LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Family |
| Description | Several enzymes catalyse mechanistically related reactions which involve the highly complex cyclic rearrangement of squalene or its 2,3 oxide. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyse a cationic cyclisation cascade converting linear triterpenes to fused ring compounds [ , ]. Lanosterol synthase () (oxidosqualene-lanosterol cyclase) catalyses the cyclisation 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 ( ) (2,3-epoxysqualene-cycloartenol cyclase), is a plant enzyme that catalyses the cyclization of (S)-2,3-epoxysqualene to cycloartenol [ ], and hopene synthase () (squalene-hopene cyclase), is a bacterial enzyme that catalyses the cyclisation of squalene into hopene or diplopterol, a key step in hopanoid (triterpenoid) metabolism [ , ] also found in Aspergillus fumigatus as part of the gene cluster that mediates the biosynthesis fumihopaside A []. These enzymes are evolutionary related [] proteins of about 70 to 85kDa and have an alpha 6 - alpha 6 barrel fold. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY []. Both enzymes have a second minor domain, which forms an α-α barrel that is inserted into the major domain. |
| Short Name | Squalene_cyclase |
