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Literature summary extracted from

  • Mikkelsen, R.; Binderup, K.; Preiss, J.
    Tyrosine residue 300 is important for activity and stability of branching enzyme from Escherichia coli (2001), Arch. Biochem. Biophys., 385, 372-377.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18
-
Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.18 Y300A mutant enzyme shows less than 1% of the wild-type activity Escherichia coli
2.4.1.18 Y300D mutant enzyme shows less than 1% of the wild-type activity Escherichia coli
2.4.1.18 Y300F mutant enzyme shows 25% of the wild-type activity, no effect on Km-value, heat stability is lowered significantly compared to that of the wild-type enzyme, lower relative activity at elevated temperatures compared to wild-type enzyme Escherichia coli
2.4.1.18 Y300L mutant enzyme shows less than 1% of the wild-type activity Escherichia coli
2.4.1.18 Y300S mutant enzyme shows less than 1% of the wild-type activity Escherichia coli
2.4.1.18 Y300W mutant enzyme shows less than 1% of the wild-type activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.18 0.0142
-
amylose amylose AS-320, pH 7.0, 30°C, wild-type enzyme Escherichia coli
2.4.1.18 0.0175
-
amylose amylose AS-320, pH 7.0, 30°C, mutant enzyme Y300F Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 amylose wild-type enzyme and mutant enzyme Y300F both preferentially transfer chains between DP5 and DP16, with a chain of DP11 being transferred at the highest frequency Escherichia coli amylose containing alpha-1,6-glucosidic linkages
-
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