Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Clark, S.E.; Hayes, P.M.; Henson, C.A.
    Characterization of barley tissue-ubiquitous beta-amylase2 and effects of the single nucleotide polymorphisms on the enzymes thermostability (2005), Crop Sci., 45, 1868-1876.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.2 isozyme Bmy2 from cultivars Morex and Steptoe, DNA and amino acid sequence determination and analysis, expression in Escherichia coli Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Hordeum vulgare
-
 cvs. Morex and Steptoe, 2 isozymes beta-amylase1 and beta-amylase2, i.e. Bmy1 and Bmy2
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.2 endosperm endosperm-specific isozyme beta-amylase1, Bmy1 Hordeum vulgare
-
3.2.1.2 additional information tissue-ubiquitous isozyme beta-amylase2, Bmy2 Hordeum vulgare
-
3.2.1.2 seed
-
 Hordeum vulgare
-

Synonyms

EC Number Synonyms Comment Organism
3.2.1.2 beta-amylase1
-
 Hordeum vulgare
3.2.1.2 beta-amylase2
-
 Hordeum vulgare
3.2.1.2 Bmy1
-
 Hordeum vulgare
3.2.1.2 Bmy2
-
 Hordeum vulgare

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.2 additional information
-
 the recombinant isozyme Bmy2 from cultivar Morex shows a slightly higher thermostability compared to the recombinant enzyme from cultivar Steptoe, T50 values, residues D238, M337, and Q362 are involved in the Morex Bmy2 thermostability, overview Hordeum vulgare