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Literature summary extracted from

  • Yang, X.; Westcott, S.; Gong, X.; Evans, E.; Zhang, X.; Lance, R.; Li, C.
    Amino acid substitutions of the limit dextrinase gene in barley are associated with enzyme thermostability (2009), Mol. Breed., 23, 61-74.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.142 A885S single nucleotide polymorphism associated with thermostability Hordeum vulgare
3.2.1.142 L102R/T233A/S235G/G298A/C415R/A885S/G888C amino acid substitutions identified by alignment of the limit dextrinase sequences of varieties Galleon and Maud Hordeum vulgare
3.2.1.142 additional information investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm Hordeum vulgare
3.2.1.142 additional information investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm. No polymorphism is associated with the enzyme activity Hordeum vulgare
3.2.1.142 T233A single nucleotide polymorphism associated with thermostability Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.142 Hordeum vulgare O48541 barley variety Igri
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3.2.1.142 Hordeum vulgare Q9FYY0 barley variety Maud
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3.2.1.142 Hordeum vulgare Q9S7S8 barley variety Galleon
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