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Literature summary for 3.2.1.54 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
Search for more literature for 3.2.1.54

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
G415E the hydrolysis of beta-cyclodextrins decreases 80fold. Substrate preference is similar to that of the wild-type enzyme Pyrococcus furiosus
H414N the hydrolysis of beta-cyclodextrins decreases 10fold. Substrate preference is similar to that of the wild-type enzyme Pyrococcus furiosus
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]

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

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
maltoheptaose + H2O
-
 Pyrococcus furiosus ?
-
 ?

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

kcat/KM [mM/s]

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