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Literature summary extracted from

  • Jung, J.H.; Seo, D.H.; Holden, J.F.; Kim, H.S.; Baik, M.Y.; Park, C.S.
    Broad substrate specificity of a hyperthermophilic alpha-glucosidase from Pyrobaculum arsenaticum (2016), Food Sci. Biotechnol., 25, 1665-1669 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.20 expression in Escherichia coli Pyrobaculum arsenaticum
3.2.1.216 expression in Escherichia coli Pyrobaculum arsenaticum

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.20 Pyrobaculum arsenaticum A4WMH3
-
-
3.2.1.20 Pyrobaculum arsenaticum DSM 13514 A4WMH3
-
-
3.2.1.216 Pyrobaculum arsenaticum A4WMH3
-
-
3.2.1.216 Pyrobaculum arsenaticum DSM 13514 A4WMH3
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.20 5.84
-
 substrate maltose, pH 5.0, 90°C Pyrobaculum arsenaticum
3.2.1.20 5.84
-
 substrate nigerose, pH 5.0, 90°C Pyrobaculum arsenaticum
3.2.1.216 4.86
-
 pH 5.0, 90°C Pyrobaculum arsenaticum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.20 maltose + H2O
-
 Pyrobaculum arsenaticum 2 D-glucose
-
 ?
3.2.1.20 maltose + H2O
-
 Pyrobaculum arsenaticum DSM 13514 2 D-glucose
-
 ?
3.2.1.20 maltotriose + 2 H2O 44% of the activity with maltose Pyrobaculum arsenaticum 3 D-glucose
-
 ?
3.2.1.20 maltotriose + 2 H2O 44% of the activity with maltose Pyrobaculum arsenaticum DSM 13514 3 D-glucose
-
 ?
3.2.1.20 additional information the enzyme mainly recognizes the non-reducing end of the substrate, releasing the glucose unit. Multifunctional enzyme that catalyzes the hydrolysis of terminal alpha-1,2-linked, alpha-1,3-linked and alpha-1,4-linked glucose residues, e.g. reaction of kojibiose hydrolase Pyrobaculum arsenaticum ?
-
 ?
3.2.1.20 additional information the enzyme mainly recognizes the non-reducing end of the substrate, releasing the glucose unit. Multifunctional enzyme that catalyzes the hydrolysis of terminal alpha-1,2-linked, alpha-1,3-linked and alpha-1,4-linked glucose residues, e.g. reaction of kojibiose hydrolase Pyrobaculum arsenaticum DSM 13514 ?
-
 ?
3.2.1.20 nigerose + H2O
-
 Pyrobaculum arsenaticum 2 D-glucose
-
 ?
3.2.1.20 nigerose + H2O
-
 Pyrobaculum arsenaticum DSM 13514 2 D-glucose
-
 ?
3.2.1.216 kojibiose + H2O
-
 Pyrobaculum arsenaticum alpha-D-glucose + D-glucose
-
 ?
3.2.1.216 additional information the enzyme mainly recognizes the non-reducing end of the substrate, releasing the glucose unit. Multifunctional enzyme that catalyzes also the hydrolysis of terminal alpha-1,4-linked, and alpha-1,3-linked glucose residues, reaction of EC 3.2.1.20 Pyrobaculum arsenaticum ?
-
 ?
3.2.1.216 additional information the enzyme mainly recognizes the non-reducing end of the substrate, releasing the glucose unit. Multifunctional enzyme that catalyzes also the hydrolysis of terminal alpha-1,4-linked, and alpha-1,3-linked glucose residues, reaction of EC 3.2.1.20 Pyrobaculum arsenaticum DSM 13514 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.20 Pars_2044
-
 Pyrobaculum arsenaticum
3.2.1.216 Pars_2044
-
 Pyrobaculum arsenaticum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.20 90
-
-
 Pyrobaculum arsenaticum
3.2.1.216 90
-
-
 Pyrobaculum arsenaticum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.20 80
-
 more than 70% of maximum activity Pyrobaculum arsenaticum
3.2.1.216 80
-
 more than 70% of maximum activity Pyrobaculum arsenaticum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.20 5
-
-
 Pyrobaculum arsenaticum
3.2.1.216 5
-
-
 Pyrobaculum arsenaticum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.20 4 6 more than 90% of maximum activity Pyrobaculum arsenaticum
3.2.1.216 4 6 more than 90% of maximum activity Pyrobaculum arsenaticum