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Information on EC 3.1.1.13 - sterol esterase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q07804

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.13 sterol esterase
IUBMB Comments
A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q07804
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cease, lysosomal acid lipase, cholesterol ester hydrolase, cholesteryl ester hydrolase, pancreatic cholesterol esterase, bile salt-stimulated lipase, cholesteryl esterase, neutral cholesteryl ester hydrolase, nceh1, kiaa1363, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid cholesteryl ester hydrolase
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-
-
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acylcholesterol lipase
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-
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cholesterase
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-
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cholesterol ester hydrolase
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-
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cholesterol ester synthetase
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cholesterol esterase
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cholesteryl ester hydrolase
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-
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cholesteryl ester synthetase
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-
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cholesteryl esterase
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-
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LAL
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sterol ester hydrolase
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Sterol esterase
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sterol-ester acylhydrolase
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triterpenol esterase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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hydrolysis of carboxylic ester
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
steryl-ester acylhydrolase
A group of enzymes of broad specificity, acting on esters of sterols and long-chain fatty acids, that may also bring about the esterification of sterols. Activated by bile salts.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-00-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cholesteryl esters + H2O
cholesterol + fatty acid
show the reaction diagram
-
-
-
?
cholesteryl oleate + H2O
cholesterol + oleic acid
show the reaction diagram
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-
-
ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cholesteryl esters + H2O
cholesterol + fatty acid
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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20% inhibition
Hg2+
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15% inhibition
N-ethylmaleimide
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complete loss of activity
p-mercuribenzoate
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60% inhibition
Triton X-100
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inhibition above 0.1% w/v
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
albumin
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slightly activating
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lysophosphatidylcholine
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phosphatidylcholine
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at pH 6.6
sodium taurocholic acid
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less effective to stimulation than phosphatidylcholine
Triton X-100
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activating by low concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.107 - 0.143
cholesteryl oleate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene products of YLL012/YEH1
Swissprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66510
x * 66510, calculated
62000
-
x * 62000, SDS-PAGE
62450
x * 62450, calculated
62980
x * 62980, calculated
70000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
sequence contains 3 potential N-glycosylation sites
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
700fold by protamine treatment, chromatography techniques to homogeneity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taketani, S.; Nishino, T.; Katsuki, H.
Purification and properties of sterol-ester hydrolase from Saccharomyces cerevisiae
J. Biochem.
89
1667-1673
1981
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mullner, H.; Deutsch, G.; Leitner, E.; Ingolic, E.; Daum, G.
YEH2/YLR020c encodes a novel steryl ester hydrolase of the yeast Saccharomyces cerevisiae
J. Biol. Chem.
280
13321-13328
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Koeffel, R.; Tiwari, R.; Falquet, L.; Schneiter, R.
The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis
Mol. Cell. Biol.
25
1655-1668
2005
Saccharomyces cerevisiae (P34163), Saccharomyces cerevisiae (Q07804), Saccharomyces cerevisiae (Q07950), Saccharomyces cerevisiae
Manually annotated by BRENDA team