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D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
additional information
?
-
Substrates: the gmhA gene product is essential for the expression of wild-type lipooligosaccharide by this pathogen
Products: -
?
D-sedoheptulose 7-phosphate

D-glycero-alpha,beta-D-manno-heptose 7-phosphate
Substrates: synthesis of ADP-D-beta-D-heptose in Escherichia coli requires three proteins, GmhA (sedoheptulose 7-phosphate isomerase), HldE (bifunctional D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase), and GmhB (D,D-heptose 1,7-bisphosphate phosphatase)
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
Substrates: first step of the biosynthesis of the inner core lipopolysaccharide precursor, ADP-L-glycero-D-manno-heptose
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate

D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: the enzyme is involved in the biosynthesis of nucleotide-activated heptose
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
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D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
-
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: first committed step in the formation of ADP-heptose
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: it is postulated that GmhA acts through an enediol-intermediate isomerase mechanism
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
-
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
-
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: first committed step in the formation of ADP-heptose
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: it is postulated that GmhA acts through an enediol-intermediate isomerase mechanism
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
additional information
?
-
Substrates: the gmhA gene product is essential for the expression of wild-type lipooligosaccharide by this pathogen
Products: -
?
D-sedoheptulose 7-phosphate

D-glycero-alpha,beta-D-manno-heptose 7-phosphate
Substrates: synthesis of ADP-D-beta-D-heptose in Escherichia coli requires three proteins, GmhA (sedoheptulose 7-phosphate isomerase), HldE (bifunctional D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase), and GmhB (D,D-heptose 1,7-bisphosphate phosphatase)
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
Substrates: first step of the biosynthesis of the inner core lipopolysaccharide precursor, ADP-L-glycero-D-manno-heptose
Products: -
?
D-sedoheptulose 7-phosphate

D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: the enzyme is involved in the biosynthesis of nucleotide-activated heptose
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
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D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: first committed step in the formation of ADP-heptose
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
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D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
-
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
-
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
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D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
r
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: first committed step in the formation of ADP-heptose
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
Substrates: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(2-(6-(N,N-dimethyl sulfamoyl)pipridin-4-yl)pyrazin-2-yl) imidazol-3-ium-1-ide
-
residues Ser55 and Ser83 are the major residues that take part in hydrogen bonding and complex stability, inhibitor movement towards allosteric site when bound to the enzyme. Binding free energy calculations predict high compound affinity for the complex
-
(2E)-2-[[4-(diethylamino)phenyl]methylidene]-N-[(Z)-1-(hydroxyamino)-2-(methylideneamino)ethenyl]hydrazine-1-carbothioamide
-
-
-
(3R)-N,N-dimethyl-3-[6-(3H-pyrazol-4-yl)pyrazin-2-yl]piperidine-1-sulfonamide
-
-
-
5,5-dimethyl-3-[2-oxo-2-[3-(1H-pyrazol-3-yl)pyrrolidin-1-yl]ethyl]imidazolidine-2,4-dione
-
-
-
5-[(1R)-1-hydroxy-2-(phosphonoamino)ethyl]-D-lyxopyranose
-
-
5-[(1R)-2-[4,5-bis(hydroxymethyl)-1H-1,2,3-triazol-1-yl]-1-hydroxyethyl]-D-lyxopyranose
-
poor inhibitor
5-[(1R,2R)-2-carboxy-1,2-dihydroxyethyl]-D-lyxopyranose
-
-
5-[(1S,2S)-1,2-dihydroxy-2-phosphonoethyl]-D-lyxopyranose
-
-
5-[(3S)-3-[4-(methanesulfonyl)-1H-pyrazol-3-yl]pyrrolidine-1-carbonyl]-4-methyl-3H-1,3-thiazol-1-ium
-
-
-
5-{(1R)-1-hydroxy-2-[(methylsulfonyl)amino]ethyl}-D-lyxopyranose
-
poor inhibitor
methyl 5-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-lyxopyranoside
-
-
methyl 5-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-xylopyranoside
-
-
methyl 5-[(1R,2R)-2-carboxy-1,2-dihydroxyethyl]-alpha-D-lyxopyranoside
-
poor inhibitor
methyl 5-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-lyxopyranoside
-
poor inhibitor
methyl 5-[(1S,2S)-1,2-dihydroxy-2-phosphonoethyl]-alpha-D-lyxopyranoside
-
-
additional information
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inhibitior identification by molecular docking study, molecular dynamic simulations. Computational pharmacokinetics determination
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0.3 - 1.53
D-sedoheptulose 7-phosphate
additional information
additional information
kinetic analysis, comparisons of enzyme kinetics, overview
-
0.3
D-sedoheptulose 7-phosphate

mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
0.31
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant wild-type enzyme
0.4
D-sedoheptulose 7-phosphate
wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
0.5
D-sedoheptulose 7-phosphate
pH 8.0, mutant enzyme R69Q
0.5
D-sedoheptulose 7-phosphate
pH not specified in the publication, temperature not specified in the publication
0.67
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant N53G
0.7
D-sedoheptulose 7-phosphate
mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
0.76
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S121G
0.83
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S126A
0.9
D-sedoheptulose 7-phosphate
pH 8.0, wild-type enzyme
0.9
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant T122A
0.92
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S123A
1.2
D-sedoheptulose 7-phosphate
pH 8.0, mutant enzyme H61Q
1.53
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant Q173A
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0.02 - 33.1
D-sedoheptulose 7-phosphate
0.02
D-sedoheptulose 7-phosphate

mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
0.07
D-sedoheptulose 7-phosphate
mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
0.09
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant T122A
0.1
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant Q173A
0.19
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S126A
0.23
D-sedoheptulose 7-phosphate
pH 8.0, mutant enzyme H61Q
0.27
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant N53G
0.31
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S123A
0.36
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S121G
0.44
D-sedoheptulose 7-phosphate
pH 8.0, wild-type enzyme
0.45
D-sedoheptulose 7-phosphate
pH 8.0, mutant enzyme R69Q
0.45
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant wild-type enzyme
0.5
D-sedoheptulose 7-phosphate
wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
33.1
D-sedoheptulose 7-phosphate
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.06 - 71.9
D-sedoheptulose 7-phosphate
0.06
D-sedoheptulose 7-phosphate

pH 8.0, 22°C, recombinant mutant Q173A
0.07
D-sedoheptulose 7-phosphate
mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
0.1
D-sedoheptulose 7-phosphate
mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
0.1
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant T122A
0.2
D-sedoheptulose 7-phosphate
pH 8.0, mutant enzyme H61Q
0.22
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S126A
0.33
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S123A
0.4
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant N53G
0.47
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant mutant S121G
0.5
D-sedoheptulose 7-phosphate
pH 8.0, wild-type enzyme
0.9
D-sedoheptulose 7-phosphate
pH 8.0, mutant enzyme R69Q
1.2
D-sedoheptulose 7-phosphate
wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C
1.45
D-sedoheptulose 7-phosphate
pH 8.0, 22°C, recombinant wild-type enzyme
71.9
D-sedoheptulose 7-phosphate
pH not specified in the publication, temperature not specified in the publication
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malfunction

-
gmhA mutant is severely defective for Caenorhabditis elegans biofilm formation and for flea blockage but only moderately defective in an in vitro biofilm assay. These results validate use of the Caenorhabditis elegans biofilm system to identify genes and pathways involved in Yersinia pestis flea blockage
malfunction
the gmhA mutant is substantially less virulent than the wild-type parent strain
malfunction
the GDP-D-glycero-alpha-D-manno-heptose is a key building block of lipopolysaccharide in mycobacteria and blocking of its biosynthetic pathway leads to high antibiotic susceptibility and reduced virulence of mycobacteria
malfunction
-
the GDP-D-glycero-alpha-D-manno-heptose is a key building block of lipopolysaccharide in mycobacteria and blocking of its biosynthetic pathway leads to high antibiotic susceptibility and reduced virulence of mycobacteria
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malfunction
-
the GDP-D-glycero-alpha-D-manno-heptose is a key building block of lipopolysaccharide in mycobacteria and blocking of its biosynthetic pathway leads to high antibiotic susceptibility and reduced virulence of mycobacteria
-
metabolism

sedoheptulose-7-phosphate isomerase is a critical enzyme involved in lipopolysaccharide biosynthetic pathway in Mycobacterium tuberculosis. The product of the pathway, GDP-D-alpha-D-heptose, is incorporated in the S-layer glycoproteins of mycobacterial membrane by specific precursor
metabolism
-
sedoheptulose-7-phosphate isomerase is a critical enzyme involved in lipopolysaccharide biosynthetic pathway in Mycobacterium tuberculosis. The product of the pathway, GDP-D-alpha-D-heptose, is incorporated in the S-layer glycoproteins of mycobacterial membrane by specific precursor
-
metabolism
-
sedoheptulose-7-phosphate isomerase is a critical enzyme involved in lipopolysaccharide biosynthetic pathway in Mycobacterium tuberculosis. The product of the pathway, GDP-D-alpha-D-heptose, is incorporated in the S-layer glycoproteins of mycobacterial membrane by specific precursor
-
physiological function

phosphoheptose isomerase of Leptospira is vital for lipopolysaccharide biosynthesis
physiological function
a knockout mutant exhibits a decreased growth rate and displays a deep rough type of lipopolysaccharide structure. It has a slight decrease in its motility and is more susceptible to novobiocin and detergents Triton X-100 and SDS. The adhesive capacity of the mutant to AGS cells is reduced significantly, and most of the infected cells don't show a classic hummingbird phenotype
physiological function
-
the enzyme is involved in lipopolysaccharide biosynthesis and catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate
physiological function
Mycobacterium tuberculosis enzyme GmhA catalyzes the isomerization of D-sedoheptulose 7-phosphate into D-glycero-D-alpha-manno-heptose-7-phosphate in the GDP-D-glycero-alpha-D-manno-heptose biosynthetic pathway. The D-glycero-alpha-D-manno-heptose is a major constituent of lipopolysaccharide and contributes to virulence and antibiotic resistance to mycobacteria
physiological function
-
Mycobacterium tuberculosis enzyme GmhA catalyzes the isomerization of D-sedoheptulose 7-phosphate into D-glycero-D-alpha-manno-heptose-7-phosphate in the GDP-D-glycero-alpha-D-manno-heptose biosynthetic pathway. The D-glycero-alpha-D-manno-heptose is a major constituent of lipopolysaccharide and contributes to virulence and antibiotic resistance to mycobacteria
-
physiological function
-
Mycobacterium tuberculosis enzyme GmhA catalyzes the isomerization of D-sedoheptulose 7-phosphate into D-glycero-D-alpha-manno-heptose-7-phosphate in the GDP-D-glycero-alpha-D-manno-heptose biosynthetic pathway. The D-glycero-alpha-D-manno-heptose is a major constituent of lipopolysaccharide and contributes to virulence and antibiotic resistance to mycobacteria
-
physiological function
-
a knockout mutant exhibits a decreased growth rate and displays a deep rough type of lipopolysaccharide structure. It has a slight decrease in its motility and is more susceptible to novobiocin and detergents Triton X-100 and SDS. The adhesive capacity of the mutant to AGS cells is reduced significantly, and most of the infected cells don't show a classic hummingbird phenotype
-
additional information

the residues involved in D-sedoheptulose 7-phosphate and Zn2+ binding are identified using the modeled MtbGmhA complexed with D-sedoheptulose 7-phosphate and Zn2+ structure, molecular dynamics simulations, showing enhanced stability of the enzyme in presence of the ligands. Analysis of the MtbGmhA structure and dynamics involved in D-sedoheptulose 7-phosphate and Zn2+ binding, small angle X-ray scattering analysis (SAXS), overview
additional information
-
the residues involved in D-sedoheptulose 7-phosphate and Zn2+ binding are identified using the modeled MtbGmhA complexed with D-sedoheptulose 7-phosphate and Zn2+ structure, molecular dynamics simulations, showing enhanced stability of the enzyme in presence of the ligands. Analysis of the MtbGmhA structure and dynamics involved in D-sedoheptulose 7-phosphate and Zn2+ binding, small angle X-ray scattering analysis (SAXS), overview
-
additional information
-
the residues involved in D-sedoheptulose 7-phosphate and Zn2+ binding are identified using the modeled MtbGmhA complexed with D-sedoheptulose 7-phosphate and Zn2+ structure, molecular dynamics simulations, showing enhanced stability of the enzyme in presence of the ligands. Analysis of the MtbGmhA structure and dynamics involved in D-sedoheptulose 7-phosphate and Zn2+ binding, small angle X-ray scattering analysis (SAXS), overview
-
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D61A
the mutant exhibits about 17fold reduced catalytic efficiency compared to the wild type enzyme
H64Q
the mutant exhibits 12fold reduced catalytic efficiency compared to the wild type enzyme
H64Q
-
the mutant exhibits 12fold reduced catalytic efficiency compared to the wild type enzyme
-
D94N
kcat/Km for D-sedoheptulose 7-phosphate is 1.8fold higher than wild-type value
H61Q
kcat/Km for D-sedoheptulose 7-phosphate is 2.5fold lower than wild-type value
N53G
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
Q173A
site-directed mutagenesis, the tetrameric mutant shows 24fold reduced activity compared to wild-type enzyme
S121G
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
S123A
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
S126A
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
T122A
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
N53G
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
S121G
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
S123A
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
S126A
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
T122A
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
N53G
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
S121G
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
S123A
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
S126A
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
T122A
-
site-directed mutagenesis, the tetrameric mutant shows reduced activity compared to wild-type enzyme
-
additional information
Glu64, His181, Thr169, Thr122 and His60 are critical for enzyme activity
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Escherichia coli (P63224), Aneurinibacillus thermoaerophilus (Q9AGY7)
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Escherichia coli (P63224), Escherichia coli, Pseudomonas aeruginosa (Q9HVZ0), Pseudomonas aeruginosa
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Escherichia coli
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