Information on EC 5.3.1.26 - galactose-6-phosphate isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.1.26
-
RECOMMENDED NAME
GeneOntology No.
galactose-6-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Galactose 6-phosphate = D-tagatose 6-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lactose and galactose degradation I
-
-
metabolism of disaccharids
-
-
Galactose metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
D-galactose-6-phosphate aldose-ketose-isomerase
Involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
39433-98-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
C7TG25
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme participates in galactose metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 D-lyxose
D-xylulose + D-xylose
show the reaction diagram
-
-
-
r
2 D-psicose
D-allose + D-altrose
show the reaction diagram
-
-
-
r
2 L-lyxose
L-xylulose + L-xylose
show the reaction diagram
-
-
-
r
D-allose
D-piscose + D-altrose
show the reaction diagram
-
-
-
r
D-Allose
D-Psicose
show the reaction diagram
D-altrose
D-psicose + D-allose
show the reaction diagram
-
-
-
r
D-arabinose
D-ribulose + D-ribose
show the reaction diagram
-
-
-
r
D-fructose
D-glucose + D-mannose
show the reaction diagram
-
-
-
r
D-galactose
D-tagatose + D-talose
show the reaction diagram
-
-
-
r
D-Galactose 6-phosphate
?
show the reaction diagram
D-Galactose 6-phosphate
D-Tagatose 6-phosphate
show the reaction diagram
D-glucose
D-fructose + D-mannose
show the reaction diagram
-
-
-
r
D-glucose
D-sorbose + D-idose
show the reaction diagram
-
-
-
r
D-mannose
D-fructose + D-glucose
show the reaction diagram
-
-
-
r
D-psicose
D-allose + D-altrose
show the reaction diagram
-
-
the enzyme produces significant quantities of D-altrose as a byproduct
-
r
D-Ribose
D-Ribulose
show the reaction diagram
C7TG25;
-
-
-
?
D-ribose
D-ribulose + D-arabinose
show the reaction diagram
-
-
-
r
D-ribulose
D-ribose + D-arabinose
show the reaction diagram
-
-
-
r
D-sorbose
D-glucose + D-idose
show the reaction diagram
-
-
-
r
D-talose
D-tagatose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
D-xylulose
D-xylose + D-lyxose
show the reaction diagram
-
-
-
r
L-fructose
L-glucose + L-mannose
show the reaction diagram
-
-
-
r
L-galactose
L-tagatose + L-talose
show the reaction diagram
-
-
-
r
L-glucose
L-fructose
show the reaction diagram
-
-
-
r
L-ribulose
L-ribose + L-arabinose
show the reaction diagram
-
-
-
r
L-tagatose
L-galactose + L-talose
show the reaction diagram
-
-
-
r
L-Xylose
L-Xylulose
show the reaction diagram
-
-
-
r
L-xylulose
L-xylose + L-lyxose
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Galactose 6-phosphate
?
show the reaction diagram
D-Galactose 6-phosphate
D-Tagatose 6-phosphate
show the reaction diagram
C7TG25
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
58
D-Allose
143
D-altrose
-
9.6
D-galactose-6-phosphate
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-
1.9
D-tagatose 6-phosphate
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
D-Allose
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pH 7.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028
D-Allose
-
pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.79
of the purified enzyme to produce D-allose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2 - 9.2
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
99000 - 100000
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sucrose density gradient centrifugation, gel filtration
135500
native enzyme by gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 15000 + x * 19000, SDS-PAGE
heterotetramer
C7TG25;
2 * 19000 + 1 * 15000, SDS-PAGE
octamer
hetero-octamer, LacA and LacB subunits
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with D-tagatose-6-phosphate, hanging drop vapor diffusion method, using 0.2 M potassium formate containing 20% (w/v) PEG 3350
C7TG25;
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
completely unstable at pH values below pH 6.5
2699
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes the enzyme during purification
-
completely unstable to freezing in phosphate buffer, pH 7.5, even in the presence of 15% v/v glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
C7TG25;
of the recombinant protein by HiTrap Q HP column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
C7TG25;
expression of both lacA and lacB is required to obtain galactose-6-phosphate isomerase activity
-
overexpression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C65A
C7TG25;
inactive
D8N
C7TG25;
inactive
H96A
C7TG25;
the mutant exhibits 25fold lower activity compared with the wild type enzyme activity
H9A
C7TG25;
inactive
N97A
C7TG25;
the mutant has an activity level of approximately 30% that of the wild type enzyme
T67A
C7TG25;
the catalytic activity of the mutant is approximately 20fold lower than that of the wild type enzyme
D158G
-
mutation enhances the activity of the enzyme by more than 20%
F160S
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mutation enhances the activity of the enzyme by more than 20%
G132D
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mutation enhances the activity of the enzyme by more than 20%
V54A
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mutation enhances the activity of the enzyme by more than 20%
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