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Literature summary extracted from

  • Zhang, W.; Kang, L.; Yang, M.; Zhou, Y.; Wang, J.; Liu, Z.; Yuan, S.
    Purification, characterization and function analysis of an extracellular beta-glucosidase from elongating stipe cell walls in Coprinopsis cinerea (2016), FEMS Microbiol. Lett., 363, fnw078 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.21 EDTA 5 mM, 40% inhibition Coprinopsis cinerea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.21 2
-
 4-nitrophenyl beta-D-glucopyranoside pH not specified in the publication, temperature not specified in the publication Coprinopsis cinerea

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.21 extracellular
-
 Coprinopsis cinerea
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.21 Fe2+ 5 mM, 110% of initial activity Coprinopsis cinerea

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.21 302200
-
 PAGE Coprinopsis cinerea

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Coprinopsis cinerea A8NIX3
-
-
3.2.1.21 Coprinopsis cinerea ATCC MYA-4618 A8NIX3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.21 glycoprotein
-
 Coprinopsis cinerea

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.21
-
 Coprinopsis cinerea

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.21 stipe stipe cell wall, enzyme is more highly expressed in the elongating apical stipe than in non-elongating basal regions Coprinopsis cinerea
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.21 117
-
 substrate laminaritriose, pH not specified in the publication, temperature not specified in the publication Coprinopsis cinerea
3.2.1.21 129
-
 substrate laminaritetraose, pH not specified in the publication, temperature not specified in the publication Coprinopsis cinerea
3.2.1.21 175
-
 substrate cellobiose, pH not specified in the publication, temperature not specified in the publication Coprinopsis cinerea
3.2.1.21 212
-
 substrate laminaribiose, pH not specified in the publication, temperature not specified in the publication Coprinopsis cinerea
3.2.1.21 268
-
 substrate gentiobiose, pH not specified in the publication, temperature not specified in the publication Coprinopsis cinerea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.21 2 laminaribiose
-
 Coprinopsis cinerea D-glucose + laminaritriose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Coprinopsis cinerea 4-nitrophenol + D-glucopyranose
-
 ?
3.2.1.21 4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Coprinopsis cinerea ATCC MYA-4618 4-nitrophenol + D-glucopyranose
-
 ?
3.2.1.21 cellobiose + H2O
-
 Coprinopsis cinerea 2 D-glucose
-
 ?
3.2.1.21 cellobiose + H2O
-
 Coprinopsis cinerea ATCC MYA-4618 2 D-glucose
-
 ?
3.2.1.21 gentiobiose + H2O
-
 Coprinopsis cinerea D-glucose
-
 ?
3.2.1.21 gentiobiose + H2O
-
 Coprinopsis cinerea ATCC MYA-4618 D-glucose
-
 ?
3.2.1.21 laminaribiose + H2O
-
 Coprinopsis cinerea 2 D-glucose
-
 ?
3.2.1.21 laminaritetraose + 3 H2O
-
 Coprinopsis cinerea 4 D-glucose
-
 ?
3.2.1.21 laminaritriose + 2 H2O
-
 Coprinopsis cinerea 3 D-glucose
-
 ?
3.2.1.21 laminaritriose + 2 H2O
-
 Coprinopsis cinerea ATCC MYA-4618 3 D-glucose
-
 ?
3.2.1.21 additional information the enzyme does not degrade beta-glucans with modified ends, whereas it hydrolyzes various beta-glucans with free ends and related oligosaccharides with beta-1,3-, beta-1,4- or beta-1,6-linkages. It shows glycosyltransferase activity, preferably transfering 1 glucose residue from the donor oligosaccharides to the acceptor oligosaccharides, yielding laminario-(n–1) oligosaccharides and laminario-(n+1) oligosaccharides Coprinopsis cinerea ?
-
 ?
3.2.1.21 additional information the enzyme does not degrade beta-glucans with modified ends, whereas it hydrolyzes various beta-glucans with free ends and related oligosaccharides with beta-1,3-, beta-1,4- or beta-1,6-linkages. It shows glycosyltransferase activity, preferably transfering 1 glucose residue from the donor oligosaccharides to the acceptor oligosaccharides, yielding laminario-(n–1) oligosaccharides and laminario-(n+1) oligosaccharides Coprinopsis cinerea ATCC MYA-4618 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.21 heterotrimer 1 * 165200, plus 1 * 87900, plus 1 * 56800, SDS-PAGE Coprinopsis cinerea

Synonyms

EC Number Synonyms Comment Organism
3.2.1.21 CC1G_08724
-
 Coprinopsis cinerea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.21 60
-
-
 Coprinopsis cinerea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.21 70
-
 30 min, 70% loss of activity Coprinopsis cinerea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.21 5
-
-
 Coprinopsis cinerea

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.21 4 9 stable for 30 min Coprinopsis cinerea

General Information

EC Number General Information Comment Organism
3.2.1.21 physiological function enzyme causes a decrease in the molecular size of stipe wall beta-glucan by removing glucose and is more highly expressed in the elongating apical stipe than in non-elongating basal regions Coprinopsis cinerea