PROSITE documentation PDOC00825Terpene synthases signature
Description
The following enzymes catalyze mechanistically related reactions which involve the highly complex cyclic rearrangement of squalene or its 2,3 oxide:
- Lanosterol synthase (EC 5.4.99.7) (oxidosqualene--lanosterol cyclase), which catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi (gene ERG7).
- Cycloartenol synthase (EC 5.4.99.8) (2,3-epoxysqualene--cycloartenol cyclase), a plant enzyme that catalyzes the cyclization of (S)-2,3- epoxysqualene to cycloartenol.
- Hopene synthase (EC 5.4.99.17) (squalene--hopene cyclase), a bacterial enzyme that catalyzes the cyclization of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism.
These enzymes are evolutionary related [1] proteins of about 70 to 85 Kd. As a signature pattern, we selected a highly conserved region which is rich in aromatic residues and which is located in the C-terminal section.
Last update:December 2004 / Pattern and text revised.
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Reference
1 | Authors | Corey E.J. Matsuda S.P.T. Bartel B. |
Title | Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen. | |
Source | Proc. Natl. Acad. Sci. U.S.A. 90:11628-11632(1993). | |
PubMed ID | 7505443 |
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