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Literature summary extracted from

  • Jung, J.H.; Seo, D.H.; Holden, J.F.; Park, C.S.
    Maltose-forming alpha-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04 (2014), Appl. Microbiol. Biotechnol., 98, 2121-2131.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.B36
-
 Pyrococcus sp.
3.2.1.133 expressed in Escherichia coli Pyrococcus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.B36 Cd2+
-
 Pyrococcus sp.
3.2.1.B36 Cu2+
-
 Pyrococcus sp.
3.2.1.133 Cd2+
-
 Pyrococcus sp.
3.2.1.133 Cu2+
-
 Pyrococcus sp.
3.2.1.133 maltose competitive Pyrococcus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.B36 0.3
-
 6-O-maltotetraosyl-beta-cyclodextrin pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 8.4
-
 maltotriose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 18.8
-
 maltotetraose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 21.2
-
 maltopentaose pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 8.4
-
 maltotriose pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 18.8
-
 maltotetraose pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 21.2
-
 maltopentaose pH 5.0, 90°C Pyrococcus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.B36 70000
-
 4 * 70000, SDS-PAGE Pyrococcus sp.
3.2.1.B36 260000
-
 gel filtration Pyrococcus sp.
3.2.1.133 70000
-
 4 * 70000, SDS-PAGE Pyrococcus sp.
3.2.1.133 70191
-
 4 * 70191, calculated from sequence Pyrococcus sp.
3.2.1.133 260000
-
 gel filtration Pyrococcus sp.

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.B36 Pyrococcus sp. I3RE04
-
-
3.2.1.B36 Pyrococcus sp. ST04 I3RE04
-
-
3.2.1.133 Pyrococcus sp. I3RE04
-
-
3.2.1.133 Pyrococcus sp. ST04 I3RE04
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.B36
-
 Pyrococcus sp.
3.2.1.133
-
 Pyrococcus sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.133 1.25
-
 pH 5.0, 90°C, substrate: maltotriose Pyrococcus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.B36 4-nitrophenyl alpha-D-maltohexaoside + H2O at an early stage of the reaction only maltose and 4-nitrophenol alpha-D-maltotetraoside, but not maltotetraose are observed. Even as the reaction proceeded, maltotetraose does not appear at all Pyrococcus sp. 4-nitrophenyl alpha-D-maltotetraoside + maltose
-
 ?
3.2.1.B36 6-O-maltosyl-beta-cyclodextrin + H2O
-
 Pyrococcus sp. maltose + beta-cyclodextrin
-
 ?
3.2.1.B36 6-O-maltotetraosyl-beta-cyclodextrin + H2O no formation of matotetraose Pyrococcus sp. 2 maltose + beta-cyclodextrin
-
 ?
3.2.1.B36 maltopentaose + H2O
-
 Pyrococcus sp. 2 maltose + D-glucose
-
 ?
3.2.1.B36 maltotetraose + H2O
-
 Pyrococcus sp. 2 maltose
-
 ?
3.2.1.B36 maltotriose + H2O
-
 Pyrococcus sp. maltose + D-glucose
-
 ?
3.2.1.B36 additional information exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a maltose unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off maltose unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points. 6-O-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant to hydrolysis Pyrococcus sp. ?
-
 ?
3.2.1.133 4-nitrophenyl alpha-D-maltohexaoside + H2O
-
 Pyrococcus sp. 4-nitrophenol + maltohexaose
-
 ?
3.2.1.133 amylopectin + H2O the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities Pyrococcus sp. maltose + ? maltose is the primary end product of hydrolysis ?
3.2.1.133 amylopectin + H2O the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities Pyrococcus sp. ST04 maltose + ? maltose is the primary end product of hydrolysis ?
3.2.1.133 glycogen + H2O the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities Pyrococcus sp. maltose + ? maltose is the primary end product of hydrolysis ?
3.2.1.133 maltopentaose + H2O
-
 Pyrococcus sp. maltose + D-glucose + ?
-
 ?
3.2.1.133 maltotetraose + H2O
-
 Pyrococcus sp. 2 maltose
-
 ?
3.2.1.133 maltotetraose + H2O
-
 Pyrococcus sp. ST04 2 maltose
-
 ?
3.2.1.133 maltotriose + H2O highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin Pyrococcus sp. maltose + D-glucose
-
 ?
3.2.1.133 maltotriose + H2O highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin Pyrococcus sp. ST04 maltose + D-glucose
-
 ?
3.2.1.133 additional information an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points Pyrococcus sp. ?
-
 ?
3.2.1.133 additional information an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points Pyrococcus sp. ST04 ?
-
 ?
3.2.1.133 starch + H2O the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities Pyrococcus sp. maltose + ? maltose is the primary end product of hydrolysis ?
3.2.1.133 starch + H2O the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities Pyrococcus sp. ST04 maltose + ? maltose is the primary end product of hydrolysis ?

Subunits

EC Number Subunits Comment Organism
3.2.1.B36 homotetramer 4 * 70000, SDS-PAGE Pyrococcus sp.
3.2.1.133 homotetramer 4 * 70000, SDS-PAGE Pyrococcus sp.
3.2.1.133 homotetramer 4 * 70191, calculated from sequence Pyrococcus sp.

Synonyms

EC Number Synonyms Comment Organism
3.2.1.B36 PSMA
-
 Pyrococcus sp.
3.2.1.B36 Py04_0872 locus name Pyrococcus sp.
3.2.1.133 PSMA Pyrococcus sp. ST04 maltose-forming alpha-amylase Pyrococcus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.B36 90
-
 assay at Pyrococcus sp.
3.2.1.B36 90 95
-
 Pyrococcus sp.
3.2.1.133 90 95
-
 Pyrococcus sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.B36 70
-
 about 55% of maximal activity Pyrococcus sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.B36 75
-
 half-life: 254 min Pyrococcus sp.
3.2.1.B36 85
-
 half-life: 72 min Pyrococcus sp.
3.2.1.133 75
-
 half-life: 254 min Pyrococcus sp.
3.2.1.133 85
-
 half-life: 72 min Pyrococcus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.B36 0.0017
-
 maltopentaose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 0.0033
-
 maltotetraose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 6.35
-
 maltotriose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 25.75
-
 6-O-maltotetraosyl-beta-cyclodextrin pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 0.0017
-
 maltopentaose pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 0.0033
-
 maltotetraose pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 6.35
-
 maltotriose pH 5.0, 90°C Pyrococcus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.B36 5
-
-
 Pyrococcus sp.
3.2.1.133 5
-
 substrate: maltotriose Pyrococcus sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.B36 4 6 pH 4.0: less than 10% of maximal activity, pH 6.0: about 40% of maximal activity Pyrococcus sp.
3.2.1.133 4 6 pH 4.0: less than 10% of maximal activity, pH 6.0: about 40% of maximal activity Pyrococcus sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.133 0.7
-
 maltose pH 5.0, 90°C Pyrococcus sp.

General Information

EC Number General Information Comment Organism
3.2.1.133 physiological function the enzyme may have a role in regulating the concentration of maltose during maltodextrin metabolism Pyrococcus sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.B36 0.000078
-
 maltopentaose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 0.00018
-
 maltotetraose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 0.76
-
 maltotriose pH 5.0, 90°C Pyrococcus sp.
3.2.1.B36 85.8
-
 6-O-maltotetraosyl-beta-cyclodextrin pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 0.000078
-
 maltopentaose pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 0.000193
-
 maltotetraose pH 5.0, 90°C Pyrococcus sp.
3.2.1.133 0.76
-
 maltotriose pH 5.0, 90°C Pyrococcus sp.