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Literature summary extracted from

  • Oh, S.W.; Jang, M.U.; Jeong, C.K.; Kang, H.J.; Park, J.M.; Kim, T.J.
    Modulation of hydrolysis and transglycosylation activity of Thermus maltogenic amylase by combinatorial saturation mutagenesis (2008), J. Microbiol. Biotechnol., 18, 1401-1407.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.133 biotechnology producing enzymes with modified substrate specificity, hydrolysis, and transglycosilation activities, as a way to produce specific functional carbohydrate materials Thermus sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.133 cloning and expression in Escherichia coli MC 1061 with p6xHTMX, transformants grown in Luria-Bertani medium with ampicillin at 37°C Thermus sp.

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 A330G/N331C/E332C F-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 A330G/N331G/E332C C-20, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 A330G/N331G/E332G G-91, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose Thermus sp.
3.2.1.133 A330G/N331G/E332S G-22, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 A330G/N331P/E332G C-43, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 A330G/N331V/E332G G-90, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 A330M/N331G/E332C B-96, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 A330S/N331A F-80, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose Thermus sp.
3.2.1.133 A330S/N331G/E332T K-37, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodexxtrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 additional information Random substitutions of amino acid residues Val329, Ala330, Asn331, and Glu332 that are forming an extra sugar-binding space with combinatorial saturation mutagenesis technique: substrate specificity, hydrolysis pattern, and transglycosylation activity of ThMA are modulated by these mutations. Activity assays with substrates: soluble starch, pullulan, beta-cyclodextrin, maltotriose, and acarbose at 60°C, pH 6.0 sodium-acetate buffer Thermus sp.
3.2.1.133 N331S/E332G I-69, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329A/A330C/N331G/E332V A-39, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329A/A330G/N331V/E332A G-13, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329A/N331L B-4, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type Thermus sp.
3.2.1.133 V329C/N331H/E332R D-3, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329F/A330T/N331G/E332W I-70, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329G/A330L/N331V/E332Y H-16, slightly higher activity with cyclodextrin, pullulan, and starch, reduced activities with maltotriose, and acarbose, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type, similar transglysocylation pattern as wild-type Thermus sp.
3.2.1.133 V329I/A330G/N331W C-56, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329S/A330C/N331S/E332P A-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329S/A330G/N331D K-33, strong reduction of all substrate hydrolyzing activities, products of acarbose hydrolization are glucose, maltose, and acarviosine instead of only glucose and carviosine-glucose as in the wild-type reaction, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: very little amount of transfer products, with acarbose significant amount of acarviosine and maltose Thermus sp.
3.2.1.133 V329S/A330G/N331G/E332V E-74, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.
3.2.1.133 V329T/A330C/N331T/E332V E-50, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type Thermus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.133 acarbose + H2O Thermus sp.
-
 glucose + acarviosine-glucose
-
 ?
3.2.1.133 alpha-(1,4)-glycosidic linked cyclodextrins + H2O Thermus sp. main depolymerization of outer amylopectin branches maltooligosaccharide
-
 ?
3.2.1.133 beta-cyclodextrin + H2O Thermus sp.
-
 maltooligosaccharide
-
 ?
3.2.1.133 maltotriose + H2O Thermus sp.
-
 isomaltose + isopanose + panose + branched glucooligosaccharides transfer products of transglycosylation ?
3.2.1.133 pullulan + H2O Thermus sp.
-
 panose + ?
-
 ?
3.2.1.133 starch + H2O Thermus sp.
-
 maltooligosaccharide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.133 Thermus sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.133 purification of ThMA variants with N-terminal six-histidines by nickel-nitrilotriacetic acid column chromatography Thermus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.133 acarbose + H2O
-
 Thermus sp. glucose + acarviosine-glucose
-
 ?
3.2.1.133 alpha-(1,4)-glycosidic linked cyclodextrins + H2O main depolymerization of outer amylopectin branches Thermus sp. maltooligosaccharide
-
 ?
3.2.1.133 beta-cyclodextrin + H2O
-
 Thermus sp. maltooligosaccharide
-
 ?
3.2.1.133 maltotriose + H2O
-
 Thermus sp. isomaltose + isopanose + panose + branched glucooligosaccharides transfer products of transglycosylation ?
3.2.1.133 pullulan + H2O
-
 Thermus sp. panose + ?
-
 ?
3.2.1.133 starch + H2O
-
 Thermus sp. maltooligosaccharide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.133 maltogenic alpha-amylase
-
 Thermus sp.
3.2.1.133 Thermus maltogenic amylase hydrolyzes cyclodextrin faster than starch Thermus sp.
3.2.1.133 ThMA
-
 Thermus sp.