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
Galactose metabolism
-
-
lactose and galactose degradation I
-
-
Metabolic pathways
-
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metabolism of disaccharids
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
C7TG25
UniProt
Manually annotated by BRENDA team
strain NCTC8511
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-
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
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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
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-
-
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
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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
Lactococcus lactis
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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
Lactococcus lactis
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pH 7.0, 30°C
945
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
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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
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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
-
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
-
mutation enhances the activity of the enzyme by more than 20%
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