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Literature summary extracted from

  • Park, S.H.; Kang, H.K.; Shim, J.H.; Woo, E.J.; Hong, J.S.; Kim, J.W.; Oh, B.H.; Lee, B.H.; Cha, H.; Park, K.H.
    Modulation of substrate preference of thermus maltogenic amylase by mutation of the residues at the interface of a dimer (2007), Biosci. Biotechnol. Biochem., 71, 1564-1567.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.133 expressed in Escherichia coli MC1061, His-tagged, recombinant protein Thermus sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 G50I/D109E double mutation, two main residues of the catalytic binding pocket, site-directed mutagenesis Thermus sp.
3.2.1.133 G50I/D109E/V431I triple mutation of three main residues of the catalytic binding pocket, site-directed mutagenesis Thermus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.133 additional information
-
 additional information lower affinity for binding of amylopectin but higher affinity for amylose in mutant enzymes demonstrated, sterospecific substrate binding properties of triple mutant enzyme determined by molecular modelling Thermus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.133 66000
-
 SDS-PAGE, recombinant and wild-type protein Thermus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.133 starch + H2O Thermus sp.
-
 alpha-maltose + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.133 Thermus sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.133 wild-type and recombinant protein, gel filtration Thermus sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.133 additional information
-
 kinetic properties determined towards amylose and amylopectin in wild-type, double and triple mutant enzymes, bicinchonimate method, determination of reducing sugars Thermus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.133 amylopectin + H2O hydrolytic release of maltose residues, wild-type, double and triple mutant enzymes studied to determine substrate size and geometric shape of catalytic site Thermus sp. alpha-maltose + ?
-
 ?
3.2.1.133 amylose + H2O substrate size and geometric shape of catalytic site analyzed, wild-type, double and triple mutant enzymes tested, wild-type enzyme hydrolyzed amylose more favourably than amylopectin Thermus sp. alpha-maltose + ?
-
 ?
3.2.1.133 starch + H2O
-
 Thermus sp. alpha-maltose + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.133 homodimer SDS-PAGE Thermus sp.

Synonyms

EC Number Synonyms Comment Organism
3.2.1.133 glucan 1,4-alpha-maltohydrolase
-
 Thermus sp.
3.2.1.133 maltogenic amylase
-
 Thermus sp.
3.2.1.133 ThMA
-
 Thermus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.133 55
-
 assay at, wild-type, double and triple mutant enzymes analyzed Thermus sp.