Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE | Pyrococcus horikoshii OT3 |
Crystallization (Comment) | Organism |
---|---|
sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD | Pyrococcus horikoshii OT3 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.013 | - |
NADH | with hydroxypyruvate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 | |
0.015 | - |
NADH | with glyoxylate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 | |
0.021 | - |
NADPH | with glyoxylate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 | |
0.025 | - |
NADPH | with hydroxypyruvate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
38000 | - |
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation | Pyrococcus horikoshii OT3 |
76500 | - |
analytical ultracentrifugation | Pyrococcus horikoshii OT3 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii OT3 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant protein from Escherichia coli | Pyrococcus horikoshii OT3 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glyoxylate + NADH + H+ | - |
Pyrococcus horikoshii OT3 | glycolate + NAD+ | - |
? | |
glyoxylate + NADPH + H+ | - |
Pyrococcus horikoshii OT3 | glycolate + NADP+ | - |
? | |
hydroxypyruvate + NADH + H+ | - |
Pyrococcus horikoshii OT3 | D-glycerate + NAD+ | - |
? | |
hydroxypyruvate + NADPH + H+ | - |
Pyrococcus horikoshii OT3 | D-glycerate + NADP+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation | Pyrococcus horikoshii OT3 |
Synonyms | Comment | Organism |
---|---|---|
More | enzyme shows NADH- and NADPH-dependent glyoxylate reductase (EC 1.1.1.26 or 1.1.1.79) activity with higher efficiency with NADH but higher affinity for NADPH when enzyme is incubated without substrate, enzyme displays also hydroxypyruvate reductase (EC 1.1.1.81) activity, closely related to D-glycerate dehydrogense (EC 1.1.1.29) | Pyrococcus horikoshii OT3 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.8 | - |
NADPH | with hydroxypyruvate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 | |
2.4 | - |
NADPH | with glyoxylate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 | |
4.1 | - |
NADH | with hydroxypyruvate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 | |
11 | - |
NADH | with glyoxylate as substrate, pH 7.5 | Pyrococcus horikoshii OT3 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | enzyme has a higher affinity for NADPH than for NADH when incubated without substrate | Pyrococcus horikoshii OT3 | |
NADPH | enzyme has a higher affinity for NADPH than for NADH when incubated without substrate | Pyrococcus horikoshii OT3 |