Information on EC 2.7.7.13 - mannose-1-phosphate guanylyltransferase

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

EC NUMBER
COMMENTARY hide
2.7.7.13
-
RECOMMENDED NAME
GeneOntology No.
mannose-1-phosphate guanylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Biosynthesis of secondary metabolites
-
-
d-mannose degradation
-
-
Fructose and mannose metabolism
-
-
GDP-mannose biosynthesis
-
-
L-ascorbate biosynthesis I (L-galactose pathway)
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP:alpha-D-mannose-1-phosphate guanylyltransferase
The bacterial enzyme can also use ITP and dGTP as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-24-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Arthrobacter sp. NRRL B1973
NRRL B1973
-
-
Manually annotated by BRENDA team
strain YJ-407, gene Afsrb1
UniProt
Manually annotated by BRENDA team
strain YJ-407, gene Afsrb1
UniProt
Manually annotated by BRENDA team
strain J2315, gene bceA
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
clone JPCM5 (MCAN/ES/98/LLM-877)
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
loss of virulence after deletion of GDPmannose pyrophosphorylase gene
-
-
Manually annotated by BRENDA team
acerola
-
-
Manually annotated by BRENDA team
genotypes Pokkali and IR64, gene OsMPG1
-
-
Manually annotated by BRENDA team
bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
Manually annotated by BRENDA team
bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
Manually annotated by BRENDA team
a S288C strain
SwissProt
Manually annotated by BRENDA team
strain P2, DSM 1617
-
-
Manually annotated by BRENDA team
strain P2, DSM 1617
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
unrooted relationship tree of MPG proteins from various organisms, phylogenetic analysis, overview
malfunction
metabolism
the enzyme catalyzes a step in the mannose activation pathways and glycoconjugate biosynthesis in Leishmania, overview
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-Azido-GTP + glucose 1-phosphate
8-Azido-GDPglucose + diphosphate
show the reaction diagram
-
-
-
?
8-Azido-GTP + mannose 1-phosphate
8-Azido-GDP mannose + diphosphate
show the reaction diagram
-
-
-
?
ATP + alpha-D-mannose 1-phosphate
ADPmannose + diphosphate
show the reaction diagram
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 18% of activity with GTP
-
?
ATP + alpha-D-mannose 1-phosphate
alpha-ADP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
ATP + D-mannose 1-phosphate
diphosphate + ADP-mannose
show the reaction diagram
-
-
-
-
CTP + alpha-D-mannose 1-phosphate
alpha-CDP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
CTP + alpha-D-mannose 1-phosphate
diphosphate + CDP-alpha-D-mannose
show the reaction diagram
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 7% of activity with GTP
-
?
CTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
D-mannose 1-phosphate + GTP
GDP-D-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
dGTP + alpha-D-mannose 1-phosphate
dGDPmannose + diphosphate
show the reaction diagram
dGTP + alpha-D-mannose 1-phosphate
diphosphate + dGDP-mannose
show the reaction diagram
-
-
-
?
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
dTTP + alpha-D-mannose 1-phosphate
alpha-dTDP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
GDP-glucose + diphosphate
D-glucose 1-phosphate + GTP
show the reaction diagram
-
most effective substrate in direction of nucleoside triphosphate formation, in the reverse direction GTP is a better glucose acceptor than ITP
-
r
GDP-mannose + diphosphate
GTP + D-mannose 1-phosphate
show the reaction diagram
GDPmannose + diphosphate
?
show the reaction diagram
-
61% of the activity with GDPglucose
-
-
r
GTP + 2-deoxy-alpha-D-glucose-1-phosphate
GDP-2-deoxy-alpha-D-glucose + diphosphate
show the reaction diagram
-
recombinant GDPmannose pyrophosphorylase, 15% of activity with mannose 1-phosphate
-
?
GTP + 2-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-2-O-methyl-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + 3-deoxy-alpha-D-arabino-hexose-1-phosphate
GDP-3-deoxy-alpha-D-arabino-hexose + diphosphate
show the reaction diagram
-
recombinant GDPmannose pyrophosphorylase, 70% of activity with mannose 1-phosphate
-
?
GTP + 3-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-3-O-methyl-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + 4-deoxy-alpha-D-lyxo-hexose-1-phosphate
GDP-4-deoxy-alpha-D-lyxo-hexose + diphosphate
show the reaction diagram
-
recombinant GDPmannose pyrophosphorylase, 22% of activity with mannose 1-phosphate
-
?
GTP + 4-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-4-O-methyl-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + 6-O-methyl-alpha-D-mannose 1-phosphate
diphosphate + GDP-6-O-methyl-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-galactose 1-phosphate
GDP-alpha-D-galactose + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-glucosamine 1-phosphate
alpha-GDP-glucosamine + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-glucosamine 1-phosphate
diphosphate + GDP-alpha-D-glucosamine
show the reaction diagram
-
-
-
?
GTP + alpha-D-glucose 1-phosphate
alpha-GDP-glucose + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-D-lyxose-1-phosphate
GDPalpha-D-lyxose + diphosphate
show the reaction diagram
-
recombinant GDPmannose pyrophosphorylase, 12% of activity with mannose 1-phosphate
-
?
GTP + alpha-D-mannose 1-phosphate
alpha-GDP-mannose + diphosphate
show the reaction diagram
-
in the presence of diphosphatase
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
GTP + alpha-D-mannose 1-phosphate + GTP
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
-
?
GTP + alpha-L-fucose 1-phosphate
GDP-alpha-L-fucose + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + alpha-N-acetyl-D-glucosamine 1-phosphate
GDP-alpha-N-acetyl-D-glucosamine + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
IDPmannose + diphosphate
ITP + mannose 1-phosphate
show the reaction diagram
-
72% of activity with GDPglucose
-
r
ITP + alpha-D-mannose 1-phosphate
IDPmannose + diphosphate
show the reaction diagram
ITP + glucose 1-phosphate
IDP-glucose + diphosphate
show the reaction diagram
-
-
-
?
UTP + alpha-D-mannose 1-phosphate
alpha-UDP-mannose + diphosphate
show the reaction diagram
-
-
-
-
?
UTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
about 8% of the activity with GTP
-
-
?
UTP + alpha-D-mannose 1-phosphate
UDPmannose + diphosphate
show the reaction diagram
-
recombinant beta subunit of GDPmannose pyrophosphorylase, 12% of activity with GTP
-
?
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
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
show the reaction diagram
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
-
r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni2+
activates slightly
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4E)-4-[(6-chloro-1,3-benzodioxol-5-yl)methylidene]-1-(3,4-dimethylphenyl)pyrazolidine-3,5-dione
-
-
(4Z)-1-(4-fluorophenyl)-4-[(5-methyltetrahydrofuran-2-yl)methylidene]pyrazolidine-3,5-dione
-
-
2-(5-ethyl-1,3,4-thiadiazol-2-yl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione
-
-
2-methyl-9H-pyrido[2,3-b]indole
-
-
3-(2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)-1H-indole
-
-
3-(2-ethyl-5-methyl-2H-pyrrol-3-yl)-6-(4-methylphenyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
3-[2-(4-methoxyphenyl)ethyl]-2H-1,2,4-benzothiadiazine 1,1-dioxide
-
-
4-(4-benzylpiperazin-1-yl)-7-chloroquinoline
-
-
4-[4-(4-tert-butylbenzyl)piperazin-1-yl]-7-chloroquinoline
-
-
4-[4-(biphenyl-4-ylmethyl)piperazin-1-yl]-7-chloroquinoline
-
-
5-methyl-2-(2-phenylethyl)-1H-benzimidazole
-
-
6-(1-ethyl-3-propyl-1H-pyrazol-5-yl)-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(2,4-dichlorophenyl)-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(2-chloro-6-fluorobenzyl)-3-(2-ethyl-5-methyl-2H-pyrrol-3-yl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(2-chloro-6-fluorobenzyl)-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(4-chlorophenyl)-3-(2-methylbenzyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-(4-fluorophenyl)-3-(4-methoxyphenyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-[[(4,6-dimethylpyrimidin-2-yl)sulfanyl]methyl]-3-phenyl[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
-
7-chloro-4-(4-methylpiperazin-1-yl)quinoline
-
-
7-methoxy-4-oxo-4H-thiochromene-3-carboxylic acid
-
-
8-(dimethylamino)-7-hydroxy-3-(1-phenyl-1H-pyrazol-4-yl)-4H-chromen-4-one
-
-
9-(3,4-dimethoxyphenyl)-2,3-dihydroimidazo[1,2-c]thieno[3,2-e]pyrimidine
-
-
ammonium sulfate
-
-
Cu2+
-
-
diphosphate
-
strong product inhibition
EDTA
complete inhibition
ethyl (2Z)-(hydroxyimino)(1H-tetrazol-5-yl)ethanoate
-
-
GDP
-
0.4 mM, 50% inhibition
GDP-6-deoyxmannose
-
GDP-glucose
GDP-mannose
glucose 1-phosphate
GMP
-
0.4 mM, 50% inhibition
Hg2+
-
-
mannose 1-phosphate
-
noncompetitive inhibition of GDP-glucose phosphorolysis
methyl 1-cyano-2-hydroxy-9,10-dimethoxy-4-oxo-6,7-dihydro-4H-pyrido[2,1-a]isoquinoline-3-carboxylate
-
-
Zn2+
-
-
[4-(7-chloroquinolin-4-yl)piperazin-1-yl](4-methylphenyl)methanone
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
41.1
2-deoxy-D-glucose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
15.2
3-deoxy-D-arabino-hexose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
0.94
4-deoxy-D-lyxo-hexose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
0.0161
alpha-D-mannose 1-phosphate
pH 7.6, 85C
0.094
D-glucose 1-phosphate
-
cosubstrate GTP, Vmax: 14 micromol/min/mg
0.012 - 0.19
D-mannose 1-phosphate
0.12
dGDP-mannose
-
pH 8.2, 37C
0.089 - 2.9
diphosphate
0.001
GDP-alpha-D-mannose
-
pH 7.8, 37C
0.024 - 2.9
GDP-mannose
0.000039 - 0.78
GDPmannose
2.85
glucose 1-phosphate
-
pH 7.5, 37C, cosubstrate GTP
0.0026 - 1
GTP
3.3
IDP-mannose
-
pH 8.2, 37C
0.28
ITP
-
pH 8.2, 37C
13.8
lyxose 1-phosphate
-
pH 8.0, 25C, recombinant enzyme
0.0004 - 0.2
mannose 1-phosphate
0.002 - 1.9
Mg2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.85 - 195.9
diphosphate
195.9
GDP-mannose
Burkholderia cepacia
Q06XM8
pH 7.6, recombinant enzyme, presence of 10 mM Mn2+
22.1
GDPmannose
Helicobacter pylori
-
pH 8.0, 37C, cosubstrate diphosphate
10.3
mannose 1-phosphate
Helicobacter pylori
-
pH 8.0, 37C, cosubstrate GTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85
ammonium sulfate
-
-
0.016
diphosphate
-
pH 8.0, 25C
11
GDP-glucose
-
pH 7.5, 37C
0.00125 - 0.12
GDP-mannose
2.5
glucose 1-phosphate
-
pH 7.5, 37C
0.06
mannose 1-phosphate
-
pH 7.5, 37C
0.001
Mg2+
-
pH 8.0, 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
GDP-6-deoxymannose
Trypanosoma brucei
B9WNA1
-
0.008
GDP-mannose
Trypanosoma brucei
B9WNA1
feedback inhibition
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.75
-
recombinant enzyme
7.3
substrates GTP, alpha-D-glucosamine 1-phosphate, pH 7.6, 85C
8.2
substrates dGTP, alpha-D-mannose 1-phosphate, pH 7.6, 85C
9.25
-
-
10.2
substrates GTP, alpha-D-mannose 1-phosphate, pH 7.6, 85C
24.1
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
GTP synthesis
6 - 7.5
-
-
6 - 8.5
-
GDPmannose synthesis
7 - 9
-
GTP synthesis
7
-
GDP-mannose synthesis, forward reaction is very sensitive to pH fluctuation
7 - 8
-
recombinant protein exhibits relatively high activity around pH 6.0 and 9.5, with a maximum in the range of pH 7.0-8.0 in phosphate buffer
8.2
-
assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
forward reaction, assay at
60
-
reverse reaction, assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 100
-
temperature dependence of the enzymatic activity is analyzed between 0 and 100C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.03
calculated from amino acid sequence
6.45
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
expression of genes OsMPG1, OsMPG2, OsMPG3 and OsMPG4
Manually annotated by BRENDA team
-
expression of gene OsMPG2
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39700
-
calculated from amino acid sequence
40520
-
calculated from amino acid sequence
42000
-
SDS-PAGE
53000
-
SDS-PAGE
54000
gel filtration, phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is a bifunctional enzyme catalyzing both the phosphomannose isomerase, i.e. PIM, and guanosine 5'-diphospho-D-mannose pyrophosphorylase, i.e. GMP, reaction
70000
-
gel filtration
108000
-
recombinant enzyme, gel filtration
412000
-
sucrose velocity sedimentation
450000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 42000, SDS-PAGE, 2 * 41769.10, ESI-MS (41769.32 theoretical mass)
monomer
1 * 56000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme in apo form, in complex with substrates mannose-1-phosphate, or with GTP, or bound to the end product GDP-Mannose and Mg2+, sitting drop vapour diffusion method, for apoenzyme: mixing of equal volumes of 20 mg/ml protein in 10 mM Tris, pH 8.0, 150 mM NaCl with reservoir solution containing 35% v/v 2-methyl-2,4-pentanediol, 0.1 M phosphate citrate, pH 7.5, for enzyme complexes: preincubation of 12.5 or 25 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, 10 mM MgCl2, with a 16:1 alpha-D-mannose 1-phosphate or a 8:1 GTP and GDP-Man molar excess of ligand for 30 min at room temperature, protein to well solution ratio of 3:1, the well solution containing 30-35% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 4.6, 20 mM MgCl2, or in a 2:1 ratio with weel solution containing 30% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 5.0, 20 mM MgCl2, X-ray diffraction structure determination and analysis at 2.1-2.95 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.7
-
most stable at
642865
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
-
30 min, 50% loss of activity
80
-
hyperthermostable, the enzyme remains stable for over 300 min without losing its activity when stored at 80C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 1 week, 50% loss of activity
-
4C, 25% glycerol, 47 d, 25% loss of activity
-
4C, 3 M ammonium sulfate, 47 d, 40% loss of activity, 122 d, 50% loss of activity
-
4C, ammonium sulfate suspension, several months, no loss of activity
-
4C, stable for a few days, purified enzyme
-
frozen, 20 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol, 1 mM EDTA, several months, no loss of activity
-
frozen, several months, little loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acid treatment, protamine sulfate, ammonium sulfate, DEAE-cellulose, Sephadex G-200, hydroxylapatite, Blue Sepharose
-
affinity chromatography using Talon-Co2+ resin, gel filtration
-
batch absorption to nickel-agarose
Biogel, Q-Sepharose, Sephacryl-200
blue-Sepharose, DEAE-Sepharose, phenyl-Sepharose, agarose-GTP affinity chromatography
-
DEAE-52, ammonium sulfate, propyl-agarose, methyl-agrose, Sephadex G-200, hydroxyapatite
-
GST-fusion protein, glutathione-Sepharose 4B beads
Hi-Trap column chromatography; recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Ni-affinity column
-
protamine sulfate, Sephadex G-25, DEAE-cellulose
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant enzyme from Escherichia coli to homogeneity by glutathione sepharose affinity chromatography
-
recombinant enzyme, Ni-nitrilotriacetic acid column, Superdex 200
-
recombinant enzyme, Q-Sepharose FF, Phenyl-Sepharose, diafiltration, Sephadex G 75, Sephadex G 200, ammonium sulfate
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recombinant enzyme, ultrafiltration, Q-Sepharose
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant His-tagged enzyme from Escherichia coli strain Origami (DE3) pLysS by nickel affinity chromatography and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by metal affinity chromatograhy
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
DNA and amino acid sequence determination and anaylsis, expression analysis and regulation of the expression, functional expression as GST-tagged enzyme in Escherichia coli strain BL21 under conditions suitable to reduce the formation of inclusion bodies using the vector pTgroE of the yeast Vig9 protein, overview; fused to glutathione S-transferase, expression in Escherichia coli, TOP10F'
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expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain
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expressed in Escherichia coli BL21(DE3) cells; gene bceA, the gene is part of the Burkholderia cepacia IST408 exopolysaccharide biosynthetic cluster, physical organization, unrooted phylogenetic tree, DNA and amino acid sequence determination, analysis, and comparisons, overview. Expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3)pLysS
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expression of GST-fusion protein in Escherichia coli
expression of GST-GDPmannose pyrophosphorylase fusion protein in Escherichia coli
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expression of His-tagged enzyme in Escherichia coli strain Origami (DE3) pLysS
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
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expression of wild-type and several PMI-GMP mutants in algA mutant 8853
gene Afsrb1, expression in Escherichia coli strain BL21(DE3)
gene bceA, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene MPG1, recombinant overexpression in Solanum lycopersicum ripe, fruits show enhanced L-ascorbate levels
genes OsMPG1, OsMPG2, OsMPG3 and OsMPG4, DNA and amino acid sequence, chromosomal locations, and alternative spliced forms determination and analysis, genetic organization, genomic distribution of MPG genes on rice chromosomes, and phylogenetic analysis, expression analysis, recombinant expression of GFP-tagged full-length MPG1 in Nicotiana tabacum using the Agrobacterium tumefaciens, strain LBA4404, transfection system. Functional complementation of yeast MPG1 YDL055C mutant by expression of OsMPG1, OsMPG2, OsMPG3 and OsMPG4 genes
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His tagged version expressed in Escherichia coli BL21
His-tagged version expressed in Escherichia coli BL21(DE3)
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overexpression in Escherichia coli
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overexpression reveals changes in cell wall assembly, restores defects in O-glycosylation, but not those in N-glycosylation, that occur in Kluyveromyces lactis cells depleted for the hexokinase Rag5p, overexpression also enhances heterologous protein secretion in Kluyveromyces lactis
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recombinant functional overexpression of Saccharomyces cerevisiae gene MPG1 in Solanum lycopersicum, fruits show 17-31fold enhanced enzyme activity and L-ascorbate levels
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K175E
approx. 9% of wild-type activity, 600fold increase in Km for mannose 1-phosphate
K175Q
approx. 40% of wild-type activity, 3200fold increase in Km for mannose 1-phosphate
K175R
470fold increase in mannose 1-phosphate Km value
K20Q
enzyme is unable to support alginate synthesis although it shows no significant differences in Vmax and Km as compared to wild-type
R19H
approx. 50% of wild-type activity, 8fold increase in Km for mannose 1-phosphate
R19K
approx. 50% of wild-type activity, 2 and 6fold increase in Km for mannose 1-phosphate and GTP, respectively
R19L
approx. 50% of wild-type activity, 5fold increase in Km for mannose 1-phosphate and GTP, respectively
S12A
approx. 44% of wild-type activity, 2 and 3fold decrease in Km for mannose 1-phosphate and GTP, respectively
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
synthesis
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