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Literature summary extracted from

  • Tang, S.Y.; Le, Q.T.; Shim, J.H.; Yang, S.J.; Auh, J.H.; Park, C.; Park, K.H.
    Enhancing thermostability of maltogenic amylase from Bacillus thermoalkalophilus ET2 by DNA shuffling (2006), FEBS J., 273, 3335-3345.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.133 expressed in Escherichia coli MC1061, His-tagged, wild-type and mutant protein Bacillus thermoalkalophilus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 N147D/F195L/N263S/D311G/A344V/F397S/N508D mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated Bacillus thermoalkalophilus
3.2.1.133 N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown Bacillus thermoalkalophilus

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 Bacillus thermoalkalophilus
-
alpha-maltose + ?
-
?
3.2.1.133 starch + H2O Bacillus thermoalkalophilus ET2
-
alpha-maltose + ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.133 Bacillus thermoalkalophilus Q68KL3
-
-
3.2.1.133 Bacillus thermoalkalophilus ET2 Q68KL3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.133 wild-type and mutant enzymes Bacillus thermoalkalophilus

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 in wild-type and mutant enzymes, relative activity indicated for several mutants from different lineages of DNA shuffling Bacillus thermoalkalophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.133 beta-cyclodextrin + H2O main product alpha-maltose Bacillus thermoalkalophilus alpha-maltose + ?
-
?
3.2.1.133 beta-cyclodextrin + H2O main product alpha-maltose Bacillus thermoalkalophilus ET2 alpha-maltose + ?
-
?
3.2.1.133 pullulan + H2O main product panose Bacillus thermoalkalophilus panose + ?
-
?
3.2.1.133 pullulan + H2O main product panose Bacillus thermoalkalophilus ET2 panose + ?
-
?
3.2.1.133 starch + H2O
-
Bacillus thermoalkalophilus alpha-maltose + ?
-
?
3.2.1.133 starch + H2O
-
Bacillus thermoalkalophilus ET2 alpha-maltose + ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.133 BTMA
-
Bacillus thermoalkalophilus
3.2.1.133 glucan 1,4-alpha-maltohydrolase
-
Bacillus thermoalkalophilus
3.2.1.133 maltogenic amylase
-
Bacillus thermoalkalophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.133 70
-
wild-type enzyme Bacillus thermoalkalophilus
3.2.1.133 80
-
mutants III-1 and III-2 Bacillus thermoalkalophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.133 additional information
-
half-lives determined at 75°C, 78°C, 80°C, and 85°C, melting temperatures of mutants III-1 and III-2 determined by differential scanning calorimetry increased by 6.1°C and 11.4°C, respectively, hydrogen bonding, hydrophobic interaction, electrostatic interaction, proper packing, and deamidation predicted as mechanisms for enhanced thermostability in the mutant enzymes Bacillus thermoalkalophilus
3.2.1.133 78
-
half-life of mutant III-1 about 20 times greater than half-life of the wild-type at 78°C Bacillus thermoalkalophilus
3.2.1.133 80
-
half-life of mutant III-2 is 568 min, half-life of the wild-type is below 1 min at 80°C Bacillus thermoalkalophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.133 8
-
thermostability tested at Bacillus thermoalkalophilus