EC Number | Application | Comment | Organism |
---|---|---|---|
5.3.1.8 | synthesis | mannose-6-phosphate isomerase from Bacillus subtilis is applied for the production of L-ribose by direct isomerization of L-ribulose | Bacillus subtilis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
5.3.1.8 | expression in Escherichia coli strain ER2566 | Bacillus subtilis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
5.3.1.8 | EDTA | complete inactivation | Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.3.1.8 | 110 | - |
D-ribose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 312 | - |
L-allose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 433 | - |
D-Lyxose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 469 | - |
D-talose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 946 | - |
D-mannose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 998 | - |
L-ribose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.3.1.8 | Ba2+ | activates | Bacillus subtilis | |
5.3.1.8 | Ca2+ | activates | Bacillus subtilis | |
5.3.1.8 | Co2+ | activates, best metal ion, maximal activity at 0.5 mM | Bacillus subtilis | |
5.3.1.8 | Cu2+ | activates | Bacillus subtilis | |
5.3.1.8 | Mg2+ | activates | Bacillus subtilis | |
5.3.1.8 | Mn2+ | highly activating | Bacillus subtilis | |
5.3.1.8 | additional information | mannose-6-phosphate isomerases are metalloenzymes that require a divalent ion metal cofactor for activity and catalysis | Bacillus subtilis | |
5.3.1.8 | Ni2+ | activates | Bacillus subtilis | |
5.3.1.8 | Zn2+ | activates | Bacillus subtilis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
5.3.1.8 | 36444 | - |
* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation | Bacillus subtilis |
5.3.1.8 | 36500 | - |
* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation | Bacillus subtilis |
5.3.1.8 | 36600 | - |
gel filtration, recombinant enzyme | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.1.8 | D-Mannose 6-phosphate | Bacillus subtilis | - |
D-Fructose 6-phosphate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.3.1.8 | Bacillus subtilis | Q9AGZ4 | enzyme from Bacillus subtilis strain HB002; ATCC 23857 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
5.3.1.8 | recombinant enzyme 27fold from Escherichia coli strain ER2566 by affinity chromatography | Bacillus subtilis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
5.3.1.8 | additional information | - |
substrate specificity, overview | Bacillus subtilis |
5.3.1.8 | 0.0101 | - |
recombinant enzyme | Bacillus subtilis |
5.3.1.8 | 0.0165 | - |
recombinant enzyme | Bacillus subtilis |
5.3.1.8 | 0.0225 | - |
recombinant enzyme | Bacillus subtilis |
5.3.1.8 | 0.0659 | - |
recombinant enzyme | Bacillus subtilis |
5.3.1.8 | 0.0918 | - |
recombinant enzyme | Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.1.8 | D-allose | - |
Bacillus subtilis | D-psicose | - |
r | |
5.3.1.8 | D-Lyxose | - |
Bacillus subtilis | D-Xylulose | - |
r | |
5.3.1.8 | D-Mannose | - |
Bacillus subtilis | D-Fructose | - |
r | |
5.3.1.8 | D-Mannose 6-phosphate | - |
Bacillus subtilis | D-Fructose 6-phosphate | - |
r | |
5.3.1.8 | D-ribose | - |
Bacillus subtilis | D-ribulose | - |
r | |
5.3.1.8 | D-talose | - |
Bacillus subtilis | D-tagatose | - |
r | |
5.3.1.8 | L-allose | - |
Bacillus subtilis | L-psicose | - |
r | |
5.3.1.8 | L-lyxose | - |
Bacillus subtilis | L-xylulose | - |
r | |
5.3.1.8 | L-Mannose | - |
Bacillus subtilis | L-Fructose | - |
r | |
5.3.1.8 | L-ribose | - |
Bacillus subtilis | L-ribulose | - |
r | |
5.3.1.8 | L-ribulose | best substrate | Bacillus subtilis | L-ribose | - |
r | |
5.3.1.8 | L-talose | - |
Bacillus subtilis | L-tagatose | - |
r | |
5.3.1.8 | additional information | the enzyme is specific for aldose substrates possessing hydroxyl groups oriented in the same direction at the C-2 and C-3 positions, such as the D- and L-enantiomers of ribose, lyxose, talose, mannose, and allose, substrate specificity, overview | Bacillus subtilis | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.3.1.8 | monomer | * 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation | Bacillus subtilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.3.1.8 | 40 | - |
recombinant enzyme | Bacillus subtilis |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.3.1.8 | 20 | 50 | - |
Bacillus subtilis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.3.1.8 | additional information | - |
first-order kinetics for thermal inactivation | Bacillus subtilis |
5.3.1.8 | 25 | - |
purified recombinant enzyme, half-life is 461 h | Bacillus subtilis |
5.3.1.8 | 30 | - |
purified recombinant enzyme, half-life is 325 h | Bacillus subtilis |
5.3.1.8 | 35 | - |
purified recombinant enzyme, half-life is 236 h | Bacillus subtilis |
5.3.1.8 | 40 | - |
purified recombinant enzyme, half-life is 111 h | Bacillus subtilis |
5.3.1.8 | 45 | - |
purified recombinant enzyme, half-life is 56 h | Bacillus subtilis |
5.3.1.8 | 50 | - |
purified recombinant enzyme, half-life is 10 h | Bacillus subtilis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.3.1.8 | 72 | - |
D-ribose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 920 | - |
L-allose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 3748 | - |
D-mannose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 7089 | - |
D-Lyxose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 17600 | - |
L-ribose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 63970 | - |
D-talose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
5.3.1.8 | 7.5 | - |
recombinant enzyme | Bacillus subtilis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
5.3.1.8 | 6.5 | 8.5 | - |
Bacillus subtilis |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.3.1.8 | 0.6 | - |
D-ribose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 2.9 | - |
L-allose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 3.5 | - |
D-mannose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 6.8 | - |
D-talose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 16.4 | - |
D-Lyxose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis | |
5.3.1.8 | 17.6 | - |
L-ribose | pH 7.5, 40°C, recombinant enzyme | Bacillus subtilis |