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Literature summary extracted from

  • Mehta, D.; Satyanarayana, T.
    Structural elements of thermostability in the maltogenic amylase of Geobacillus thermoleovorans (2015), Int. J. Biol. Macromol., 79, 570-576 .
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.133 the highest thermostability of the enzyme among bacterial maltogenic amylases is attributed to the presence of four salt bridges. Among four salt bridges, the key structural determinants that govern its thermostabilization are intra-chain cross-domain, buried and networked salt bridges Geobacillus thermoleovorans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.133 Geobacillus thermoleovorans I6RE37
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.133 starch + H2O
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Geobacillus thermoleovorans ?
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?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.133 Gt-MamyIII
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Geobacillus thermoleovorans
3.2.1.133 maltogenic amylase
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Geobacillus thermoleovorans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.133 80
-
-
Geobacillus thermoleovorans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.133 80
-
T1/2: 35 h Geobacillus thermoleovorans
3.2.1.133 86
-
Tm-value Geobacillus thermoleovorans