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Literature summary for 3.2.1.133 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
Search for more literature for 3.2.1.133

Activating Compound

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

Protein Variants

Protein Variants Comment Organism
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

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

Organism

Organism UniProt Comment Textmining
Thermus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus sp.

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
maltogenic amylase
-
 Thermus sp.

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
82
-
 Tm-value of mutant R26Q/S169N/I333V/A398V/Q411L/P453L is 81.5°C Thermus sp.
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.