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Literature summary extracted from

  • Kim, Y.W.; Choi, J.H.; Kim, J.W.; Park, C.; Cha, H.; Lee, S.B.; Oh, B.H.; Moon, T.W.; Park, K.H.
    Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance (2003), Appl. Environ. Microbiol., 69, 4866-4874.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 A398V random mutagenesis, using DNA shuffling Thermus sp.
3.2.1.133 I333V random mutagenesis, using DNA shuffling Thermus sp.
3.2.1.133 M375T random mutagenesis, using DNA shuffling Thermus sp.
3.2.1.133 P453L random mutagenesis, using DNA shuffling Thermus sp.
3.2.1.133 Q411L random mutagenesis, using DNA shuffling Thermus sp.
3.2.1.133 R26Q random mutagenesis, using DNA shuffling Thermus sp.
3.2.1.133 S169N random mutagenesis, using DNA shuffling Thermus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.133 0.05
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant DM Thermus sp.
3.2.1.133 0.09
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 4B74 Thermus sp.
3.2.1.133 0.16
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, wild-type and variants 3C71, 4B78 and 4A48 Thermus sp.
3.2.1.133 0.17
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variants 1B76, 1B100 Thermus sp.
3.2.1.133 0.19
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 2A39 Thermus sp.

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.133 Thermus sp.
-
-
-
3.2.1.133 Thermus sp. IM6501
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.133 wild-type and mutant enzymes Thermus sp.

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 0.2
-
 pH 6.0, 60°C, beta-cyclodextrin as substrate, variant DM Thermus sp.
3.2.1.133 0.3
-
 pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B74 Thermus sp.
3.2.1.133 1
-
 pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B78 Thermus sp.
3.2.1.133 1.5
-
 pH 6.0, 60°C, beta-cyclodextrin as substrate, wild-type Thermus sp.
3.2.1.133 1.7
-
 pH 6.0, 60°C, beta-cyclodextrin as substrate, variants 2A39, 4A48 and 3C71 Thermus sp.
3.2.1.133 2
-
 pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B100 Thermus sp.
3.2.1.133 2.1
-
 pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B76 Thermus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.133 60
-
 wild-type Thermus sp.
3.2.1.133 75
-
 ThMA-DM, highly thermostable mutant enzyme Thermus sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.133 80
-
 ThMA-DM, highly thermostable mutant enzyme, half-life 172 min, wild type enzyme completely inactivated in less than 1 min Thermus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.133 20
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variants DM and 4B74 Thermus sp.
3.2.1.133 110
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 4B78 Thermus sp.
3.2.1.133 120
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 3C71 Thermus sp.
3.2.1.133 130
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 4A48 Thermus sp.
3.2.1.133 160
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, wild-type Thermus sp.
3.2.1.133 170
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 2A39 Thermus sp.
3.2.1.133 190
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 1B100 Thermus sp.
3.2.1.133 200
-
 beta-cyclodextrin pH 6.0, 60°C, hydrolysis, variant 1B76 Thermus sp.