3.2.1.58: glucan 1,3-beta-glucosidase

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For detailed information about glucan 1,3-beta-glucosidase, go to the full flat file.

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

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.58 glucan 1,3-beta-glucosidase

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Results	in table
329	AA Sequence
12	Application
1	CAS Registry Number
18	Cloned(Commentary)
7	Crystallization (Commentary)
2	Expression
12	General Information
145	Inhibitors
9	kcat/KM [mM/s]
6	Ki Value [mM]
79	KM Value [mM]
49	Localization
15	Metals/Ions
70	Molecular Weight [Da]
24	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
146	Organism
2	Pathway
27	PDB ID
52	pH Optimum
20	pH Range
13	pH Stability
11	pI Value
17	Posttranslational Modification
34	Protein Variants
41	Purification (Commentary)
1	Reaction
123	Reference
39	Source Tissue
57	Specific Activity [micromol/min/mg]
13	Storage Stability
393	Substrates and Products (Substrate)
69	Subunits
101	Synonyms
1	Systematic Name
42	Temperature Optimum [°C]
8	Temperature Range [°C]
29	Temperature Stability [°C]
25	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.58 - glucan 1,3-beta-glucosidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

mutants F258I, E292Q, E292S /F229A and F144Y/F258Y, and mutant E292S/F229A complexed with laminaritriose

Candida albicans

P29717

714963

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

Candida albicans

P29717

731316

resolution 1.85 A

Candida albicans

-

136680

resolution 1.9 A

Candida albicans

-

136677

molecular modeling of structure. Residue Glu173 is the acid/base, and Glu292 is the nucleophile

Cellulomonas fimi

F4H166

738437

modeling of structure and molecular dynamics simulation. A set of amino acids substitutions in the surface and loop regions confer increased flexibility to the enzyme, thereby facilitating its structure to cold adaptation. The catalytic activity and structural flexibility at cold environment are attained through a reduced amount of hydrogen bonds and salt bridges

Glaciozyma antarctica

A0A182AUG2

738430

hanging drop vapor diffusion method, using 1.8 M of Na/K phosphate, pH 6.8

Thermochaetoides thermophila

G0S3N2

744425