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Literature summary for 2.4.1.269 extracted from

  • Martins, L.O.; Empadinhas, N.; Marugg, J.D.; Miguel, C.; Ferreira, C.; Da Costa, M.S.; Santos, H.
    Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase (1999), J. Biol. Chem., 274, 35407-35414.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rhodothermus marinus

KM Value [mM]

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

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Rhodothermus marinus Q9RFR0
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rhodothermus marinus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
70
-
pH 7.6, 90°C Rhodothermus marinus

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 45000, SDS-PAGE Rhodothermus marinus
? x * 46125, calculated from sequence Rhodothermus marinus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
85 90 native and recombinant enzyme Rhodothermus marinus

Temperature Range [°C]

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 [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 7 activity remains nearly constant between pH 5.5 and 7.0 Rhodothermus marinus

pI Value

Organism Comment pI Value Maximum pI Value
Rhodothermus marinus isoelectric focusing
-
4.8