Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GDP-alpha-D-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
GDP-mannose + D-lactate
?
GDP-mannose + glycolic acid
?
-
the kcat/KM-value for glycolic acid is 70fold lower than the value for glycolic acid at 25°C
-
-
?
additional information
?
-
-
enzyme is able to efficiently synthesize mannosylglycerate and glucosylglycerate alike
-
-
?
GDP-alpha-D-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
-
the enzyme catalyzes the formation of the stress protectant 2-O-alpha-D-mannosyl glycerate
-
-
?
GDP-alpha-D-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
-
at 37°C mannosylglycerate synthase shows donor flexibility and can use alpha-GDP-D-Man, alpha-GDP-D-Glc, beta-GDP-L-fucose, alpha-UDP-D-Man and alpha-UDP-D-Glc, but not Man-1-P, as substrates. The kcat/KM-value for GDP-glucose is 2.5fold lower than the value for GDP-mannose at 25°C. The kcat/KM-value for GDP-glucose is 8.6fold lower than the value for GDP-mannose at 65°C
-
-
?
GDP-alpha-D-glucose + D-glycerate
2-O-(alpha-D-glucopyranosyl)-D-glycerate + GDP
-
-
-
-
?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
-
-
-
?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
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)
-
-
?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
-
at 37°C mannosylglycerate synthase shows donor flexibility and can use alpha-GDP-D-Man, alpha-GDP-D-Glc, beta-GDP-L-fucose, alpha-UDP-D-Man and alpha-UDP-D-Glc, but not Man-1-P, as substrates. The kcat/KM-value for GDP-glucose is 2.5fold lower than the value for GDP-mannose at 25°C. The kcat/KM-value for GDP-glucose is 8.6fold lower than the value for GDP-mannose at 65°C
-
-
?
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
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
-
-
ir
GDP-mannose + D-glycerate
2-O-(alpha-D-mannopyranosyl)-D-glycerate + GDP
-
-
-
-
?
GDP-mannose + D-lactate
?
-
-
-
?
GDP-mannose + D-lactate
?
-
the kcat/KM-value for D-lactate is 70fold lower than the value for D-glycerate at 25°C
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
Co2+
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
Mn2+
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
Ni2+
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
Sr2+
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
Zn2+
-
divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0014 - 121.9
D-glycerate
124.9 - 138.6
GDP-glucose
0.00031 - 89.4
GDP-mannose
23.7
glycolic acid
-
pH 7.8, 25°C, cosubstrate: GDP-mannose
0.0014
D-glycerate
mutant K9A, pH 7.0, 23°C, presence of Mn2+
0.0022
D-glycerate
wild-type, pH 7.0, 23°C, presence of Mn2+
0.0038
D-glycerate
mutant R73A, pH 7.0, 23°C, presence of Mn2+
0.0041
D-glycerate
mutant R73G, pH 7.0, 23°C, presence of Mn2+
0.0058
D-glycerate
mutant R218A, pH 7.0, 23°C, presence of Mn2+
0.0078
D-glycerate
mutant M229A, pH 7.0, 23°C, presence of Mn2+
0.015
D-glycerate
mutant W189A, pH 7.0, 23°C, presence of Mn2+
0.017
D-glycerate
mutant Y37A, pH 7.0, 23°C, presence of Mn2+
0.03
D-glycerate
mutant K76A, pH 7.0, 23°C, presence of Mn2+
0.032
D-glycerate
mutant E166A, pH 7.0, 23°C, presence of Mn2+
0.07
D-glycerate
mutant Q66A, pH 7.0, 23°C, presence of Mn2+
0.6
D-glycerate
pH 7.6, 90°C, native enzyme
0.9
D-glycerate
pH 7.6, 90°C, recombinant enzyme
1.1
D-glycerate
mutant Y220A, pH 7.0, 23°C, presence of Mn2+
1.2
D-glycerate
-
cosubstrate GDP-mannose, pH 8.0, 25°C
1.3
D-glycerate
mutant D135A, pH 7.0, 23°C, presence of Mn2+
1.6
D-glycerate
-
cosubstrate GDP-glucose, pH 8.0, 25°C
1.9
D-glycerate
mutant H217A, pH 7.0, 23°C, presence of Mn2+
3.3
D-glycerate
mutant T139A, pH 7.0, 23°C, presence of Mn2+
3.4
D-glycerate
-
cosubstrate GDP-glucose, pH 8.0, 50°C
3.8
D-glycerate
mutant Y220F, pH 7.0, 23°C, presence of Mn2+
4.4
D-glycerate
-
cosubstrate GDP-mannose, pH 8.0, 50°C
96.5
D-glycerate
-
pH 7.8, 65°C, cosubstrate: GDP-mannose
121.9
D-glycerate
-
pH 7.8, 25°C, cosubstrate: GDP-mannose
0.0022
D-lactate
wild-type, pH 7.0, 23°C, presence of Mn2+
21.3
D-lactate
-
pH 7.8, 25°C, cosubstrate: GDP-mannose
124.9
GDP-glucose
-
pH 7.8, 25°C, cosubstrate: D-glycerate
138.6
GDP-glucose
-
pH 7.8, 25°C, cosubstrate: D-glycerate
0.00031
GDP-mannose
mutant T139A, pH 7.0, 23°C, presence of Mn2+
0.001
GDP-mannose
mutant Q66A, pH 7.0, 23°C, presence of Mn2+
0.001
GDP-mannose
mutant R73A, pH 7.0, 23°C, presence of Mn2+
0.0017
GDP-mannose
mutant K9A, pH 7.0, 23°C, presence of Mn2+
0.0027
GDP-mannose
mutant Y37A, pH 7.0, 23°C, presence of Mn2+
0.0028
GDP-mannose
mutant M229A, pH 7.0, 23°C, presence of Mn2+
0.0028
GDP-mannose
mutant W189A, pH 7.0, 23°C, presence of Mn2+
0.0029
GDP-mannose
mutant Y220A, pH 7.0, 23°C, presence of Mn2+
0.0031
GDP-mannose
wild-type, pH 7.0, 23°C, presence of Mn2+
0.0041
GDP-mannose
mutant R73G, pH 7.0, 23°C, presence of Mn2+
0.0063
GDP-mannose
mutant D135A, pH 7.0, 23°C, presence of Mn2+
0.0065
GDP-mannose
mutant Y220F, pH 7.0, 23°C, presence of Mn2+
0.0096
GDP-mannose
mutant E166A, pH 7.0, 23°C, presence of Mn2+
0.011
GDP-mannose
mutant K76A, pH 7.0, 23°C, presence of Mn2+
0.012
GDP-mannose
mutant H217A, pH 7.0, 23°C, presence of Mn2+
0.033
GDP-mannose
mutant R218A, pH 7.0, 23°C, presence of Mn2+
0.2
GDP-mannose
-
pH 8.0, 25°C
0.2
GDP-mannose
pH 7.6, 90°C, recombinant enzyme
0.3
GDP-mannose
pH 7.6, 90°C, native enzyme
0.6
GDP-mannose
-
pH 8.0, 25°C
1
GDP-mannose
-
pH 8.0, 50°C
2.4
GDP-mannose
-
pH 8.0, 50°C
81.2
GDP-mannose
-
pH 7.8, 25°C, cosubstrate: D-glycerate
89.4
GDP-mannose
-
pH 7.8, 65°C, cosubstrate: D-glycerate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0052
glycolic acid
-
pH 7.8, 25°C, cosubstrate: GDP-mannose
0.017
D-glycerate
mutant T139A, pH 7.0, 23°C, presence of Mn2+
0.023
D-glycerate
mutant E166A, pH 7.0, 23°C, presence of Mn2+
0.023
D-glycerate
mutant Q66A, pH 7.0, 23°C, presence of Mn2+
0.032
D-glycerate
wild-type, pH 7.0, 23°C, presence of Mn2+
0.055
D-glycerate
mutant R73A, pH 7.0, 23°C, presence of Mn2+
0.06
D-glycerate
mutant R73G, pH 7.0, 23°C, presence of Mn2+
0.065
D-glycerate
mutant D135A, pH 7.0, 23°C, presence of Mn2+
0.067
D-glycerate
mutant Y220A, pH 7.0, 23°C, presence of Mn2+
0.07
D-glycerate
mutant Y220F, pH 7.0, 23°C, presence of Mn2+
0.075
D-glycerate
mutant K76A, pH 7.0, 23°C, presence of Mn2+
0.077
D-glycerate
mutant W189A, pH 7.0, 23°C, presence of Mn2+
0.083
D-glycerate
mutant H217A, pH 7.0, 23°C, presence of 3 mM Mg2+
0.115
D-glycerate
mutant K9A, pH 7.0, 23°C, presence of Mn2+
0.135
D-glycerate
mutant M229A, pH 7.0, 23°C, presence of Mn2+
0.183
D-glycerate
mutant Y37A, pH 7.0, 23°C, presence of Mn2+
0.25
D-glycerate
mutant R218A, pH 7.0, 23°C, presence of Mn2+
0.267
D-glycerate
mutant H217A, pH 7.0, 23°C, presence of Mn2+
0.6
D-glycerate
wild-type, pH 7.0, 23°C, presence of 3 mM Ca2+
1.02
D-glycerate
-
pH 7.8, 25°C, cosubstrate: GDP-mannose
1.92
D-glycerate
wild-type, pH 7.0, 23°C, presence of 3 mM Mg2+
6.5
D-glycerate
-
pH 7.8, 65°C, cosubstrate: GDP-mannose
0.0026
D-lactate
-
pH 7.8, 25°C, cosubstrate: GDP-mannose
0.017
D-lactate
wild-type, pH 7.0, 23°C, presence of Mn2+
0.63
GDP-glucose
-
pH 7.8, 25°C, cosubstrate: D-glycerate
1.1
GDP-glucose
-
pH 7.8, 25°C, cosubstrate: D-glycerate
0.018
GDP-mannose
wild-type, pH 7.0, 23°C, presence of Mn2+
0.028
GDP-mannose
mutant E166A, pH 7.0, 23°C, presence of Mn2+
0.037
GDP-mannose
mutant Y220F, pH 7.0, 23°C, presence of Mn2+
0.042
GDP-mannose
mutant Y220A, pH 7.0, 23°C, presence of Mn2+
0.045
GDP-mannose
mutant D135A, pH 7.0, 23°C, presence of Mn2+
0.047
GDP-mannose
mutant R73A, pH 7.0, 23°C, presence of Mn2+
0.06
GDP-mannose
mutant R73G, pH 7.0, 23°C, presence of Mn2+
0.067
GDP-mannose
mutant W189A, pH 7.0, 23°C, presence of Mn2+
0.068
GDP-mannose
mutant K76A, pH 7.0, 23°C, presence of Mn2+
0.082
GDP-mannose
mutant K9A, pH 7.0, 23°C, presence of Mn2+
0.085
GDP-mannose
mutant T139A, pH 7.0, 23°C, presence of Mn2+
0.127
GDP-mannose
mutant M229A, pH 7.0, 23°C, presence of Mn2+
0.163
GDP-mannose
mutant Y37A, pH 7.0, 23°C, presence of Mn2+
0.183
GDP-mannose
mutant R218A, pH 7.0, 23°C, presence of Mn2+
0.483
GDP-mannose
mutant H217A, pH 7.0, 23°C, presence of Mn2+
0.967
GDP-mannose
mutant Q66A, pH 7.0, 23°C, presence of Mn2+
1.02
GDP-mannose
-
pH 7.8, 25°C, cosubstrate: D-glycerate
6.1
GDP-mannose
-
pH 7.8, 65°C, cosubstrate: D-glycerate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D100A
-
inactive mutant enzyme
D135A
very high Km value for D-glycerate and a slight increase in kcat
E166A
15-fold increase in Km for glycerate
K76A
3-4-fold increase in kcat coupled with an elevation in Km for D-glycerate and GDP-Man of 15- and 3-fold, respectively
K9A
significant increase in kcat, little effect on the Km value for GDP-Man
M229A
minor influence on catalytic performance
Q66A
substantial increases in kcat and Km for both the acceptor and donor substrates
R131A
-
inactive mutant enzyme
R218A
significant increase in kcat and Km values for GDP-Man, only a modest influence on the Km value for the acceptor substrate
R73A
minor influence on catalytic performance
R73G
minor influence on catalytic performance
T139A
Km value for lactate above 100 mM, modest decrease in kcat but a 1500-fold increase in the Km values for D-glycerate
W189A
3- and 7-fold increase in kcat and Km for D-glycerate, compared with the wild-type enzyme, no influence on utilization of GDP-Man
Y220A
500-fold increase in Km for D-glycerate
Y220F
1500-fold increase in Km for D-glycerate
Y37A
significant increase in kcat, little effect on the Km value for GDP-Man
D102A
-
inactive mutant enzyme
D102A
completely inactive in the presence of all metals tested
H217A
-
inactive mutant enzyme
H217A
significant change in metal preference. Mutant is essentially inactive in the presence of Ca2+, whereas the kcat value is reduced 23-fold in the presence of Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
J. Biol. Chem.
274
35407-35414
1999
Rhodothermus marinus (Q9RFR0), Rhodothermus marinus
brenda
Flint, J.; Taylor, E.; Yang, M.; Bolam, D.N.; Tailford, L.E.; Martinez-Fleites, C.; Dodson, E.J.; Davis, B.G.; Gilbert, H.J.; Davies, G.J.
Structural dissection and high-throughput screening of mannosylglycerate synthase
Nat. Struct. Mol. Biol.
12
608-614
2005
Rhodothermus marinus
brenda
Nielsen, M.M.; Suits, M.D.; Yang, M.; Barry, C.S.; Martinez-Fleites, C.; Tailford, L.E.; Flint, J.E.; Dumon, C.; Davis, B.G.; Gilbert, H.J.; Davies, G.J.
Substrate and metal ion promiscuity in mannosylglycerate synthase
J. Biol. Chem.
286
15155-15164
2011
Rhodothermus marinus (Q9RFR0), Rhodothermus marinus
brenda
Nobre, A.; Empadinhas, N.; Nobre, M.; Lourenco, E.; Maycock, C.; Ventura, M.; Mingote, A.; da Costa, M.
The plant Selaginella moellendorffii possesses enzymes for synthesis and hydrolysis of the compatible solutes mannosylglycerate and glucosylglycerate
Planta
237
891-901
2012
Selaginella moellendorffii
brenda