic pathways in S. cerevisiae and describe the characteristic features of the gene products involved. We focus on recent discoveries in these fields and address questions on the regulation of lipid synthesis, subcellular localization of lipid biosynthetic steps, cross‐talk between organelles during lipid synthesis and subcellular distribution of lipids. Finally, we discuss distinct functions of certain key lipids and their possible roles in cellular processes. © 1998 John Wiley & Sons, Ltd.

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“…According to the PEPPLOT program (36), a typical QW motif contains part of a (3-strand at the N terminus and a turn at the C terminus. We (37) and others (16) have postulated that the aromatic amino acids of the QW motif might play a structural or functional role in catalysis by stabilizing the carbocationic intermediates through cation-I interactions.…”

mentioning

confidence: 99%

“…Recently, two OSC enzymes have been cloned and sequenced from the fungi Saccharomyces cerevisiae (15,16) and Candida albicans (17)(18)(19)). An oxidosqualene cycloartenol-cyclase was cloned and sequenced from the plantArabidopsis thaliana (20).…”

mentioning

confidence: 99%

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Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA.

Abe

Prestwich

1995

Proc. Natl. Acad. Sci. U.S.A.

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A cDNA encoding rat oxidosqualene lanosterol-cyclase [lanosterol synthase; (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol- Oxidosqualene lanosterol-cyclase (OSC) [lanosterol synthase; (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol-forming), EC 5.4.99.7] catalyzes the conversion of (3S)-2,3-oxidosqualene to lanosterol, forming a total of six new carbon-carbon bonds in a single reaction (1). The regulation of OSC levels in vivo has clinical importance and has been a potential target for the design of hypercholesteremic drugs (2). The formation of lanosterol is initiated in the chair-boat-chair-like conformation of oxidosqualene, and the proton-initiated cyclization is postulated to proceed through a series of rigidly held carbocationic intermediates (1). The intermediate C-20 protosterol cation then undergoes backbone rearrangement to yield the lanosterol skeleton ( Fig. 1) (3-6). Oxidosqualene is also the precursor for a variety of other polycyclic triterpenes, and the relationship between enzyme structure and cyclization mechanism has been extensively studied (1).Several OSCs have been purified to homogeneity from vertebrate (7-9), plant (10-13), and yeast sources (14). Re

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Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae.

Abstract: TheERG7geneencodingoxidosqualene-lans-

Cited by 102 publications

References 41 publications

Squalene-Hopene Cyclases

Squalene-Hopene Cyclases

Biochemistry, cell biology and molecular biology of lipids ofSaccharomyces cerevisiae

Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA.

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