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Literature summary for 3.2.1.142 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
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Protein Variants

Protein Variants Comment Organism
A885S single nucleotide polymorphism associated with thermostability Hordeum vulgare
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
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
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
T233A single nucleotide polymorphism associated with thermostability Hordeum vulgare

Organism

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