Cloned (Comment) | Organism |
---|---|
the nucleotide sequence coding for the Arabidopsis thaliana acetohydroxy acid synthase is genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in Escherichia coli | Spinacia oleracea |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.007 | - |
NADPH | pH 8.2, 30°C, chimeric enzyme Arabidopsis thaliana acetohydroxy acid synthase is genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli | Spinacia oleracea | |
0.01 | - |
2-aceto-2-hydroxybutanoate | pH 8.2, 30°C, chimeric enzyme Aabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli | Spinacia oleracea |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Spinacia oleracea | |
Mg2+ | Km: 0.5 mM | Spinacia oleracea |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
120000 | - |
2 * 120000, Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in Escherichia coli, SDS-PAGE | Spinacia oleracea |
240000 | - |
Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli, gel filtration | Spinacia oleracea |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-acetolactate + NADPH | Spinacia oleracea | enzyme of branched chain amino acid synthesis | 2,3-dihydroxy-3-methylbutanoate + NADP+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Spinacia oleracea | - |
overexpressed in Escherichia coli | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.9 | - |
Arabidopsis thaliana acetohydroxy acid synthase is genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli | Spinacia oleracea |
Storage Stability | Organism |
---|---|
-80°, chimeric enzyme composed of Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli, several months, no loss of activity | Spinacia oleracea |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-acetolactate + NADPH | enzyme of branched chain amino acid synthesis | Spinacia oleracea | 2,3-dihydroxy-3-methylbutanoate + NADP+ | - |
r | |
NADPH + 2-aceto-2-hydroxybutyrate | - |
Spinacia oleracea | NADP+ + ? | - |
? | |
NADPH + 2-acetolactate | - |
Spinacia oleracea | NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 120000, Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in Escherichia coli, SDS-PAGE | Spinacia oleracea |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.2 | - |
isomeroreductase activity of the chimeric enzyme composed of Arabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in Escherichia coli | Spinacia oleracea |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Spinacia oleracea |