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Information on EC 3.2.1.104 - steryl-beta-glucosidase
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3.2.1.104 steryl-beta-glucosidaseIUBMB Comments
Acts on glucosides of cholesterol and sitosterol, but not on some related sterols such as coprostanol.
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The enzyme appears in viruses and cellular organisms
Synonyms
EGCrP2, Egh1, endoglycoceramidase-related protein 2, ergosteryl-beta-glucosidase, glucosidase, hydroxy steroid beta-, SG hydrolase, steryl beta-D-glucoside hydrolase, steryl glucoside hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EGCrP2
Egh1
endoglycoceramidase-related protein 2
ergosteryl-beta-glucosidase
glucosidase, hydroxy steroid beta-
-
-
-
-
steryl beta-D-glucoside hydrolase
-
-
-
-
steryl glucoside hydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cholesteryl-beta-D-glucoside + H2O = D-glucose + cholesterol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
cholesteryl-beta-D-glucoside glucohydrolase
Acts on glucosides of cholesterol and sitosterol, but not on some related sterols such as coprostanol.
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CAS REGISTRY NUMBER
COMMENTARY
69494-88-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide + H2O
D-glucose + 6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanol
cholesteryl 3-O-beta-glucoside + H2O
D-glucose + cholesterol
-
-
-
?
ergosteryl 3-O-beta-glucoside + H2O
D-glucose + erosterol
-
-
-
?
indoxyl beta-D-glucoside + H2O
D-glucose + indoxyl
-
-
-
?
n-octyl beta-D-glucoside + H2O
D-glucose + n-octanol
-
-
-
?
resorufin 3-O-beta-D-glucoside + H2O
D-glucose + resorufin
-
-
-
?
sitosteryl 3-O-beta-D-glucoside + H2O
D-glucose + sitosterol
-
-
-
?
sitosteryl 3-O-beta-glucoside + H2O
D-glucose + sitosterol
-
-
-
?
(6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide + H2O
D-glucose + 6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanol
-
-
-
?
(6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide + H2O
D-glucose + 6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanol
Cryptococcus neoformans ATCC 208821
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
D-glucose + 4-methylumbelliferone
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
D-glucose + 4-methylumbelliferone
Cryptococcus neoformans ATCC 208821
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
D-glucose + 4-methylumbelliferone
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
D-glucose + 4-methylumbelliferone
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
D-glucose + 4-nitrophenol
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
D-glucose + 4-nitrophenol
Cryptococcus neoformans ATCC 208821
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
D-glucose + 4-nitrophenol
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
D-glucose + 4-nitrophenol
-
-
-
?
cholesteryl 3-O-beta-D-glucoside + H2O
D-glucose + cholesterol
-
-
-
?
cholesteryl 3-O-beta-D-glucoside + H2O
D-glucose + cholesterol
-
-
-
?
ergosteryl 3-O-beta-D-glucoside + H2O
D-glucose + ergosterol
-
-
-
?
ergosteryl 3-O-beta-D-glucoside + H2O
D-glucose + ergosterol
-
-
-
?
glucosylceramide + H2O
D-glucose + ceramide
-
-
-
?
additional information
?
-
no activity with alpha-glucosides or beta-galactosides, under acidic conditions
-
-
?
additional information
?
-
-
no activity with alpha-glucosides or beta-galactosides, under acidic conditions
-
-
?
additional information
?
-
Cryptococcus neoformans ATCC 208821
no activity with alpha-glucosides or beta-galactosides, under acidic conditions
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
39% inhibition at a concentration of 50%, hydrolysis of p-nitrophenyl beta-D-glucoside
gluconolactone
-
50% inhibition at 4 mM, hydrolysis of cholesteryl beta-D-glucoside. 50% inhibition at 2 mM, hydrolysis of p-nitrophenyl beta-D-glucoside
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
45% stimulation at 0.1 mM, hydrolysis of cholesteryl beta-D-glucoside. No effect on hydrolysis of p-nitrophenyl beta-D-glucoside
ethanol
-
64% stimulation at a concentration of 20%, hydrolysis of cholesteryl beta-D-glucoside. 65% stimulation at a concentration of 20%, hydrolysis of p-nitrophenyl beta-D-glucoside
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0384
(6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide
pH 6.0, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.53
(6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide
pH 6.0, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.8
(6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide
pH 6.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 5.6
-
hydrolysis of cholesteryl beta-D-glucoside or p-nitrophenyl beta-D-glucoside
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
pH 4.0: about % of maximal activity, pH 7.0: about % of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16 - 40
16°C: about 50% of maximal activity, 40°C: about 75% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
changes in activity during germination, distribution between cotyledons and roots
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the intracellular localization is changed depending on the growth phase. Distributed in the cytosol until the initial logarithmic phase (12 h), then delivered to an organelle with a granule structure in the middle logarithmic phase (14 h), and finally localized at the vacuole membranes in the stationary phase (18-20 h)
brenda
-
the intracellular localization is changed depending on the growth phase. Distributed in the cytosol until the initial logarithmic phase (12 h), then delivered to an organelle with a granule structure in the middle logarithmic phase (14 h), and finally localized at the vacuole membranes in the stationary phase (18-20 h)
-
brenda
the intracellular localization is changed depending on the growth phase. Distributed in the cytosol until the initial logarithmic phase (12 h), then delivered to an organelle with a granule structure in the middle logarithmic phase (14 h), and finally localized at the vacuole membranes in the stationary phase (18-20 h)
brenda
-
the intracellular localization is changed depending on the growth phase. Distributed in the cytosol until the initial logarithmic phase (12 h), then delivered to an organelle with a granule structure in the middle logarithmic phase (14 h), and finally localized at the vacuole membranes in the stationary phase (18-20 h)
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
disruption of the EGCrP2 gene (egcrp2) results in the accumulation of ergosteryl 3-O-beta-glucoside, a major sterylglucoside in fungi. Distinct growth arrest, a dysfunction in cell budding, and an abnormal vacuole morphology are detected in the egcrp2-disrupted mutants
malfunction
the disruption of EGH1 in Saccharomyces cerevisiae BY4741 (egh1DELTA) results in the accumulation of ergosteryl 3-O-beta-glucoside and fragmentation of vacuoles
malfunction
Cryptococcus neoformans ATCC 208821
-
disruption of the EGCrP2 gene (egcrp2) results in the accumulation of ergosteryl 3-O-beta-glucoside, a major sterylglucoside in fungi. Distinct growth arrest, a dysfunction in cell budding, and an abnormal vacuole morphology are detected in the egcrp2-disrupted mutants
-
malfunction
-
the disruption of EGH1 in Saccharomyces cerevisiae BY4741 (egh1DELTA) results in the accumulation of ergosteryl 3-O-beta-glucoside and fragmentation of vacuoles
-
physiological function
involved in sterylglucoside catabolism and vacuole formation
physiological function
the enzyme is involved in the catabolism of ergosteryl 3-O-beta-glucoside in the vacuoles of Cryptococcus neoformans
physiological function
Cryptococcus neoformans ATCC 208821
-
the enzyme is involved in the catabolism of ergosteryl 3-O-beta-glucoside in the vacuoles of Cryptococcus neoformans
-
physiological function
-
involved in sterylglucoside catabolism and vacuole formation
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A228BX09_CRYNV
851
0
94743
TrEMBL
-
EGH1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
764
0
86979
Swiss-Prot
-
GLCM_HUMAN
536
0
59716
Swiss-Prot
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
pharmacology
the enzyme may be a promising target for anti-cryptococcal drugs
pharmacology
Cryptococcus neoformans ATCC 208821
-
the enzyme may be a promising target for anti-cryptococcal drugs
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kalinowska, M.; Wojciechowski, Z.A.
Purification and some properties of steryl beta-D-glucoside hydrolase from Sinapis alba seedlings
Phytochemistry
17
1533-1537
1978
Sinapis alba
-
brenda
Kalinowska, M.; Wojciechowski, Z.A.
Modulation of activities of steryl glucoside hydrolase and UDPG:sterol glucosyltransferase from Sinapis alba by detergents and lipids
Phytochemistry
25
45-49
1986
Sinapis alba
-
brenda
Kalinowska, M.; Wojciechowski, Z.A.
Sterol conjugate interconversions during germination of white mustard (Sinapis alba)
Phytochemistry
23
2485-2488
1984
Sinapis alba
-
brenda
Watanabe, T.; Tani, M.; Ishibashi, Y.; Endo, I.; Okino, N.; Ito, M.
Ergosteryl-beta-glucosidase (Egh1) involved in sterylglucoside catabolism and vacuole formation in Saccharomyces cerevisiae
Glycobiology
25
1079-1089
2015
Saccharomyces cerevisiae (P40566), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P40566)
brenda
Watanabe, T.; Ito, T.; Goda, H.; Ishibashi, Y.; Miyamoto, T.; Ikeda, K.; Taguchi, R.; Okino, N.; Ito, M.
Sterylglucoside catabolism in cryptococcus neoformans with endoglycoceramidase-related protein 2 (EGCrP2), the first steryl-beta-glucosidase identified in fungi
J. Biol. Chem.
290
1005-1019
2015
Cryptococcus neoformans (A0A228BX09), Cryptococcus neoformans, Cryptococcus neoformans ATCC 208821 (A0A228BX09)
brenda
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