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Literature summary for 3.2.1.73 extracted from

  • Jia, H.; Li, Y.; Liu, Y.; Yan, Q.; Yang, S.; Jiang, Z.
    Engineering a thermostable beta-1,3-1,4-glucanase from Paecilomyces thermophila to improve catalytic efficiency at acidic pH (2012), J. Biotechnol., 159, 50-55.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene PtLic16A, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Paecilomyces sp. 'thermophila'

Protein Variants

Protein Variants Comment Organism
C263S random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme Paecilomyces sp. 'thermophila'
D221G2 random mutagenesis, the mutant shows unaltered properties compared to the wild-type enzyme Paecilomyces sp. 'thermophila'
D56G random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme Paecilomyces sp. 'thermophila'
D56G/D221G/C263S random mutagenesis, mutant PtLic16AM2 shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme. Mutation D221G alone does not lead to altered enzyme properties Paecilomyces sp. 'thermophila'
additional information screening of the random mutant library, mutations D56G, D221G, and C263S have only minor effects on specific activity and pH stability Paecilomyces sp. 'thermophila'

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information 3.69 mg/ml for the wild-type enzyme and 3.30 mg/ml for mutant D56G/D221G/C263S, with barley beta-glucan at pH 5.0, 70°C Paecilomyces sp. 'thermophila'

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Paecilomyces sp. 'thermophila' beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans ?
-
?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Paecilomyces sp. 'thermophila'

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
barley beta-glucan + H2O
-
Paecilomyces sp. 'thermophila' ?
-
?
additional information beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans Paecilomyces sp. 'thermophila' ?
-
?

Subunits

Subunits Comment Organism
More molecular structure modeling and analysis Paecilomyces sp. 'thermophila'

Synonyms

Synonyms Comment Organism
beta-1,3-1,4-glucanase
-
Paecilomyces sp. 'thermophila'
PtLic16A
-
Paecilomyces sp. 'thermophila'

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
Paecilomyces sp. 'thermophila'

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 90 activity range, wild-type and mutant enzymes, profile overview Paecilomyces sp. 'thermophila'

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
102
-
Barley beta-glucan pH 5.0, 70°C, wild-type enzyme Paecilomyces sp. 'thermophila'
143
-
Barley beta-glucan pH 5.0, 70°C, mutant D56G/D221G/C263S Paecilomyces sp. 'thermophila'

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
amino acid residues at positions 56 and 263 are important in determining optimal pH activity Paecilomyces sp. 'thermophila'
5
-
mutant D56G/D221G/C263S Paecilomyces sp. 'thermophila'
5.5
-
mutant C263S Paecilomyces sp. 'thermophila'
6
-
mutant D56G Paecilomyces sp. 'thermophila'
7
-
wild-type enzyme and mutant D221G Paecilomyces sp. 'thermophila'

pH Range

pH Minimum pH Maximum Comment Organism
3 10 activity range, wild-type and mutant enzymes, profile overview Paecilomyces sp. 'thermophila'

General Information

General Information Comment Organism
additional information molecular structure modeling and analysis Paecilomyces sp. 'thermophila'