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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.141 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
3.2.1.141 D255A site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase Saccharolobus solfataricus
3.2.1.141 D380A site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase Saccharolobus solfataricus
3.2.1.141 E286A site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase Saccharolobus solfataricus
3.2.1.141 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
3.2.1.141 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
3.2.1.141 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
3.2.1.141 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
3.2.1.141 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]

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.141 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 ?
-
 ?
3.2.1.141 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

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.141 0.1
-
 mutant D380 Saccharolobus solfataricus
3.2.1.141 0.74
-
 mutant E286A Saccharolobus solfataricus
3.2.1.141 1.23
-
 mutant D255A Saccharolobus solfataricus
3.2.1.141 5.31
-
 mutant W218A Saccharolobus solfataricus
3.2.1.141 52
-
 mutant W218F Saccharolobus solfataricus
3.2.1.141 472
-
 mutant R356K Saccharolobus solfataricus
3.2.1.141 492
-
 mutant Y328F Saccharolobus solfataricus
3.2.1.141 597
-
 mutant F355Y Saccharolobus solfataricus
3.2.1.141 787
-
 mutant A259S Saccharolobus solfataricus
3.2.1.141 814
-
 wild-type enzyme Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.141 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 ?
-
 ?
3.2.1.141 additional information hydrolysis of G3T-G5T and G5-G7. Production of trehalose from starch together with isoamylase and maltooligosyltrehalose synthase, overview Saccharolobus solfataricus ?
-
 ?
3.2.1.141 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 ?
-
 ?
3.2.1.141 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

EC Number Synonyms Comment Organism
3.2.1.141 maltooligosyltrehalose trehalohydrolase
-
 Saccharolobus solfataricus
3.2.1.141 MTHase
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.141 60
-
 assay at Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.141 5
-
 assay at Saccharolobus solfataricus