Information on EC 5.1.3.3 - Aldose 1-epimerase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.1.3.3
-
RECOMMENDED NAME
GeneOntology No.
Aldose 1-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-Glucose = beta-D-glucose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
D-galactose degradation I (Leloir pathway)
-
-
D-galactose degradation V (Leloir pathway)
-
-
Galactose metabolism
-
-
Glycolysis / Gluconeogenesis
-
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Metabolic pathways
-
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Microbial metabolism in diverse environments
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trehalose degradation VI (periplasmic)
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starch degradation
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SYSTEMATIC NAME
IUBMB Comments
Aldose 1-epimerase
Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. This enzyme catalyses the first step in galactose metabolism by converting beta-D-galactose into alpha-D-galactose, which is the substrate for EC 2.7.1.6, galactokinase [5,6].
CAS REGISTRY NUMBER
COMMENTARY hide
9031-76-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
green pepper
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
subsp. cremonis MG1363
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Mushroom
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity. The active sites for the two enzymatic activities are located in different regions of the epimerase homoenzyme
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-Fucose
beta-D-Fucose
show the reaction diagram
alpha-D-Galactose
beta-D-Galactose
show the reaction diagram
alpha-D-Glucose
beta-D-Glucose
show the reaction diagram
alpha-D-Glycero-D-galactoheptopyranose
beta-D-Glycero-D-galactoheptopyranose
show the reaction diagram
alpha-D-Xylose
beta-D-Xylose
show the reaction diagram
alpha-L-Arabinose
beta-L-Arabinose
show the reaction diagram
beta-D-Cellobiose
?
show the reaction diagram
beta-D-Fructose
alpha-D-Fructose
show the reaction diagram
-
135% of the activity relative to alpha-D-glucose
-
-
beta-Glucose 6-phosphate
alpha-Glucose-6-phosphate
show the reaction diagram
-
-
-
-
beta-Lactose
alpha-Lactose
show the reaction diagram
beta-Maltose
alpha-Maltose
show the reaction diagram
additional information
?
-
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
alpha-D-Glucose
beta-D-Glucose
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,5-Anhydro-D-fructose
-
slight inhibition
1,5-Anhydro-D-glucitol
-
slight inhibition
2-deoxy-D-galactose
-
competitive
2-deoxy-D-glucose
-
competitive
2-deoxy-D-ribose
-
competitive
3-O-methyl-D-glucose
-
competitive
Ag+
-
-
alpha-methyl-D-glucoside
alpha-O-Methylglycoside
-
-
beta-Methyl-D-xyloside
-
competitive
Cd2+
-
-
cellobiose
Co2+
-
-
Cu2+
-
-
D-Allose
-
competitive
D-arabinose
-
competitive
D-erythrose
-
competitive
D-fructose
-
-
D-fucose
-
competitive
D-Galactono-gamma-lactone
-
-
D-galactose
D-galacturonic acid
-
competitive
D-glucono-1,5-lactone
-
-
D-glucuronic acid
-
competitive
D-Inositol
-
competitive
D-maltose
D-mannitol
-
competitive
D-melibiose
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competitive
D-ribose
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competitive
D-sorbitol
-
competitive
D-xylitol
-
competitive
D-xylose
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competitive
diethylstilbestrol
-
-
DL-glyceraldehyde
-
-
erythritol
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competitive
estriol
-
-
estrone
-
-
galactitol
-
competitive
L-arabinose
L-arabitol
-
competitive
L-fucose
-
competitive
L-Glucose
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competitive
L-Xylose
N-Acetylimidazole
-
-
N-bromosuccinimide
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-
Pb2+
-
-
PCMB
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-
phloretin
phlorizin
progesterone
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weak
Zn2+
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
alpha-D-Fucose
10 - 37
alpha-D-galactose
5 - 180
alpha-D-glucose
8 - 13.2
alpha-D-xylose
8.3
alpha-L-arabinose
-
-
18
beta-D-arabinose
-
enzyme form I2 from liver
13
D-fucose
6.5
D-galactose
15
D-glucose
23
D-xylose
-
-
475
lactose
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-
additional information
additional information
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equilibrium exchange kinetic studies
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12000
alpha-D-galactose
Homo sapiens
Q96C23
pH 8.0, 20°C
2600 - 16500
alpha-D-glucose
additional information
additional information
Escherichia coli
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.68
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crude enzyme, pH 7.4, temperature not specified in the publication
14.03
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purified enzyme, pH 7.4, temperature not specified in the publication
16.3
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enzyme form I, small intestine
35.8
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enzyme form II, small intestine
200
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gene expressed in Escherichia coli
510
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enzyme form II, kidney
512
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enzyme form I, kidney
709
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enzyme form II, liver
720
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enzyme form I1, liver
745
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enzyme form I2, liver
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
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5.6
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beta-glucose-6-phosphate
6.5 - 8
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free and immobilized enzyme
7 - 7.5
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enzyme form I and II from kidney, enzyme form I2 and II from liver, enzyme form I and II from small intestine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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6.0: about 70% of maximal activity, free enzyme. About 90% of maximal activity, immobilized enzyme, 9: about 40% of maximal activity, free enzyme. About 60% of maximal activity, immobilized enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
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enzyme form I, II, III, and IV
35 - 38
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-
40 - 45
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-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
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20°C: about 50% of maximal activity, 55°C: about 80% of maximal activity, immobilized enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mucosal cells, 10-day-old rats: 4 enzyme forms, I-IV. Adult rats: 2 enzyme forms, I and II, enzyme activity in suckling rats is several times higher than that of adult rats
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
gel filtration
34200 - 37400
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sucrose density gradient centrifugation, gel filtration
35900
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gel filtration
36400
-
x * 36400, calculation from amino acid composition
36600 - 37500
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sucrose density gradient centrifugation, gel filtration
36800
-
1 * 36800, calf, SDS-PAGE
37000 - 38100
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adult, embryo and calf, sucrose density gradient centrifugation, gel filtration
37500
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liver and kidney, sucrose density gradient centrifugation
37800
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1 * 37800, adult, SDS-PAGE
38000
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x * 38000, SDS-PAGE
38300
-
gel filtration
38500
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enzyme form II, sucrose density gradient centrifugation
38800
-
enzyme form III, sucrose density gradient centrifugation
39000
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enzyme form II, sucrose density gradient centrifugation
39100
-
enzyme form IV, sucrose density gradient centrifugation
41800
-
x * 41800, enzyme form I from kidney, SDS-PAGE
50000
-
sedimetation data
70000
-
calculation from sedimentation data
130000
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2 * 130000, SDS-PAGE
260000
-
gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 130000, SDS-PAGE
monomer
additional information
-
structural analysis of the N-terminal-blocked peptides
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol 4000, 200 mM sodium acetate and 100 mM Tris-HCl pH 8.5
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hanging-drop vapour-diffusion method
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
-
20°C, 24 h, complete loss of activity
2374
2 - 10
-
5 min, stable
2364
3
-
20°C, 24 h, 50% loss of activity
2374
5.5 - 9
-
20°C, 24 h, no inactivation
2374
10.5
-
20°C, 24 h, 66% loss of activity
2374
11
-
20°C, 24 h, complete loss of activity
2374
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
slow precipitation starts after a few minutes. High substrate concentrations stabilize
50 - 55
-
immobilized hog kidney enzyme is 5 to 50 times more stable as the soluble form of the closely related bovine kidney enzyme
50
-
stable up to, enzyme form I and II from kidney liver and small instetine
50 - 55
-
immobilized hog kidney enzyme is 5 to 50 times more stable as the soluble form of the closely related bovine kidney enzyme
55
-
30 min, stable below
60
-
30 min, 5% loss of activity
65
-
30 min, 25% loss of activity
75
-
half-life: 6.9 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization to porious silica does not stabilize the enzyme to a sufficient degree that it can be used for long periods of time
-
photoinactivation in presence of methylene blue or rose bengal. A constant photoinactivation rate is observed in the range pH 5.5-8.0 which increases rapidly at higher values. The competitive inhibitor Hg2+ increases the photosensitivity of the enzyme. The competitive inhibitors, L-fucose and L-xylose protect from photoinactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for indefinite periods in EDTA buffer, slow inactivation when frozen
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme form I and II from kidney and enzyme form II from liver
-
multiple forms: I, II, III, and IV. Two major forms: I and II are purified
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native enzyme 8.35fold from liver by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
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Ni-NTA affinity column chromatography and Superdex 200 gel filtration
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Ni–NTA affinity column chromatography
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UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity. The active sites for the two enzymatic activities are located in different regions of the epimerase homoenzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
baculovirus expression system
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cloned into pRSET-C vector (Invitrogen), expression in Escherichia coli
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construction of a shuttle plasmid for Bacillus megaterium and Escherichia coli that contains the promoter and repressor gene of the Bacillus megaterium borne operon for xylose utilization. A polylinker downstream the promoter allows versatile cloning of genes under its transcriptional control
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construction of a shuttle plasmid for Bacillus megaterium and Escherichia coli that contains the promoter and repressor gene of the Bacillus megaterium borne operon for xylose utilization. A polylinker downstream the promoter allows versatile cloning of genes under its transcriptional control; expression in Escherichia coli
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expressed in Escherichia coli Rosetta (DE3) cells
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expression in Corynebacterium glutamicum
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expression in Escherichia coli
overexpression in a mutarotase defective Escherichia coli strain restores the ability of these bacteria to grow in minimal medium with phenyl-beta-galactoparanoside as the sole carbon source
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E307A
mutant enzyme without aldose 1-epimerase activity
H107A
mutant enzyme with 5fold reduced activity with alpha-D-galactose and 7.8fold reduced activity with alpha-D-glucose, compared to wild-type enzyme
H176A
mutant enzyme without aldose 1-epimerase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis
-
improvement of a bacterial L-arabinose utilization pathway consisting of L-arabinose isomerase from Bacillus licheniformis and L-ribulokinase and L-ribulose-5-phosphate 4-epimerase from Escherichia coli after expression of the corresponding genes in Saccharomyces cerevisiae. After adaptation of codon usage, yeast transformants show strongly improved L-arabinose conversion rates. The ethanol production rate from L-arabinose can be increased more than 2.5fold from 0.014 g ethanol per h and g dry weight to 0.036 g ethanol per h and g dry weight and the ethanol yield can be increased from 0.24 g ethanol per g consumed L-arabinose to 0.39 g ethanol per g consumed L-arabinose
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