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Literature summary for 2.3.3.14 extracted from

  • Bulfer, S.L.; Scott, E.M.; Couture, J.F.; Pillus, L.; Trievel, R.C.
    Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis (2009), J. Biol. Chem., 284, 35769-35780.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.3.14

Application

Application Comment Organism
medicine homocitrate synthase is a potential target for antifungal drugs Schizosaccharomyces pombe

Cloned(Commentary)

Cloned (Comment) Organism
into the parallel expression vector pHIS2 Schizosaccharomyces pombe

Crystallization (Commentary)

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

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 [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

Metals/Ions Comment Organism Structure
Co2+
-
 Schizosaccharomyces pombe
Zn2+
-
 Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Schizosaccharomyces pombe
-
-
-

Purification (Commentary)

Purification (Comment) Organism
on a Talon Co2+ immobilized metal affinity chromatography column or a Zn2+ charged IMAC sepharose column Schizosaccharomyces pombe

Substrates and Products (Substrate)

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

Subunits Comment Organism
homodimer
-
 Schizosaccharomyces pombe

Synonyms

Synonyms Comment Organism
HCS
-
 Schizosaccharomyces pombe
homocitrate synthase
-
 Schizosaccharomyces pombe
SpHCS
-
 Schizosaccharomyces pombe

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 activity assay at room temperature Schizosaccharomyces pombe

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 activity assay Schizosaccharomyces pombe

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Schizosaccharomyces pombe

General Information

General Information Comment Organism
metabolism reaction is the first step in the lysine biosynthetic pathway through alpha-aminoadipate Schizosaccharomyces pombe