Information on EC 3.2.1.B32 - kojibiose hydrolase

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The expected taxonomic range for this enzyme is: Sulfolobus acidocaldarius

EC NUMBER
COMMENTARY hide
3.2.1.B32
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
kojibiose hydrolase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
kojibiose + H2O
alpha-D-glucose
show the reaction diagram
i.e. alpha-D-Glc-(1->2)-D-Glc. Multifunctional enzyme that catalyzes also the hydrolysis of terminal alpha-1,4-linked, alpha-1,3-linked and alpha-1,6-linked glucose residues (EC 3.2.1.20/EC 3.2.1.84/EC 3.2.1.10)
-
-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
12 * 72000, SDS-PAGE
73000
12 * 73000, calculated from sequence
914000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
12 * 72000, SDS-PAGE; 12 * 73000, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
half-life: 33.8 h
100
half-life: 10.6 h
105
half-life: 1.8 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stored for at least 6 months without any loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Sulfolobus acidocaldarius. Attempts to obtain soluble enzyme from Escherichia coli strains are unsuccessful
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium