2.5.1.21: squalene synthase
This is an abbreviated version!
For detailed information about squalene synthase, go to the full flat file.
Word Map on EC 2.5.1.21
-
2.5.1.21
-
farnesylation
-
cholesterol
-
prenylation
-
sterol
-
ftase
-
mevalonate
-
geranylgeranylation
-
isoprenoids
-
leukemia
-
geranylgeranyltransferase
-
pyrophosphate
-
tipifarnib
-
hmg-coa
-
statin
-
h-ras
-
peptidomimetic
-
epoxidase
-
prenyltransferase
-
dolichols
-
rhob
-
isoprenylation
-
triterpene
-
farnesol
-
3-hydroxy-3-methylglutaryl
-
lamins
-
ergosterol
-
cholesterol-lowering
-
hmgcr
-
prelamin
-
p21ras
-
lovastatin
-
hutchinson-gilford
-
lanosterol
-
manumycin
-
triterpenoids
-
synthesis
-
progerin
-
farnesylpyrophosphate
-
cis-prenyltransferase
-
drug development
-
oxidosqualene
-
ras-transformed
-
medicine
-
ras-dependent
-
nonsterols
-
ras-mediated
-
withanolides
-
srebp-2
-
ganoderic
-
agriculture
-
geranylgeraniol
-
industry
-
cycloartenol
-
non-thiol
-
2,3-oxidosqualene
- 2.5.1.21
-
farnesylation
- cholesterol
-
prenylation
- sterol
- ftase
- mevalonate
-
geranylgeranylation
-
isoprenoids
- leukemia
-
geranylgeranyltransferase
- pyrophosphate
- tipifarnib
- hmg-coa
- statin
- h-ras
-
peptidomimetic
-
epoxidase
- prenyltransferase
- dolichols
- rhob
-
isoprenylation
-
triterpene
- farnesol
-
3-hydroxy-3-methylglutaryl
- lamins
- ergosterol
-
cholesterol-lowering
- hmgcr
-
prelamin
-
p21ras
- lovastatin
-
hutchinson-gilford
- lanosterol
- manumycin
-
triterpenoids
- synthesis
-
progerin
-
farnesylpyrophosphate
- cis-prenyltransferase
- drug development
- oxidosqualene
-
ras-transformed
- medicine
-
ras-dependent
-
nonsterols
-
ras-mediated
-
withanolides
- srebp-2
-
ganoderic
- agriculture
- geranylgeraniol
- industry
- cycloartenol
-
non-thiol
- 2,3-oxidosqualene
Reaction
2 (2E,6E)-farnesyl diphosphate + + = + 2 diphosphate +
Synonyms
BbSS, BSS, CrSQS, dt-ySQase, Erg9, EtSS, farnesyl-diphosphate farnesyltransferase, farnesyl-diphosphate:farnesyldiphosphate farnesyltransferase, farnesyldiphosphate farnesyltransferase 1, farnesyldiphosphate:farnesyldiphosphate farnesyltransferase, farnesyltransferase, FDFT1, hSQS, presqualene synthase, presqualene-diphosphate synthase, SgSQS, SQase, SQS, SQS1, SQS2, squalene synthase, squalene synthase 1, squalene synthase 2, squalene synthetase, SS1, SSase, SSN, synthase, squalene, TkSQS1, TkSQS2
ECTree
Advanced search results
Localization
Localization on EC 2.5.1.21 - squalene synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
combined in silico prediction and subcellular localization, experiments in tobacco indicate that squalene synthase is probably in the cytoplasm or on the cytoskeleton. The squalene synthase protein has two transmembrane regions in the C-terminal
squalene synthase TkSQS1 and squalene epoxidase TkSQE1 proteins colocalize in the endoplasmic reticulum membrane
associated enzyme with C-terminus anchored in the endoplasmic reticulum membrane and the N-terminus including active site is exposed in the cytosol
-
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane
-
CrSQS protein has two putative transmembrane domains at the C-terminus, Phe398-Glu420 and Gln436-Leu458
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain which consists of a hinge region and a membrane spanning helix responsible for tethering the enzyme to the cytosolic face of the endoplasmic reticulum
bound, the membrane-binding domains of the human enzyme are 30 residues of the N-terminus and 47 residues of the C-terminus
-
model of the secondary structure and its possible membrane orientation
the enzyme has two transmembrane domains at its C-terminus