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Literature summary for 3.2.1.84 extracted from

  • Choi, K.H.; Hwang, S.; Cha, J.
    Identification and characterization of MalA in the maltose/maltodextrin operon of Sulfolobus acidocaldarius DSM639 (2013), J. Bacteriol., 195, 1789-1799.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.84

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Sulfolobus acidocaldarius. Attempts to obtain soluble enzyme from Escherichia coli strains are unsuccessful Sulfolobus acidocaldarius

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
 Sulfolobus acidocaldarius 5622
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
 12 * 72000, SDS-PAGE Sulfolobus acidocaldarius
73000
-
 12 * 73000, calculated from sequence Sulfolobus acidocaldarius
914000
-
 gel filtration Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q4J9M3
-
-
Sulfolobus acidocaldarius DSM 639 Q4J9M3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sulfolobus acidocaldarius

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:maltose-grown cell the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 11fold higher during growth in YT medium (Brock’s mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing maltose, than during growth on other sugars Sulfolobus acidocaldarius
-
culture condition:starch-grown cell the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 10fold higher during growth in YT medium (Brock’s mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing starch, than during growth on other sugars Sulfolobus acidocaldarius
-

Storage Stability

Storage Stability Organism
4°C, stored for at least 6 months without any loss of activity Sulfolobus acidocaldarius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nigerose + H2O i.e. alpha-D-Glc-(1->3)-D-Glc. The multifunctional enzyme also catalyzes the hydrolysis of terminal alpha-1,4-linked, alpha-1,2-linked and alpha-1,6-linked glucose residues (EC 3.2.1.20/kojibiose/EC 3.2.1.10 hydrolase) Sulfolobus acidocaldarius alpha-D-glucose + D-glucose
-
 ?
nigerose + H2O i.e. alpha-D-Glc-(1->3)-D-Glc. The multifunctional enzyme also catalyzes the hydrolysis of terminal alpha-1,4-linked, alpha-1,2-linked and alpha-1,6-linked glucose residues (EC 3.2.1.20/kojibiose/EC 3.2.1.10 hydrolase) Sulfolobus acidocaldarius DSM 639 alpha-D-glucose + D-glucose
-
 ?

Subunits

Subunits Comment Organism
dodecamer 12 * 72000, SDS-PAGE Sulfolobus acidocaldarius
dodecamer 12 * 73000, calculated from sequence Sulfolobus acidocaldarius

Synonyms

Synonyms Comment Organism
MalA
-
 Sulfolobus acidocaldarius
Saci1160 locus name Sulfolobus acidocaldarius

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
95
-
 half-life: 33.8 h Sulfolobus acidocaldarius
100
-
 half-life: 10.6 h Sulfolobus acidocaldarius
105
-
 half-life: 1.8 h Sulfolobus acidocaldarius

pI Value

Organism Comment pI Value Maximum pI Value
Sulfolobus acidocaldarius calculated from sequence
-
 5.9

Expression

Organism Comment Expression
Sulfolobus acidocaldarius the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium up