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Literature summary for 3.2.1.133 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
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Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Thermus sp.
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 + ?
-
 ?
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 + ?
-
 ?
starch + H2O
-
 Thermus sp. alpha-maltose + ?
-
 ?

Subunits

Subunits Comment Organism
homodimer SDS-PAGE Thermus sp.

Synonyms

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

Temperature Optimum [°C]

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