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Literature summary for 2.4.1.64 extracted from

  • Nihira, T.; Saito, Y.; Chiku, K.; Kitaoka, M.; Ohtsubo, K.; Nakai, H.
    Potassium ion-dependent trehalose phosphorylase from halophilic Bacillus selenitireducens MLS10 (2013), FEBS Lett., 587, 3382-3386.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Salisediminibacterium selenitireducens

Inhibitors

Inhibitors Comment Organism Structure
alpha,alpha-trehalose
-
Salisediminibacterium selenitireducens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
phosphate recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens
0.86
-
alpha,alpha-trehalose recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens
2
-
beta-D-glucose 1-phosphate recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens
5.5
-
D-glucose recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens

Metals/Ions

Metals/Ions Comment Organism Structure
K+ essential for enzymatic activity. Decreasing potassium ion concentrations significantly reduce thermal and pH stabilities of the enzyme Salisediminibacterium selenitireducens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
87889
-
2 * 87889, calculated from amino acid sequence Salisediminibacterium selenitireducens
88000
-
2 * 88000, SDS-PAGE Salisediminibacterium selenitireducens
170000
-
gel filtration Salisediminibacterium selenitireducens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha,alpha-trehalose + phosphate Salisediminibacterium selenitireducens
-
D-glucose + beta-D-glucose 1-phosphate
-
r
alpha,alpha-trehalose + phosphate Salisediminibacterium selenitireducens MLS10
-
D-glucose + beta-D-glucose 1-phosphate
-
r
D-glucose + beta-D-glucose 1-phosphate Salisediminibacterium selenitireducens
-
alpha,alpha-trehalose + phosphate
-
r
D-glucose + beta-D-glucose 1-phosphate Salisediminibacterium selenitireducens MLS10
-
alpha,alpha-trehalose + phosphate
-
r

Organism

Organism UniProt Comment Textmining
Salisediminibacterium selenitireducens D6XSD4
-
-
Salisediminibacterium selenitireducens MLS10 D6XSD4
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography Salisediminibacterium selenitireducens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha,alpha-trehalose + phosphate
-
Salisediminibacterium selenitireducens D-glucose + beta-D-glucose 1-phosphate
-
r
alpha,alpha-trehalose + phosphate
-
Salisediminibacterium selenitireducens MLS10 D-glucose + beta-D-glucose 1-phosphate
-
r
D-glucose + beta-D-glucose 1-phosphate
-
Salisediminibacterium selenitireducens alpha,alpha-trehalose + phosphate
-
r
D-glucose + beta-D-glucose 1-phosphate
-
Salisediminibacterium selenitireducens MLS10 alpha,alpha-trehalose + phosphate
-
r

Subunits

Subunits Comment Organism
homodimer 2 * 88000, SDS-PAGE Salisediminibacterium selenitireducens
homodimer 2 * 87889, calculated from amino acid sequence Salisediminibacterium selenitireducens

Synonyms

Synonyms Comment Organism
Bsel_1207 recombinant protein Salisediminibacterium selenitireducens
trehalose phosphorylase
-
Salisediminibacterium selenitireducens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
60
-
D-glucose recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens
68
-
beta-D-glucose 1-phosphate recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens
210
-
alpha,alpha-trehalose recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
95
-
alpha,alpha-trehalose recombinant enzyme, at pH 6.5 and 30°C Salisediminibacterium selenitireducens

General Information

General Information Comment Organism
metabolism the enzyme is involved in osmotic control through the biosynthesis of trehalose Salisediminibacterium selenitireducens