3.2.1.58: glucan 1,3-beta-glucosidase
This is an abbreviated version!
For detailed information about glucan 1,3-beta-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.58
Reaction
Synonyms
1,3-beta-D-glucanohydrolase, AkLam33, ALAM, beta-(1,3)(1,3)-glucanase, beta-(1,3)-glucanase, beta-1,3-exoglucanase, beta-1,3-glucan exo-hydrolase, beta-1,3-glucanase, BGL1, Bglu3B, BGN3.2, BGN3.4, CC1G_06564, CC1G_07313, Celf_3321, ChinLam, Exg, Exg1, EXG2, ExgA, ExgP, exo (13)-beta-glucanase, exo-1,3-beta-D-glucanase, exo-1,3-beta-glucanase, Exo-1,3-beta-glucanase I/II, exo-1,3-beta-glucosidase, Exo-beta 1,3 glucanase, exo-beta-(1,3)-glucanase, exo-beta-(13)-D-glucanase, exo-beta-(13)-glucanohydrolase, exo-beta-1,3-D-glucanase, exo-beta-1,3-glucanase, exo-beta-glucanase, Exo1, Glu1, Glu17A, glucan (1-->3)-beta-glucosidase, GP29, Lam55, Lam55A, lamC, laminarinase, More, panomycocin, PiEXO, tag83, Xog1
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3.2.1.58 glucan 1,3-beta-glucosidaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.2.1.58 - glucan 1,3-beta-glucosidase
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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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monanchocidin A
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inhibits 98.6% at 0.257 mM, irreversible slow inhibition
monanchomycalin B
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inhibits 98.5% at 0.278 mM, irreversible slow inhibition
normonanchocidin A
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inhibits 99.3% at 0.287 mM, irreversible slow inhibition
periodate-oxidized and borohydride reduced laminarin
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substrate inhibition
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additional information
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actvitiy is not affected by 5 mM K+, Mg2+, Ca2+, or Zn2+
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additional information
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enzyme is not affected by 5 mM K+, Mg2+, Ca2+, or Zn2+
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additional information
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inhibitory effects of pentacyclic guanidine alkaloids (monanchomycalin B, monanchocidin A, and normonanchocidin A) from the marine sponge Monanchora pulchra on exo-beta-1,3-D-glucanase ChinLam enzyme activity, compound identification by mass spectrosmetry
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additional information
the enzyme is active under typical wine-related conditions, such as low pH (3.5-4.0), high sugar concentrations (up to 20% w/v), high ethanol concentrations (10-15% v/v), presence of sulfites (up to 2 mM) and various cations
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