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Literature summary extracted from

  • Li, D.; Park, J.T.; Li, X.; Kim, S.; Lee, S.; Shim, J.H.; Park, S.H.; Cha, J.; Lee, B.H.; Kim, J.W.; Park, K.H.
    Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100 degrees C, from the hyperthermophilic archaeon Staphylothermus marinus (2010), New Biotechnol., 27, 300-307.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.B8 food industry the enzyme might be of potential value in the food and starch industries due to its extreme thermostability Staphylothermus marinus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.B8 phylogenetic tree, overexpression of C-terminally [Leu-Glu-(His)6]-tagged SMMA in Escherichia coli Staphylothermus marinus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.133 additional information tapioca starch is modified using branching enzyme, BE, isolated from, Bacillus subtilis strain 168, and Bacillus stearothermophilus maltogenic amylase, BSMA. BE cleaves alpha-1,4 linkages of amylose and amylopectin, and moiety of glycosyl residues are transferred to another amylose and amylopectin to produce branched glucan and branching enzyme-treated tapioca starch by forming alpha-1,6 branch linkages. The product is further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points, overview Geobacillus stearothermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.B8 82500
-
 2 * 82500, recombinant [Leu-Glu-(His)6]-tagged enzyme, SDS-PAGE, 2 * 83600, about, recombinant [Leu-Glu-(His)6]-tagged enzyme, mass spectrometry Staphylothermus marinus
3.2.1.B8 83600
-
 2 * 82500, recombinant [Leu-Glu-(His)6]-tagged enzyme, SDS-PAGE, 2 * 83600, about, recombinant [Leu-Glu-(His)6]-tagged enzyme, mass spectrometry Staphylothermus marinus
3.2.1.B8 173000
-
 recombinant tagged enzyme, sedimentation equilibrium analytical ultracentrifugation Staphylothermus marinus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.B8 acarbose + 2 H2O Staphylothermus marinus
-
 acarviosine + 2 D-glucose
-
 ?
3.2.1.B8 alpha-cyclodextrin + H2O Staphylothermus marinus
-
 maltose + D-glucose primary products ?
3.2.1.B8 beta-cyclodextrin + H2O Staphylothermus marinus
-
 maltose + D-glucose primary products ?
3.2.1.B8 cycloamylose + H2O Staphylothermus marinus
-
 maltose + D-glucose primary products ?
3.2.1.B8 gamma-cyclodextrin + H2O Staphylothermus marinus
-
 maltose + D-glucose primary products ?
3.2.1.B8 linear maltoheptaose + H2O Staphylothermus marinus SMMA preferentially hydrolyzed the first and second glycosidic bonds from the reducing end maltose + D-glucose primary products ?
3.2.1.B8 linear maltohexaose + H2O Staphylothermus marinus best substrate maltose + D-glucose primary products ?
3.2.1.B8 linear maltooligosaccharide + H2O Staphylothermus marinus maximal activity of SMMA toward G6, but almost no activity toward G3 maltose + D-glucose primary products ?
3.2.1.B8 pullulan + H2O Staphylothermus marinus
-
 panose + D-glucose
-
 ?
3.2.1.B8 starch + H2O Staphylothermus marinus
-
 maltose + D-glucose primary products ?
3.2.1.133 additional information Geobacillus stearothermophilus BSMA preferentially hydrolyzes longer branch chains, releasing maltose and glucose from the non-reducing end of the branch chains, and transfers the resulting maltooligosaccharides to the non-reducing ends of the shorter branch chains by forming alpha-1,6-glucosidic linkages ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.B8 Staphylothermus marinus
-
-
-
3.2.1.133 Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.B8 recombinant His-tagged SMMA 34.8fold from Escherichia coli by heat treatment at 70°C for 20 min, and nickel affinity chromatography, to homogeneity Staphylothermus marinus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.B8 hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the reducing ends of the chains hydrolysis to D-glucose and maltose Staphylothermus marinus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.B8 1.13
-
 crude recombinant enzyme in Escherichia coli cell extract, substrate gamma-cyclodextrin Staphylothermus marinus
3.2.1.B8 39.3
-
 purified recombinant enzyme Staphylothermus marinus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.B8 acarbose + 2 H2O
-
 Staphylothermus marinus acarviosine + 2 D-glucose
-
 ?
3.2.1.B8 alpha-cyclodextrin + H2O
-
 Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.B8 beta-cyclodextrin + H2O
-
 Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.B8 cycloamylose + H2O
-
 Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.B8 gamma-cyclodextrin + H2O
-
 Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.B8 linear maltoheptaose + H2O SMMA preferentially hydrolyzed the first and second glycosidic bonds from the reducing end Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.B8 linear maltohexaose + H2O best substrate Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.B8 linear maltooligosaccharide + H2O maximal activity of SMMA toward G6, but almost no activity toward G3 Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.B8 additional information SMMA hydrolyzes linear maltooligosaccharides, starch, cyclodextrins, and cycloamylose, primarily to maltose and glucose, and shows highest activity toward acarbose and pullulan, hydrolyzed to acarviosine-glucose and panose, respectively. Product analysis, overview Staphylothermus marinus ?
-
 ?
3.2.1.B8 pullulan + H2O
-
 Staphylothermus marinus panose + D-glucose
-
 ?
3.2.1.B8 starch + H2O
-
 Staphylothermus marinus maltose + D-glucose primary products ?
3.2.1.133 additional information BSMA preferentially hydrolyzes longer branch chains, releasing maltose and glucose from the non-reducing end of the branch chains, and transfers the resulting maltooligosaccharides to the non-reducing ends of the shorter branch chains by forming alpha-1,6-glucosidic linkages Geobacillus stearothermophilus ?
-
 ?
3.2.1.133 additional information the enzyme forms highly branched products from branched glucan and branching enzyme-treated tapioca starch Geobacillus stearothermophilus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.B8 dimer 2 * 82500, recombinant [Leu-Glu-(His)6]-tagged enzyme, SDS-PAGE, 2 * 83600, about, recombinant [Leu-Glu-(His)6]-tagged enzyme, mass spectrometry Staphylothermus marinus
3.2.1.B8 More in SMMA, non-polar side chains at 357W, 408W, 449Y, 451W, 463Y, 490Y, 501Y, 517Y 519Y, 529Y, 593W, and 608Y are located at the termini of alpha-helixes and beta-sheets contributing to the extreme thermostability of the enzyme Staphylothermus marinus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.B8 maltogenic amylase
-
 Staphylothermus marinus
3.2.1.B8 More the enzyme belongs to the family 13 glycosyl hydrolase, GH13 Staphylothermus marinus
3.2.1.B8 SMMA
-
 Staphylothermus marinus
3.2.1.133 BSMA
-
 Geobacillus stearothermophilus
3.2.1.133 maltogenic amylase
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.B8 100
-
-
 Staphylothermus marinus
3.2.1.133 50
-
 assay at Geobacillus stearothermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.B8 85 110
-
 Staphylothermus marinus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.B8 additional information
-
 in SMMA, non-polar side chains at 357W, 408W, 449Y, 451W, 463Y, 490Y, 501Y, 517Y 519Y, 529Y, 593W, and 608Y are located at the termini of alpha-helixes and beta-sheets contributing to the extreme thermostability of the enzyme Staphylothermus marinus
3.2.1.B8 20 130 differential scanning calorimetric analysis of SMMA, profile, overview Staphylothermus marinus
3.2.1.B8 100 109 the enzyme is extremely thermostable, with a temperature optimum of 100°C and a melting temperature of 109°C Staphylothermus marinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.B8 5
-
-
 Staphylothermus marinus
3.2.1.133 6
-
 assay at Geobacillus stearothermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.B8 3.5 5 activity range, 52% and 90% of maximal activity at pH 3.5 and pH 4.0, respectively Staphylothermus marinus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.B8 5 10 purified recombinant SMMA shows excellent stability over the pH range of 5.0-10, when incubated at 37 8C for 24 h Staphylothermus marinus