Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Rhodothermus marinus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | - |
GDP-mannose | pH 7.6, 90°C, recombinant enzyme | Rhodothermus marinus | |
0.3 | - |
GDP-mannose | pH 7.6, 90°C, native enzyme | Rhodothermus marinus | |
0.6 | - |
D-glycerate | pH 7.6, 90°C, native enzyme | Rhodothermus marinus | |
0.9 | - |
D-glycerate | pH 7.6, 90°C, recombinant enzyme | Rhodothermus marinus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | addition of Mg2+ is required for maximal activity. The activity of mannosylglycerate synthase is 2.5-fold lower in the absence of this divalent cation | Rhodothermus marinus | |
additional information | NaCl and KCl, in the concentration range of 50-500 mM, have no effect on the enzyme activity | Rhodothermus marinus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
45000 | - |
x * 45000, SDS-PAGE | Rhodothermus marinus |
46125 | - |
x * 46125, calculated from sequence | Rhodothermus marinus |
122000 | - |
gel filtration | Rhodothermus marinus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GDP-mannose + D-glycerate | Rhodothermus marinus | Rhodothermus marinus possesses two enzymatic systems for the synthesis of mannosylglycerate. The first one is a single-step pathway in which mannosylglycerate synthase catalyses the synthesis of 2-O-(alpha-D-mannopyranosyl)-D-glycerate in one-step from GDP-mannose and D-glycerate. The second system is a two-step pathway in which mannosyl-3-phosphoglycerate synthase (EC 2.4.1.217) catalyses the conversion of GDP-mannose and 3-phospho-D-glycerate into 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-mannopyranosyl)-D-glycerate by mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) | 2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodothermus marinus | Q9RFR0 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Rhodothermus marinus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
70 | - |
pH 7.6, 90°C | Rhodothermus marinus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GDP-mannose + D-glycerate | Rhodothermus marinus possesses two enzymatic systems for the synthesis of mannosylglycerate. The first one is a single-step pathway in which mannosylglycerate synthase catalyses the synthesis of 2-O-(alpha-D-mannopyranosyl)-D-glycerate in one-step from GDP-mannose and D-glycerate. The second system is a two-step pathway in which mannosyl-3-phosphoglycerate synthase (EC 2.4.1.217) catalyses the conversion of GDP-mannose and 3-phospho-D-glycerate into 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-mannopyranosyl)-D-glycerate by mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) | Rhodothermus marinus | 2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP | - |
? | |
GDP-mannose + D-glycerate | the enzyme is specific for GDP-mannose and D-glycerate. The enzyme shows no activity for the reverse reaction. No activity with: ADP-mannose, UDP-mannose (less than 3% of that of GDP mannose), GDP-glucose, UDP-glucose, ADP-glucose, mannose 1-phosphate, and mannose 6-phosphate as sugar donors, and L-glycerate, glycerol 3-phosphate, glucose 6-phosphate, glucose 1-phosphate and D-3-phosphoglycerate as sugar acceptors | Rhodothermus marinus | 2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP | - |
ir |
Subunits | Comment | Organism |
---|---|---|
? | x * 45000, SDS-PAGE | Rhodothermus marinus |
? | x * 46125, calculated from sequence | Rhodothermus marinus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | 90 | native and recombinant enzyme | Rhodothermus marinus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
75 | 95 | 75°C: native enzyme shows about 70% of maximal activity, recombinant enzyme shows about 40% of maximal activity, 95°C: native enzyme shows about 60% of maximal activity, recombinant enzyme shows about 70% of maximal activity | Rhodothermus marinus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermostability is not improved by Ca2+ (5 mM), nor is it enhanced under anaerobic conditions. The properties of the native and recombinant enzyme are similar, but the recombinant form is less thermostable | Rhodothermus marinus |
65 | - |
half-life: 170 min | Rhodothermus marinus |
90 | - |
half-life: 30 min for the native enzyme, 17 min for the recombinant enzyme | Rhodothermus marinus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | 7 | activity remains nearly constant between pH 5.5 and 7.0 | Rhodothermus marinus |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Rhodothermus marinus | isoelectric focusing | - |
4.8 |