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Literature summary for 3.2.1.133 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)

Cloned (Comment) Organism
expressed in Escherichia coli Pyrococcus sp.

Inhibitors

Inhibitors Comment Organism Structure
Cd2+
-
Pyrococcus sp.
Cu2+
-
Pyrococcus sp.
maltose competitive Pyrococcus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8.4
-
maltotriose pH 5.0, 90°C Pyrococcus sp.
18.8
-
maltotetraose pH 5.0, 90°C Pyrococcus sp.
21.2
-
maltopentaose pH 5.0, 90°C Pyrococcus sp.

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Pyrococcus sp. I3RE04
-
-
Pyrococcus sp. ST04 I3RE04
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus sp.

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-maltohexaoside + H2O
-
Pyrococcus sp. 4-nitrophenol + maltohexaose
-
?
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 ?
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 ?
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 ?
maltopentaose + H2O
-
Pyrococcus sp. maltose + D-glucose + ?
-
?
maltotetraose + H2O
-
Pyrococcus sp. 2 maltose
-
?
maltotetraose + H2O
-
Pyrococcus sp. ST04 2 maltose
-
?
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
-
?
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
-
?
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. ?
-
?
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 ?
-
?
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 ?
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

Subunits Comment Organism
homotetramer 4 * 70000, SDS-PAGE Pyrococcus sp.
homotetramer 4 * 70191, calculated from sequence Pyrococcus sp.

Synonyms

Synonyms Comment Organism
PSMA Pyrococcus sp. ST04 maltose-forming alpha-amylase Pyrococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90 95
-
Pyrococcus sp.

Temperature Stability [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0017
-
maltopentaose pH 5.0, 90°C Pyrococcus sp.
0.0033
-
maltotetraose pH 5.0, 90°C Pyrococcus sp.
6.35
-
maltotriose pH 5.0, 90°C Pyrococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
substrate: maltotriose Pyrococcus sp.

pH Range

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

Ki Value [mM]

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

General Information

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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.000078
-
maltopentaose pH 5.0, 90°C Pyrococcus sp.
0.000193
-
maltotetraose pH 5.0, 90°C Pyrococcus sp.
0.76
-
maltotriose pH 5.0, 90°C Pyrococcus sp.