Literature summary for 3.7.1.1 extracted from

Chen, C.; Sun, Q.; Narayanan, B.; Nuss, D.L.; Herzberg, O.
Structure of oxalacetate acetylhydrolase, a virulence factor of the chestnut blight fungus (2010), J. Biol. Chem., 285, 26685-26696.

Crystallization (Commentary)

Crystallization (Comment)	Organism
OAH alone, in complex with a inhibitor 3,3-difluorooxalacetate, and in complex with reaction product oxalate, soaking of ligand-free OAH crystals in solution containing 0.2 M MnCl2 or 0.2 M MgCl2, 10 mM CaCl2, 2 mM 3,3-difluorooxalacetate, 0.1 M Na-HEPES, pH 7.5, and 30% v/v PEG 400 for 5-10 min yielded the desired enzyme inhibitor complex, X-ray diffraction structure determination and analysis at resolution limit of 1.30, 1.55, and 1.65 A , respectively, molecular replacement	Cryphonectria parasitica

Crystallization (Comment)

Organism

OAH alone, in complex with a inhibitor 3,3-difluorooxalacetate, and in complex with reaction product oxalate, soaking of ligand-free OAH crystals in solution containing 0.2 M MnCl2 or 0.2 M MgCl2, 10 mM CaCl2, 2 mM 3,3-difluorooxalacetate, 0.1 M Na-HEPES, pH 7.5, and 30% v/v PEG 400 for 5-10 min yielded the desired enzyme inhibitor complex, X-ray diffraction structure determination and analysis at resolution limit of 1.30, 1.55, and 1.65 A , respectively, molecular replacement

Cryphonectria parasitica

Inhibitors

Inhibitors	Comment	Organism	Structure
3,3-difluorooxalacetate	a mechanism-based inhibitor that binds in a gem-diol form analogous to the oxalacetate intermediate/transition state, binding structure, overview	Cryphonectria parasitica

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	steady-state kinetic constants for divalent metal-activated OAH from	Cryphonectria parasitica
0.134	-	oxaloacetate	in presence of Mg2+, pH 7.5, 25°C	Cryphonectria parasitica
0.48	-	oxaloacetate	in presence of Mn2+, pH 7.5, 25°C	Cryphonectria parasitica
1.248	-	oxaloacetate	in presence of Ca2+, pH 7.5, 25°C	Cryphonectria parasitica

Metals/Ions

Metals/Ions	Comment	Organism
Ca2+	required, in addition to the active site metal cofactors, two additional Ca2+-binding sites mediate intermolecular interactions	Cryphonectria parasitica
Mg2+	can partially substitute for Mn2+	Cryphonectria parasitica
Mn2+	required, active site metal ion	Cryphonectria parasitica

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
oxaloacetate + H2O	Cryphonectria parasitica	-	oxalate + acetate	-	?

Organism

Organism	UniProt	Comment	Textmining
Cryphonectria parasitica	D5LIR7	gene oah is a single gene	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	OAH also exhibits C-C bond cleavagea activity with (2R,3S)-dimethylmalate with 1000fold lower efficacy compared to oxaloacetate hydrolysis. Structural features of substrate binding, overview	Cryphonectria parasitica	?	-	?
oxaloacetate + H2O	-	Cryphonectria parasitica	oxalate + acetate	-	?
oxaloacetate + H2O	oxalate binds in a planar conformation, but the gating loop is largely disordered	Cryphonectria parasitica	oxalate + acetate	-	?

Subunits

Subunits	Comment	Organism
More	an active site gating loop exhibits conformational disorder in the ligand-free structure	Cryphonectria parasitica
tetramer	OAH assembles into a dimer of dimers with each subunit exhibiting an (alpha/beta)8 barrel fold and each pair swapping the 8th alpha-helix	Cryphonectria parasitica

Synonyms

Synonyms	Comment	Organism
OAH	-	Cryphonectria parasitica
oxalacetate acetylhydrolase	-	Cryphonectria parasitica

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Cryphonectria parasitica

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
1.9	-	oxaloacetate	in presence of Ca2+, pH 7.5, 25°C	Cryphonectria parasitica
3.6	-	oxaloacetate	in presence of Mg2+, pH 7.5, 25°C	Cryphonectria parasitica
35.2	-	oxaloacetate	in presence of Mn2+, pH 7.5, 25°C	Cryphonectria parasitica

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Cryphonectria parasitica

General Information

General Information	Comment	Organism
evolution	oxalacetate acetylhydrolase is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily	Cryphonectria parasitica
malfunction	knockout of the oah gene in Cryphonectria parasitica, the chestnut blight fungus, reduces the ability of the fungus to form cankers on chestnut trees	Cryphonectria parasitica
physiological function	oxalacetate acetylhydrolase plays a key role in virulence	Cryphonectria parasitica