Literature summary for 1.1.1.79 extracted from

Kutner, J.; Shabalin, I.G.; Matelska, D.; Handing, K.B.; Gasiorowska, O.; Sroka, P.; Gorna, M.W.; Ginalski, K.; Wozniak, K.; Minor, W.
Structural, biochemical, and evolutionary characterizations of glyoxylate/hydroxypyruvate reductases show their division into two distinct subfamilies (2018), Biochemistry, 57, 963-977 .

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIPL cells	Sinorhizobium meliloti

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme with NADP+ plus sulfate, sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M ammonium sulfate. Enzyme with NADPH plus oxalate, sitting drop vapor diffusion method, using 0.2 M ammonium citrate tribasic pH 7.0, 20% (w/v) PEG 3350. Apo enzyme form, sitting drop vapor diffusion method, using 0.1 M sodium citrate, pH 5.6, 20% (v/v) 2-propanol, 20% (w/v) PEG 4000	Sinorhizobium meliloti

Crystallization (Comment)

Organism

enzyme with NADP+ plus sulfate, sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M ammonium sulfate. Enzyme with NADPH plus oxalate, sitting drop vapor diffusion method, using 0.2 M ammonium citrate tribasic pH 7.0, 20% (w/v) PEG 3350. Apo enzyme form, sitting drop vapor diffusion method, using 0.1 M sodium citrate, pH 5.6, 20% (v/v) 2-propanol, 20% (w/v) PEG 4000

Sinorhizobium meliloti

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
9.7	-	pyruvate	at pH 7.5 and 25°C	Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
glyoxylate + NADPH + H+	Sinorhizobium meliloti	enzyme GhrA shows highest catalytic efficiency for glyoxylate	glycolate + NADP+	-	?
hydroxypyruvate + NADH + H+	Sinorhizobium meliloti	with hydroxypyruvate as a substrate at a saturating concentration (66.7 mM), the enzyme GhrA exhibits 2-3% activity with 0.4 mM NADH as compared to 0.4 mM NADPH	D-glycerate + NAD+	-	?
hydroxypyruvate + NADPH + H+	Sinorhizobium meliloti	-	D-glycerate + NADP+	-	?
additional information	Sinorhizobium meliloti	no activity with 2-oxo-D-gluconate	?	-	-
oxalate + NADPH + H+	Sinorhizobium meliloti	-	?	-	?
pyruvate + NADPH + H+	Sinorhizobium meliloti	low efficiency	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Sinorhizobium meliloti	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA resin column chromatography and Superdex 200 pg gel filtration	Sinorhizobium meliloti

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
glyoxylate + NADPH + H+	enzyme GhrA shows highest catalytic efficiency for glyoxylate	Sinorhizobium meliloti	glycolate + NADP+	-	?
hydroxypyruvate + NADH + H+	with hydroxypyruvate as a substrate at a saturating concentration (66.7 mM), the enzyme GhrA exhibits 2-3% activity with 0.4 mM NADH as compared to 0.4 mM NADPH	Sinorhizobium meliloti	D-glycerate + NAD+	-	?
hydroxypyruvate + NADPH + H+	-	Sinorhizobium meliloti	D-glycerate + NADP+	-	?
additional information	no activity with 2-oxo-D-gluconate	Sinorhizobium meliloti	?	-	-
oxalate + NADPH + H+	-	Sinorhizobium meliloti	?	-	?
pyruvate + NADPH + H+	low efficiency	Sinorhizobium meliloti	?	-	?

Subunits

Subunits	Comment	Organism
homodimer	x-ray crystallography	Sinorhizobium meliloti

Synonyms

Synonyms	Comment	Organism
GhrA	-	Sinorhizobium meliloti

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Sinorhizobium meliloti