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Literature summary extracted from

  • Kaper, T.; Leemhuis, H.; Uitdehaag, J.C.; van der Veen, B.A.; Dijkstra, B.W.; van der Maarel, M.J.; Dijkhuizen, L.
    Identification of acceptor substrate binding subsites +2 and +3 in the amylomaltase from Thermus thermophilus HB8 (2007), Biochemistry, 46, 5261-5269.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.25 D293A site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus
2.4.1.25 D293N site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus
2.4.1.25 D294S site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus
2.4.1.25 D395A site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus
2.4.1.25 D395N site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus
2.4.1.25 E340A site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus
2.4.1.25 E340Q site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus
2.4.1.25 F366L site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme Thermus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.25 acarbose a strong mixed inhibitor with almost equal competitive and uncompetitive binding constants, acarbose is both bound in the active site and at another site Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.25 additional information
-
additional information kinetics of wild-type and mutant enzymes at pH 6.5 and 70°C, overview Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.25 59337
-
x * 59337, sequence calculation Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.25 additional information Thermus thermophilus Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily ?
-
?
2.4.1.25 additional information Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.25 Thermus thermophilus O87172
-
-
2.4.1.25 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 O87172
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.25 maltoheptaose + maltoheptaose
-
Thermus thermophilus ?
-
?
2.4.1.25 maltoheptaose + maltoheptaose
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?
2.4.1.25 maltohexaose + maltohexaose
-
Thermus thermophilus ?
-
?
2.4.1.25 maltohexaose + maltohexaose
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?
2.4.1.25 maltopentaose + maltopentaose
-
Thermus thermophilus ?
-
?
2.4.1.25 maltopentaose + maltopentaose
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?
2.4.1.25 maltotetraose + maltotetraose
-
Thermus thermophilus ?
-
?
2.4.1.25 maltotriose + maltotriose
-
Thermus thermophilus glucose + maltooligosaccharides
-
?
2.4.1.25 additional information Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily Thermus thermophilus ?
-
?
2.4.1.25 additional information substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview Thermus thermophilus ?
-
?
2.4.1.25 additional information Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?
2.4.1.25 additional information substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?

Subunits

EC Number Subunits Comment Organism
2.4.1.25 ? x * 59337, sequence calculation Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
2.4.1.25 AMase
-
Thermus thermophilus
2.4.1.25 amylomaltase
-
Thermus thermophilus
2.4.1.25 More the enzyme belongs to the glycoside hydrolase family 77, GH77, which belongs to the alpha-amylase superfamily, Clan H, together with GH13 and GH70 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.25 70
-
assay at Thermus thermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.4.1.25 50 90
-
Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.25 80
-
stable up to at pH 5.5, half-life is 18 min Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.25 0.68
-
maltotriose pH 5.5, 70°C, mutant D249S Thermus thermophilus
2.4.1.25 0.97
-
maltotetraose pH 5.5, 70°C, mutant D249S Thermus thermophilus
2.4.1.25 1.99
-
maltoheptaose pH 5.5, 70°C, mutant D249S Thermus thermophilus
2.4.1.25 3.26
-
maltohexaose pH 5.5, 70°C, mutant D249S Thermus thermophilus
2.4.1.25 3.98
-
maltopentaose pH 5.5, 70°C, mutant D249S Thermus thermophilus
2.4.1.25 106
-
maltotetraose pH 5.5, 70°C, mutant F366L Thermus thermophilus
2.4.1.25 111
-
maltotriose pH 5.5, 70°C, mutant F366L Thermus thermophilus
2.4.1.25 159
-
maltoheptaose pH 5.5, 70°C, mutant F366L Thermus thermophilus
2.4.1.25 179
-
maltopentaose pH 5.5, 70°C, mutant F366L Thermus thermophilus
2.4.1.25 188
-
maltohexaose pH 5.5, 70°C, mutant F366L Thermus thermophilus
2.4.1.25 213
-
maltoheptaose pH 5.5, 70°C, wild-type enzyme Thermus thermophilus
2.4.1.25 304
-
maltohexaose pH 5.5, 70°C, wild-type enzyme Thermus thermophilus
2.4.1.25 317
-
maltotriose pH 5.5, 70°C, wild-type enzyme Thermus thermophilus
2.4.1.25 329
-
maltopentaose pH 5.5, 70°C, wild-type enzyme Thermus thermophilus
2.4.1.25 425
-
maltotetraose pH 5.5, 70°C, wild-type enzyme Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.25 5.5
-
assay at Thermus thermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.25 4 7.5 pH dependence of wild-type and mutant enzymes, D293N and E340Q are active below pH 6.5 and pH 5.5, respectively, but precipitate during the necessary prolonged incubation times, wild-type Tt AMase precipitates below pH 5.5 under similar extended incubation times as well, overview Thermus thermophilus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.4.1.25 4 7.5 pH stability of wild-type and mutant enzymes, overview Thermus thermophilus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.1.25 0.003
-
acarbose pH 5.5, 70°C, competitive inhibition Thermus thermophilus
2.4.1.25 0.004
-
acarbose pH 5.5, 70°C, uncompetitive inhibition Thermus thermophilus