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Literature summary for 3.2.1.21 extracted from

  • Yang, S.; Jiang, Z.; Yan, Q.; Zhu, H.
    Characterization of a thermostable extracellular beta-glucosidase with activities of exoglucanase and transglycosylation from Paecilomyces thermophila (2008), J. Agric. Food Chem., 56, 602-608.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol slight inhibition Paecilomyces sp. 'thermophila'
Ag+ 80% inhibition at 4 mM Paecilomyces sp. 'thermophila'
D-glucono-1,5-lactone competitive inhibition Paecilomyces sp. 'thermophila'
D-glucose competitive inhibition Paecilomyces sp. 'thermophila'
EDTA slight inhibition Paecilomyces sp. 'thermophila'
Hg2+ 95.5% inhibition at 4 mM Paecilomyces sp. 'thermophila'
additional information no or poor inhibition by Ca2+ and DTT Paecilomyces sp. 'thermophila'
SDS slight inhibition Paecilomyces sp. 'thermophila'

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.26
-
4-nitrophenyl-beta-D-glucopyranoside pH 6.2, 50°C Paecilomyces sp. 'thermophila'
0.65
-
cellobiose pH 6.2, 50°C Paecilomyces sp. 'thermophila'
0.77
-
gentiobiose pH 6.2, 50°C Paecilomyces sp. 'thermophila'
1.06
-
sophorose pH 6.2, 50°C Paecilomyces sp. 'thermophila'
1.39
-
Salicin pH 6.2, 50°C Paecilomyces sp. 'thermophila'
1.45
-
amygdalin pH 6.2, 50°C Paecilomyces sp. 'thermophila'

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Paecilomyces sp. 'thermophila'
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Paecilomyces sp. 'thermophila'
Cu2+ activates slightly Paecilomyces sp. 'thermophila'
Fe2+ activates by 36% Paecilomyces sp. 'thermophila'
Mg2+ activates Paecilomyces sp. 'thermophila'
Mn2+ activates Paecilomyces sp. 'thermophila'
additional information no metalloprotein, not affected by Al3+ at 1.0 mM Paecilomyces sp. 'thermophila'
Ni2+ activates Paecilomyces sp. 'thermophila'
Sr2+ activates slightly Paecilomyces sp. 'thermophila'
Zn2+ activates Paecilomyces sp. 'thermophila'

Organism

Organism UniProt Comment Textmining
Paecilomyces sp. 'thermophila'
-
-
-
Paecilomyces sp. 'thermophila' J18
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the extracellular enzyme contains 82.3% carbohydrate Paecilomyces sp. 'thermophila'

Purification (Commentary)

Purification (Comment) Organism
native enzyme 105fold to homogeneity by anion exchange chromatography and gel filtration Paecilomyces sp. 'thermophila'

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
97.2
-
purified enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside Paecilomyces sp. 'thermophila'

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-glucopyranoside + H2O best substrate Paecilomyces sp. 'thermophila' 4-nitrophenol + beta-D-glucose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O best substrate Paecilomyces sp. 'thermophila' J18 4-nitrophenol + beta-D-glucose
-
?
amygdalin + 2 H2O
-
Paecilomyces sp. 'thermophila' mandelonitrile + 2 beta-D-glucose
-
?
cellobiose + H2O
-
Paecilomyces sp. 'thermophila' 2 beta-D-glucose
-
?
cellobiose + H2O
-
Paecilomyces sp. 'thermophila' J18 2 beta-D-glucose
-
?
cellopentaose + H2O
-
Paecilomyces sp. 'thermophila' 5 D-glucose
-
?
cellotetraose + 3 H2O
-
Paecilomyces sp. 'thermophila' 4 beta-D-glucose
-
?
cellotriose + H2O
-
Paecilomyces sp. 'thermophila' 3 D-glucose
-
?
daidzin + H2O
-
Paecilomyces sp. 'thermophila' beta-D-glucose + daidzein
-
?
genistin + H2O
-
Paecilomyces sp. 'thermophila' beta-D-glucose + genistein
-
?
gentiobiose + H2O
-
Paecilomyces sp. 'thermophila' 2 beta-D-glucose
-
?
gentiobiose + H2O
-
Paecilomyces sp. 'thermophila' J18 2 beta-D-glucose
-
?
laminarin + H2O
-
Paecilomyces sp. 'thermophila' beta-D-glucose
-
?
lichenan + H2O
-
Paecilomyces sp. 'thermophila' beta-D-glucose
-
?
additional information the extracellular enzyme exhibits a broad substrate specificity, shows also exoglucanase and transglycosylation activities, overview Paecilomyces sp. 'thermophila' ?
-
?
additional information the extracellular enzyme exhibits a broad substrate specificity, shows also exoglucanase and transglycosylation activities, overview Paecilomyces sp. 'thermophila' J18 ?
-
?
salicin + H2O
-
Paecilomyces sp. 'thermophila' beta-D-glucose + 2-(hydroxymethyl)phenol
-
?
sophorose + H2O
-
Paecilomyces sp. 'thermophila' 2 beta-D-glucose
-
?
sophorose + H2O
-
Paecilomyces sp. 'thermophila' J18 2 beta-D-glucose
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
-
Paecilomyces sp. 'thermophila'

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
temperature profile Paecilomyces sp. 'thermophila'

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
purified enzyme, quite stable up to Paecilomyces sp. 'thermophila'
70
-
purified enzyme, 57.9% remaining activity Paecilomyces sp. 'thermophila'

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7
-
sophorose pH 6.2, 50°C Paecilomyces sp. 'thermophila'
4.2
-
gentiobiose pH 6.2, 50°C Paecilomyces sp. 'thermophila'
4.5
-
cellobiose pH 6.2, 50°C Paecilomyces sp. 'thermophila'
7.1
-
Salicin pH 6.2, 50°C Paecilomyces sp. 'thermophila'
7.9
-
amygdalin pH 6.2, 50°C Paecilomyces sp. 'thermophila'
13
-
4-nitrophenyl-beta-D-glucopyranoside pH 6.2, 50°C Paecilomyces sp. 'thermophila'

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
-
Paecilomyces sp. 'thermophila'

pH Range

pH Minimum pH Maximum Comment Organism
5 8.5 pH profile Paecilomyces sp. 'thermophila'

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.49
-
D-glucono-1,5-lactone pH 6.2, 50°C Paecilomyces sp. 'thermophila'
73
-
D-glucose pH 6.2, 50°C Paecilomyces sp. 'thermophila'