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Literature summary for 3.2.1.141 extracted from

  • Fang, T.Y.; Tseng, W.C.; Shih, T.Y.; Wang, M.Y.
    Identification of the essential catalytic residues and selectivity-related residues of maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092 (2008), J. Agric. Food Chem., 56, 562-533.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
A259S site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively Saccharolobus solfataricus
D255A site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase Saccharolobus solfataricus
D380A site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase Saccharolobus solfataricus
E286A site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase Saccharolobus solfataricus
F355Y site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively Saccharolobus solfataricus
R356K site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively Saccharolobus solfataricus
W218A site-directed mutagenesis, the mutant shows decreased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively Saccharolobus solfataricus
W218F site-directed mutagenesis, the mutant shows decreased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively Saccharolobus solfataricus
Y328F site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of wild-type and mutant enzymes, overview Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharolobus solfataricus MTHase catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose, D255, E286, and D380 are essential catalytic residues, while residues A259, Y328, F355, and R356 are related to enzyme selectivity, mutational analysis, overview ?
-
?
additional information Saccharolobus solfataricus P2 MTHase catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose, D255, E286, and D380 are essential catalytic residues, while residues A259, Y328, F355, and R356 are related to enzyme selectivity, mutational analysis, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P95867 strain KM1 and ATCC 35092
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Saccharolobus solfataricus P2 P95867 strain KM1 and ATCC 35092
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli by anion exchange chromatography and gel filtration Saccharolobus solfataricus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.1
-
mutant D380 Saccharolobus solfataricus
0.74
-
mutant E286A Saccharolobus solfataricus
1.23
-
mutant D255A Saccharolobus solfataricus
5.31
-
mutant W218A Saccharolobus solfataricus
52
-
mutant W218F Saccharolobus solfataricus
472
-
mutant R356K Saccharolobus solfataricus
492
-
mutant Y328F Saccharolobus solfataricus
597
-
mutant F355Y Saccharolobus solfataricus
787
-
mutant A259S Saccharolobus solfataricus
814
-
wild-type enzyme Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information MTHase catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose, D255, E286, and D380 are essential catalytic residues, while residues A259, Y328, F355, and R356 are related to enzyme selectivity, mutational analysis, overview Saccharolobus solfataricus ?
-
?
additional information hydrolysis of G3T-G5T and G5-G7. Production of trehalose from starch together with isoamylase and maltooligosyltrehalose synthase, overview Saccharolobus solfataricus ?
-
?
additional information MTHase catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose, D255, E286, and D380 are essential catalytic residues, while residues A259, Y328, F355, and R356 are related to enzyme selectivity, mutational analysis, overview Saccharolobus solfataricus P2 ?
-
?
additional information hydrolysis of G3T-G5T and G5-G7. Production of trehalose from starch together with isoamylase and maltooligosyltrehalose synthase, overview Saccharolobus solfataricus P2 ?
-
?

Synonyms

Synonyms Comment Organism
maltooligosyltrehalose trehalohydrolase
-
Saccharolobus solfataricus
MTHase
-
Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at Saccharolobus solfataricus