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Literature summary extracted from

  • Terashima, M.; Katoh, S.
    Modification of alpha-amylase functions by protein engineering (1996), Ann. N. Y. Acad. Sci., 799, 65-69.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 expression in Saccharomyces cerevisiae Oryza sativa

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.1 additional information creation of a chimeric enzyme Amy1A/3D, which has 158 amino acid residues of the N-terminus of isoenzyme Amy1A and 252 amino acid residues of the C-terminus of isoenzyme Amy3D Oryza sativa
3.2.1.1 N240Q mutant of isoenzyme Amy1A Oryza sativa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information
-
 Oryza sativa

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Oryza sativa
-
 two major isoenzymes: Amy1A and Amy3D
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.1 glycoprotein isoenzyme Amy1A has an N-linked carbohydrate chain in the mature protein, isoenzyme Amy3D and chimeric enzyme Amy1A/3D do not contain N-linked carbohydrate chain Oryza sativa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 maltoheptaose + H2O
-
 Oryza sativa additional information
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 isoenzyme Amy1A shows the highest thermostability, mutant enzyme N240Q of isoenzyme Amy1A shows almost identical thermostability to those of Amy3D and Amy1A/3D Oryza sativa