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Literature summary for 3.2.1.133 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

General Stability Organism
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

Organism UniProt Comment Textmining
Geobacillus thermoleovorans I6RE37
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Gt-MamyIII
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Geobacillus thermoleovorans
maltogenic amylase
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Geobacillus thermoleovorans

Temperature Optimum [°C]

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

Temperature Stability [°C]

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