Application | Comment | Organism |
---|---|---|
medicine | homocitrate synthase is a potential target for antifungal drugs | Schizosaccharomyces pombe |
Cloned (Comment) | Organism |
---|---|
into the parallel expression vector pHIS2 | Schizosaccharomyces pombe |
Crystallization (Comment) | Organism |
---|---|
the crystal structure of the homocitrate synthase apoenzyme and two distinct structures of the enzyme in complex with the substrate 2-oxoglutarate are reported | Schizosaccharomyces pombe |
Protein Variants | Comment | Organism |
---|---|---|
E167A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
E167Q | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
E74A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
E74Q | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
H103A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
Q47A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
R163A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
R163K | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
R163Q | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
R43A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
R43K | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
R43Q | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
S165A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
T197A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
T197S | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
T197V | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
Y332A | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
Y332F | mutant, reveals the contribution of this residue to substrate binding and catalysis | Schizosaccharomyces pombe |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.006 | - |
acetyl-CoA | mutant T197S | Schizosaccharomyces pombe | |
0.00744 | - |
acetyl-CoA | mutant T197A | Schizosaccharomyces pombe | |
0.0107 | - |
acetyl-CoA | wild-type enzyme | Schizosaccharomyces pombe | |
0.0186 | - |
acetyl-CoA | mutant S165A | Schizosaccharomyces pombe | |
0.0307 | - |
acetyl-CoA | mutant E74Q | Schizosaccharomyces pombe | |
0.0352 | - |
acetyl-CoA | mutant H103A | Schizosaccharomyces pombe | |
0.04 | - |
acetyl-CoA | mutant Y332F | Schizosaccharomyces pombe | |
0.0576 | - |
acetyl-CoA | mutant Q47A | Schizosaccharomyces pombe | |
0.146 | - |
acetyl-CoA | mutant R163K | Schizosaccharomyces pombe | |
0.159 | - |
2-oxoglutarate | wild-type enzyme | Schizosaccharomyces pombe | |
0.229 | - |
2-oxoglutarate | mutant T197S | Schizosaccharomyces pombe | |
0.341 | - |
2-oxoglutarate | mutant T197A | Schizosaccharomyces pombe | |
0.461 | - |
2-oxoglutarate | mutant Y332F | Schizosaccharomyces pombe | |
0.536 | - |
2-oxoglutarate | mutant S165A | Schizosaccharomyces pombe | |
0.791 | - |
2-oxoglutarate | mutant E74Q | Schizosaccharomyces pombe | |
3.56 | - |
2-oxoglutarate | mutant H103A | Schizosaccharomyces pombe | |
4.94 | - |
2-oxoglutarate | mutant Q47A | Schizosaccharomyces pombe | |
24.4 | - |
2-oxoglutarate | mutant R163K | Schizosaccharomyces pombe |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | - |
Schizosaccharomyces pombe | |
Zn2+ | - |
Schizosaccharomyces pombe |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + H2O + 2-oxoglutarate | Schizosaccharomyces pombe | - |
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Schizosaccharomyces pombe | - |
- |
- |
Purification (Comment) | Organism |
---|---|
on a Talon Co2+ immobilized metal affinity chromatography column or a Zn2+ charged IMAC sepharose column | Schizosaccharomyces pombe |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + H2O + 2-oxoglutarate | - |
Schizosaccharomyces pombe | (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | - |
Schizosaccharomyces pombe |
Synonyms | Comment | Organism |
---|---|---|
HCS | - |
Schizosaccharomyces pombe |
homocitrate synthase | - |
Schizosaccharomyces pombe |
SpHCS | - |
Schizosaccharomyces pombe |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
activity assay at room temperature | Schizosaccharomyces pombe |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
acetyl-CoA | mutant T197A | Schizosaccharomyces pombe | |
0.2 | - |
2-oxoglutarate | mutant T197A | Schizosaccharomyces pombe | |
0.3 | - |
2-oxoglutarate | mutant H103A | Schizosaccharomyces pombe | |
0.33 | - |
acetyl-CoA | mutant H103A | Schizosaccharomyces pombe | |
0.35 | - |
2-oxoglutarate | mutant Y332F | Schizosaccharomyces pombe | |
0.39 | - |
acetyl-CoA | mutant Y332F | Schizosaccharomyces pombe | |
0.56 | - |
2-oxoglutarate | mutant Q47A | Schizosaccharomyces pombe | |
0.57 | - |
acetyl-CoA | mutant R163K | Schizosaccharomyces pombe | |
0.58 | - |
acetyl-CoA | mutant Q47A | Schizosaccharomyces pombe | |
0.74 | - |
acetyl-CoA | mutant E74Q | Schizosaccharomyces pombe | |
0.78 | - |
2-oxoglutarate | mutant E74Q | Schizosaccharomyces pombe | |
0.87 | - |
2-oxoglutarate | mutant R163K | Schizosaccharomyces pombe | |
2.07 | - |
acetyl-CoA | mutant T197S | Schizosaccharomyces pombe | |
2.28 | - |
2-oxoglutarate | mutant T197S | Schizosaccharomyces pombe | |
2.63 | - |
acetyl-CoA | mutant S165A | Schizosaccharomyces pombe | |
2.67 | - |
2-oxoglutarate | mutant S165A | Schizosaccharomyces pombe | |
4.98 | - |
acetyl-CoA | wild-type enzyme | Schizosaccharomyces pombe | |
5.13 | - |
2-oxoglutarate | wild-type enzyme | Schizosaccharomyces pombe |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
activity assay | Schizosaccharomyces pombe |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Schizosaccharomyces pombe |
General Information | Comment | Organism |
---|---|---|
metabolism | reaction is the first step in the lysine biosynthetic pathway through alpha-aminoadipate | Schizosaccharomyces pombe |