3.2.1.141: 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase
This is an abbreviated version!
For detailed information about 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase, go to the full flat file.
Word Map on EC 3.2.1.141
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3.2.1.141
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sulfolobus
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maltooligosaccharides
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disaccharide
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solfataricus
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starch
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mtsases
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trey
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acidocaldarius
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arthrobacter
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synthesis
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amylolytic
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alpha-1,4-glucosidic
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maltopentaose
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archaebacterium
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food industry
- 3.2.1.141
- sulfolobus
- maltooligosaccharides
- disaccharide
- solfataricus
- starch
- mtsases
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trey
- acidocaldarius
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arthrobacter
- synthesis
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amylolytic
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alpha-1,4-glucosidic
- maltopentaose
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archaebacterium
- food industry
Reaction
Synonyms
4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase, BvMTH, glycosyltrehalose trehalohydrolase, GTHase, malto-oligosyltrehalose trehalohydrolase, maltooligosyl trehalose tetrahydrolase, Maltooligosyl trehalose trehalohydrolase, maltooligosyl trehalose trehalohydrolase (Rhizobium strain M-11 clone pMBTU1 gene treZ reduced), maltooligosyltrehalose trehalohydrolase, maltooligosyltrehalose trehalosidase, MhMTH, MTH, MTHase, ST0926, ST0927, StMTHase, trehalosidase, maltooligosyltrehalose, trehalosidase, maltooligosyltrehalose (Rhizobium strain M-11 clone pBMTU1 gene treZ reduced), TreZ
ECTree
3.2.1.141 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.141 - 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A259S
D156A
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kcat/Km for maltooligosyltrehalose is 3.8fold lower than wild-type value
D252E
mutant shows 0.03% of enzymatic activity compared to the wild-type
D252S
mutant shows 0.6% of enzymatic activity compared to the wild-type
D255A
D380A
E283Q
mutant shows 0.04% of enzymatic activity compared to the wild-type
E286A
E450A
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kcat/Km for maltooligosyltrehalose is 1.2fold lower than wild-type value
F355Y
H195A
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kcat/Km for maltooligosyltrehalose is 357fold lower than wild-type value
R356K
R447A
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kcat/Km for maltooligosyltrehalose is 6.5fold lower than wild-type value
W218A
W218F
Y155A
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kcat/Km for maltooligosyltrehalose is 160fold lower than wild-type value
Y155F
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kcat/Km for maltooligosyltrehalose is 33fold lower than wild-type value
Y328F
D156A
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kcat/Km for maltooligosyltrehalose is 3.8fold lower than wild-type value
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D252E
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mutant shows 0.03% of enzymatic activity compared to the wild-type
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D252S
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mutant shows 0.6% of enzymatic activity compared to the wild-type
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E283Q
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mutant shows 0.04% of enzymatic activity compared to the wild-type
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E450A
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kcat/Km for maltooligosyltrehalose is 1.2fold lower than wild-type value
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H195A
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kcat/Km for maltooligosyltrehalose is 357fold lower than wild-type value
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Y155A
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kcat/Km for maltooligosyltrehalose is 160fold lower than wild-type value
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Y155F
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kcat/Km for maltooligosyltrehalose is 33fold lower than wild-type value
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A259S
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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
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D255A
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site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
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D380A
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site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
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E286A
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site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
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W218A
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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
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additional information
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
A259S
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mutation increases selectivity ratio glucose/trehalose formation
D255A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
D380A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
E286A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
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
F355Y
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mutation increases selectivity ratio glucose/trehalose formation
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
R356K
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mutation increases selectivity ratio glucose/trehalose formation
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
W218A
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mutation decreases selectivity ratio glucose/trehalose formation
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
W218F
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mutation decreases selectivity ratio glucose/trehalose formation
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
Y328F
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mutation increases selectivity ratio glucose/trehalose formation
additional information
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introduction of the trehalose biosynthesis pathway without producing trehalose 6-phosphate as an intermediate in plants: construction of a gene that encodes a bifunctional in-frame fusion (BvMTSH) of maltooligosyltrehalose synthase (BvMTS) and maltooligosyltrehalose trehalohydrolase (BvMTH) from the nonpathogenic bacterium Brevibacterium helvolum to avoid growth inhibition by trehalose 6-phosphate in transgenic Oryzsa sativa subsp. japonica cv. Nakdong plants. Transgenic rice plants that overexpress BvMTSH under the control of the constitutive rice cytochrome c promoter (101MTSH) or the abscisic acid-inducible Ai promoter (105MTSH) show enhanced drought tolerance without growth inhibition, as well as an abscisic acid-hyposensitive phenotype in the roots, overview
additional information
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bifunctional fusion enzyme (MhMTSH) of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH)
additional information
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bifunctional fusion enzyme (MhMTSH) of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH)
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additional information
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bifunctional fusion enzyme (MhMTSH) of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH)
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additional information
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
additional information
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
additional information
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generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
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additional information
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generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
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additional information
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generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
-
additional information
-
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
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