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Literature summary for 3.2.1.58 extracted from

  • 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 (2009), J. Mol. Graph. Model., 27, 908-920.
    View publication on PubMed
Search for more literature for 3.2.1.58

Application

Application Comment Organism
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 Candida albicans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-1,3-glucan + H2O Candida albicans
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 ?
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 ?

Organism

Organism UniProt Comment Textmining
Candida albicans P29717
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-1,3-glucan + H2O
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 Candida albicans ?
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 ?
laminarihexaose + H2O
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 Candida albicans ?
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 ?
laminaripentaose + H2O
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 Candida albicans ?
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 ?
laminaritetraose + H2O
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 Candida albicans ?
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 ?
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 Candida albicans ?
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Subunits

Subunits Comment Organism
More 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 Candida albicans

Synonyms

Synonyms Comment Organism
beta-1,3-exoglucanase
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 Candida albicans
Exg
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 Candida albicans
More the enzyme belongs to the glycosyl hydrolase family 5, GH5 Candida albicans