Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Application

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.54 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

EC Number Protein Variants Comment Organism
3.2.1.54 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.54 8.78
-
beta-cyclodextrin pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
3.2.1.54 9.07
-
maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
3.2.1.54 9.77
-
maltoheptaose pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
3.2.1.54 154
-
beta-cyclodextrin pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.54 Pyrococcus furiosus Q8TZP8
-
-

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
-
Pyrococcus furiosus ?
-
?
3.2.1.54 maltoheptaose + H2O
-
Pyrococcus furiosus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.54 CD-hydrolyzing amylase
-
Pyrococcus furiosus
3.2.1.54 PFTA
-
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 1.63
-
maltoheptaose pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
3.2.1.54 93.3
-
maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
3.2.1.54 199
-
beta-cyclodextrin pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
3.2.1.54 382
-
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 0.17
-
maltoheptaose pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
3.2.1.54 1.29
-
beta-cyclodextrin pH 4.5, 85°C, mutant enzyme G415E Pyrococcus furiosus
3.2.1.54 10.3
-
maltoheptaose pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus
3.2.1.54 43.5
-
beta-cyclodextrin pH 4.5, 85°C, wild-type enzyme Pyrococcus furiosus