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Literature summary for 3.2.1.54 extracted from

  • Park, J.T.; Song, H.N.; Jung, T.Y.; Lee, M.H.; Park, S.G.; Woo, E.J.; Park, K.H.
    A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus (2013), Biochim. Biophys. Acta, 1834, 380-386.
    View publication on PubMed
Search for more literature for 3.2.1.54

Application

Application Comment Organism
synthesis the G415E mutant is an excellent candidate for the industrial production of specific-length maltooligosaccharides from cyclodextrins Pyrococcus furiosus

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop method at 18°C. The structure studies supporting the proposition that cyclodextrin-hydrolyzing amylases from hyperthermophilic microorganisms contain all of the structural components required for substrate binding within a single monomer, distinguishing PFTA from the classical bacterial cyclodextrin-hydrolyzing enzymes of the GH13 family Pyrococcus furiosus

Protein Variants

Protein Variants Comment Organism
G415E the mutant enzyme reveals considerable differences in substrate preference relative to the wild-type enzyme. Increased substrate selectivity of the mutant enzyme for the beta-cyclodextrin substrate, whereas the mutant shows no difference in activity for the maltoheptaose substrate Pyrococcus furiosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8.78
-
 beta-cyclodextrin pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
9.07
-
 maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
9.77
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
154
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8TZP8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
CD-hydrolyzing amylase
-
 Pyrococcus furiosus
PFTA
-
 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
1.63
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
93.3
-
 maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
199
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
382
-
 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
0.17
-
 maltoheptaose pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
1.29
-
 beta-cyclodextrin pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
10.3
-
 maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
43.5
-
 beta-cyclodextrin pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus