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Information on EC 3.2.1.58 - glucan 1,3-beta-glucosidase and Organism(s) Candida albicans and UniProt Accession P29717
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3.2.1.58 glucan 1,3-beta-glucosidaseIUBMB Comments
Acts on oligosaccharides, but very slowly on laminaribiose.
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The taxonomic range for the selected organisms is: Candida albicans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
panomycocin, exo-1,3-beta-glucanase, glucan 1,3-beta-glucosidase, exo-beta-glucanase, exo-1,3-beta-d-glucanase, bgn3.2, beta-1,3-exoglucanase, beta-(1,3)-glucanase, bgn3.4, lam55a, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,3-beta-D-glucanohydrolase
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-
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beta-1,3-glucan exo-hydrolase
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-
-
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exo (13)-beta-glucanase
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-
-
-
exo-1,3-beta-D-glucanase
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-
-
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exo-1,3-beta-glucanase
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-
-
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Exo-1,3-beta-glucanase I/II
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-
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exo-1,3-beta-glucosidase
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-
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Exo-beta 1,3 glucanase
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-
-
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exo-beta-(13)-D-glucanase
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exo-beta-(13)-glucanohydrolase
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-
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exo-beta-1,3-D-glucanase
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exo-beta-1,3-glucanase
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GP29
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-
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-
additional information
the enzyme belongs to the glycosyl hydrolase family 5, GH5
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3-beta-D-glucan glucohydrolase
Acts on oligosaccharides, but very slowly on laminaribiose.
CAS REGISTRY NUMBER
COMMENTARY
9073-49-8
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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
laminarin + H2O
D-glucose + laminaribiose + gentiobiose + oligosaccharides + laminaritriose
4-methyl-umbelliferyl-beta-D-glucoside
4-methylumbelliferone + D-glucose
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-
-
?
4-methyl-umbelliferyl-beta-D-glucoside
4-methylumbelliferone + D-glucose
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-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + gentiobiose + oligosaccharides + laminaritriose
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-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + gentiobiose + oligosaccharides + laminaritriose
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-
different combinations and amounts of following products: D-glucose (main product), laminaribiose, gentiobiose, oligosaccharides, laminaritriose
?
additional information
?
-
two surface loops, amino acids 36-47 and 101-106, might play a functional role after substrate binding. The loops could bind the enzyme to a glucan chain in the cell wall. Molecular dynamics and modelling of enzyme-substrate complexes, overview
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-
?
additional information
?
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requirement for double-sided CH/pi interactions at the +1 subsite, and necessity for phenylalanine rather than tyrosine or tryptophan. Carbohydrate-protein interactions at the +1 subsite of Exg provide the main contribution to the transition state interaction energy
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-
?
additional information
?
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the enzyme shows glycohydrolase and transglycosidase activities, substrate binding structures determined from mutant E292S complex crystal structures, detailed overview
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?
NATURAL SUBSTRATE
NATURAL 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
LL-37
antimicrobial peptide derived from human cathelicidin, by proteinase-3 cleavage. LL-37 significantly reduces Candida albicans adhesion to plastic, oral epidermoid OECM-1 cells, and urinary bladders of female BALB/c mice. LL-37 reduces Xog1 activity and thus interrupts cell-wall remodeling
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Laminarin
KM value of wild-type is 4.8 mg/ml, pH 5.6, 37°C
additional information
additional information
-
laminarin 3.8 mg/ml, mutant E230Q 2.6 mM, mutnat E330Q 2.9 mM, mutant Q330E 2.9 mM
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Laminarin
kcat/KM value of wild-type is 32.7 mg per ml and sec, pH 5.6, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
deletion of XOG1 leads to decrease in cellular exoglucanase activity, cell adhesion and binding of antimicrobial peptide LL-37. Antibodies against Xog1p also decrease cell adhesion. Xog1 has a role in Candida albicans adhesion to polystyrene and, by inference, attachment to host cells via direct or indirect manners
physiological function
the enzyme is involved in cell wall beta-D-glucan metabolism and morphogenesis through its hydrolase and transglycosidase activities
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
generation of a series of enzyme-substrate complexes using molecular docking, ranging from Exg-glucose to Exg-laminarihexaose, structure optimizations followed by molecular dynamics, conducted for each complex to assess the flexibility of the substrate, of the enzyme as a whole, and of enzyme-substrate interactions, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants F258I, E292Q, E292S /F229A and F144Y/F258Y, and mutant E292S/F229A complexed with laminaritriose
purified recombinant mutant E282S alone or in complex with alpha-D-glucopyranosyl fluoride and 4-nitrophenyl-beta-D-glucopyranoside, or with 4-nitrophenyl-gentiobiose, X-ray diffraction structure determination and analysis at 1.59-1.96 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E292S
site-directed mutagenesis, the mutant shows altered transglycosidase activity as the wild-type enzyme and displays modest glycosynthase activity with alpha-D-glucopyranosyl fluoride as the donor and 4-nitrophenyl-beta-D-glucopyranoside as the acceptor, but surprisingly shows a marked preference for synthesizing beta-1,6-linked over beta-1,3- and beta-1,4-linked disaccharide products. Mechanism and expected regiospecificity for the glycosynthase reaction, overview
F258A
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
F258I
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
F258W
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
F258Y
activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
the small enzyme is an ideal computational model for its family of enzymes, GH5, and can be used to create several enzyme-substrate models starting from a crystallographic glucanase inhibitor structure
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Molina, M.; Cenamor, R.; Sanchez, M.; Nobela, C.
Purification and some properties of Candida albicans exo-1,3-beta-glucanase
J. Gen. Microbiol.
135
309-314
1989
Candida albicans
Molina, M.; Cenamor, R.; Nobela, C.
exo-1,3-beta-Glucanase activity in Candida albicans: effect of the yeast-to-mycelium transition
J. Gen. Microbiol.
133
609-617
1987
Candida albicans
Cutfield, S.; Brooke, G.; Sullivan, P.; Cutfield, J.
Crystallization of the exo(1,3)-beta-glucanase from Candida albicans
J. Mol. Biol.
225
217-218
1992
Candida albicans
Chambers, R.S.; Broughton, M.J.; Cannon, R.D.; Carne, A.; Emerson, G.W.; Sullivan, P.A.
An exo-beta-(1,3)-glucanase of Candida albicans: purification of the enzyme and molecular cloning of the gene
J. Gen. Microbiol.
139
325-334
1993
Candida albicans
Chambers, R.S.; Waldern, A.R.; Brooke, G.S.; Cutfield, J.F.; Sullivan, P.A.
Identification of a putative active site residue in the exo-beta-(1,3)-glucanase of Candida albicans
FEBS Lett.
327
366-369
1993
Candida albicans
Cutfield, S.M.; Davies, G.J.; Murshudov, G.; Anderson, B.F.; Moody, P.C.E.; Sullivan, P.A.; Cutfield, J.F.
The structure of the exo-beta-(1,3)-glucanase from Candida albicans in native and bound forms: Relationship between a pocte an groove in family 5 glycosyl hydrolases
J. Mol. Biol.
294
771-783
1999
Candida albicans
Mackenzie, L.F.; Brooke, G.S.; Cutfield, J.F.; Sullivan, P.A.; Withers, S.G.
Identification of Glu-330 as the catalytic nucleophile of Candida albicans exo-beta-(1,3)-glucanase
J. Biol. Chem.
272
3161-3167
1997
Candida albicans
Moura-Tamames, S.A.; Ramos, M.J.; Fernandes, P.A.
Modelling beta-1,3-exoglucanase-saccharide interactions: structure of the enzyme-substrate complex and enzyme binding to the cell wall
J. Mol. Graph. Model.
27
908-920
2009
Candida albicans (P29717)
Patrick, W.M.; Nakatani, Y.; Cutfield, S.M.; Sharpe, M.L.; Ramsay, R.J.; Cutfield, J.F.
Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe clamp at the active site entrance
FEBS J.
277
4549-4561
2010
Candida albicans (P29717)
Tsai, P.W.; Yang, C.Y.; Chang, H.T.; Lan, C.Y.
Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37
PLoS ONE
6
e21394
2011
Candida albicans (P29717)
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