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Literature summary extracted from

  • Kim, Y.; Kim, D.; Kim, M.; Cha, H.; Park, C.; Moon, T.; Park, K.
    Engineering Thermus maltogenic amylase with improved thermostability: Probing the role of the conserved calcium binding site in cyclodextrin-degrading enzymes (2005), J. Appl. Glycosci., 52, 7-13.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.133 EDTA increases activity of wild-type enzyme and of mutant enzyme R26Q/S169N/I333V/A398V/Q411L/P453L Thermus sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L mutant enzyme shows highly improved thermostability and catalytic activity in presence of Ca2+ Thermus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.133 Ca2+ mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L shows highly improved thermostability and catalytic activity in presence of Ca2+. Thermus sp.

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.133
-
Thermus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.133 beta-cyclodextrin + H2O
-
Thermus sp. maltose + ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.133 maltogenic amylase
-
Thermus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.133 70
-
mutant R26Q/S169N/I333V/A398V/Q411L/P453L Thermus sp.
3.2.1.133 75
-
mutant R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L Thermus sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.133 82
-
Tm-value of mutant R26Q/S169N/I333V/A398V/Q411L/P453L is 81.5°C Thermus sp.
3.2.1.133 85
-
Tm-value of mutant enzyme R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L, Tm-value decreases to 79.9°C in presence of EDTA. Tm-value increases to 87.4°C in presence of CaCl2 Thermus sp.