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Literature summary extracted from

  • Yang, S.J.; Min, B.C.; Kim, Y.W.; Jang, S.M.; Lee, B.H.; Park, K.H.
    Changes in the catalytic properties of Pyrococcus furiosus thermostable amylase by mutagenesis of the substrate binding sites (2007), Appl. Environ. Microbiol., 73, 5607-5612.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.54 mutant enzymes expressed in Escherichi coli Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.54 G415E the hydrolysis of beta-cyclodextrins decreases 80fold. Substrate preference is similar to that of the wild-type enzyme Pyrococcus furiosus
3.2.1.54 H414N the hydrolysis of beta-cyclodextrins decreases 10fold. Substrate preference is similar to that of the wild-type enzyme Pyrococcus furiosus
3.2.1.54 H414N/G415E the hydrolysis of beta-cyclodextrins decreases 8fold. Mutant enzyme exhibits strongly enhanced alpha-(1,4)-transglycosylation activity, resulting in the production of a series of maltooligosaccharides that are longer than the initial substrates Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.54 1.8
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme M439W/D440H Pyrococcus furiosus
3.2.1.54 2
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme M439W/D440H Pyrococcus furiosus
3.2.1.54 4
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme D440H Pyrococcus furiosus
3.2.1.54 6
-
 beta-cyclodextrin pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
3.2.1.54 13
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme D440H Pyrococcus furiosus
3.2.1.54 14
-
 maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.54 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.54
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.54 beta-cyclodextrin + H2O wild-type enzyme and mutant enzymes G415E, H414N/G415E and H414N hydrolyze beta-cyclodextrin intp maltoheptaose as the major product plus several small maltooligosaccharides Pyrococcus furiosus ?
-
 ?
3.2.1.54 maltoheptaose + H2O
-
 Pyrococcus furiosus ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.54 85
-
 assay at Pyrococcus furiosus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.54 23
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme M439W/D440H Pyrococcus furiosus
3.2.1.54 55
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme M439W/D440H Pyrococcus furiosus
3.2.1.54 64
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme D440H Pyrococcus furiosus
3.2.1.54 160
-
 maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
3.2.1.54 170
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme D440H Pyrococcus furiosus
3.2.1.54 610
-
 beta-cyclodextrin pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.54 4.5
-
 assay at Pyrococcus furiosus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.54 11
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme M439W/D440H Pyrococcus furiosus
3.2.1.54 11
-
 maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
3.2.1.54 13
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme D440H Pyrococcus furiosus
3.2.1.54 16
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme D440H Pyrococcus furiosus
3.2.1.54 31
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme M439W/D440H Pyrococcus furiosus
3.2.1.54 100
-
 beta-cyclodextrin pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus