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Literature summary for 3.2.1.1 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
Search for more literature for 3.2.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae Oryza sativa

Protein Variants

Protein Variants Comment Organism
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
N240Q mutant of isoenzyme Amy1A Oryza sativa

KM Value [mM]

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

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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