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Literature summary extracted from

  • Ichikawa, K.; Tonozuka, T.; Mizuno, M; Nishikawa, A.; Sakano, Y.
    Site-directed mutagenesis of tryptophan 622 of Thermoactinomyces vulgaris R-47 glucoamylase: pH optima and activities of five mutants (2005), J. Appl. Glycosci., 52, 277-279.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.3 expression of wild-type and mutant enzymes in Escherichia coli strain MV1184 Thermoactinomyces vulgaris

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.3 W622C site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme Thermoactinomyces vulgaris
3.2.1.3 W622D site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme Thermoactinomyces vulgaris
3.2.1.3 W622G site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme Thermoactinomyces vulgaris
3.2.1.3 W622H site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme Thermoactinomyces vulgaris
3.2.1.3 W622S site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme Thermoactinomyces vulgaris

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Thermoactinomyces vulgaris
-
-
-
3.2.1.3 Thermoactinomyces vulgaris R-47
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.3 (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose residue Trp622 is important in substrate binding rather than in determination of pH optimum, and probably does not interact with the catalytic base Thermoactinomyces vulgaris
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 maltotetraose + H2O
-
 Thermoactinomyces vulgaris maltotriose + beta-D-glucose
-
 ?
3.2.1.3 maltotetraose + H2O
-
 Thermoactinomyces vulgaris R-47 maltotriose + beta-D-glucose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 glucoamylase
-
 Thermoactinomyces vulgaris
3.2.1.3 tGA
-
 Thermoactinomyces vulgaris

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 40
-
 assay at Thermoactinomyces vulgaris

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 50
-
 30 min, mutants W622C and W622S, stable Thermoactinomyces vulgaris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 6.2
-
 optimum of mutant W622D Thermoactinomyces vulgaris
3.2.1.3 6.4
-
 optimum of mutant W622G Thermoactinomyces vulgaris
3.2.1.3 6.5
-
 optimum of wild-type enzyme Thermoactinomyces vulgaris
3.2.1.3 6.6
-
 optimum of mutants W622C and W622S Thermoactinomyces vulgaris
3.2.1.3 6.8
-
 optimum of mutant W622H Thermoactinomyces vulgaris