Yeast Squalene Synthase: Expression, Purification, and Characterization of Soluble Recombinant Enzyme
Abstract
Squalene synthase is the first pathway-specific enzyme in the cholesterol biosynthetic pathway. The gene (ERG9) encoding squalene synthase in Saccharomyces cerevisiae has been isolated and characterized (S. M. Jennings, Y. H. Tsay, T. M. Fisch, and G. W. Robinson, 1991, Proc. Natl. Acad. Sci. USA 88, 6038-6042: M. Fegueur, L. Richard, A. D. Charles, F. Karst, 1991, Curr. Genet. 20, 365-372). The structural gene for the enzyme was modified by the polymerase chain reaction to remove a hydrophobic C-terminal domain, and the open reading frame for the truncated protein was cloned into yeast and Escherichia coli expression vectors. In E. coli, overexpressed truncated squalene synthase was soluble and constituted 2-5% of total cellular protein. The recombinant enzyme was purified to > 95% homogeneity in two steps by chromatography on hydroxyapatite and phenyl-Superose. Soluble truncated squalene synthase is monomeric and catalyzes the two-step conversion of farnesyl diphosphate (FPP) to squalene via presqualene diphosphate in the presence of Mg2+ and NADPH. The concentration of FPP needed for half-maximal activity was 40 microM. At higher concentrations, FPP was an inhibitor. The activity of squalene synthase was stimulated by detergents and reached a maximal value of kcat = 3.3 s-1 at 100 microM FPP in the presence of 1% (v/v) Tween 80.
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A kcat of 3.3 s-1 has been reported for a soluble recombinant yeast SQS enzyme.
“a kcat = 3.3 sec-1 has been reported for a soluble recombinant yeast enzyme [47]”
From Relative expression of genes of terpene metabolism in different tissues of Artemisia annuaL (2011) · cites this paper as [47]
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“Squalene synthase has been characterized previously from human [43], rodents [44, 45], plants [46–48], protozoa [49] and fungi [50].”
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BackgroundBioorganic Chemistry. A Natural Reunion of the Physical and Life Sciences
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“2 reported for the yeast enzyme (Zhang et al., 1993).”
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Hage‐Hülsmann, J., Metzger, S. U., Wewer, V., Buechel, F., Troost, K., Thies, S., Loeschcke, A., Jaeger, K., & Drepper, T. (2019) · Journal of Biotechnology · doi:10.1016/j.btecx.2020.100014 · Cited by 11 · see citing works
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“Gene constructs consisted of a truncated form of the yeast squalene synthase (ySQS) gene (ERG9, GenBank accession NM 001179321) (Zhang et al. , 1993), fused squalene synthase-like genes 1 and 3 (SSL1-3) (HQ585058, HQ585060) from Botryococcus braunii creating a chimeric botryococcene synthase,…”
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“…and C-terminally truncated enzymes can be expressed as soluble form as detected by the activity in the supernatant of the cell extract (Jennings et al. 1991; Zhang et al. 1993), while the tobacco SQS can only be expressed as active form if the C-terminus is deleted (Devarenne et al. 1998).”
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Rehm, H. (2001) · Biotechnology Set · doi:10.1002/9783527620999.ch20k
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Rehm, H. (2001) · Biotechnology · doi:10.1002/9783527620937.ch20
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Terpenoid balance in Aspergillus nidulans unveiled by heterologous squalene synthase expressionPreprint
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Rational membrane engineering for development of industrial platform biocatalysts
Chavez-Santoscoy, M. I. (2021) · doi:10.31274/td-20240329-622
- Authors
- Zhang, D. L., Jennings, S. M., Robinson, G. W., & Poulter, C. D.
- Affiliations
- University of Utah (US)
- ORCID
- Poulter, C.D
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1993-07
- Volume
- 304
- Issue
- 1
- Pages
- 133-143
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2053865525
- Cited by
- 77
- References
- 0
- Citations by year
- 2024: 3 · 2022: 3 · 2021: 6 · 2020: 1 · 2019: 1 · 2018: 4 · 2017: 3 · 2016: 2 · 2015: 5 · 2014: 5 · 2013: 4 · 2012: 3
- FWCI
- 1.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM 21328)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- squalene synthase, Saccharomyces cerevisiae, cholesterol biosynthesis, farnesyl pyrophosphate, recombinant enzyme expression, truncated protein, enzyme purification, enzyme kinetics
- MeSH terms
- Base Sequence, Cloning, Molecular, Ethylmaleimide, Hydrogen-Ion Concentration, Kinetics, Magnesium, Molecular Sequence Data, Oligodeoxyribonucleotides, Recombinant Proteins, Saccharomyces cerevisiae, Solubility, Farnesyl-Diphosphate Farnesyltransferase, Substrate Specificity, Sequence Deletion
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