1.1.1.79: glyoxylate reductase (NADP+)

This is an abbreviated version, for detailed information about glyoxylate reductase (NADP+), go to the full flat file.

Reaction

D-glycerate
+
NAD(P)+
=
glyoxylate
+
NADPH
+
H+

Synonyms

At3g25530, AtGLYR1, AtGLYR2, AtGR1, AtGR2, D-2-hydroxy-acid dehydrogenase, glycerate dehydrogenase, glyoxylate reductase, glyoxylate reductase 1, glyoxylate reductase 2, glyoxylate reductase isoform 1, glyoxylate reductase/hydroxypyruvate reductase, GLYR1, GLYR2, GOR1, GR/HPR, GR1, GR2, GRHPR, GRHRP, HPR2, HPR3, More, NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases, PfuGRHPR, PhoGRHPR, PtGR, PyaGRHPR, TthGR1

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.79 glyoxylate reductase (NADP+)

Crystallization

Crystallization on EC 1.1.1.79 - glyoxylate reductase (NADP+)

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
-
purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M MES buffer, pH 6.5, 0.01 M cobalt (II) chloride, and 1.8 M ammonium sulfate, 20C, X-ray diffraction structure determination and analysis at 1.75 A resolution
purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, hanging drop vapour diffusion method, from a mother liquor containing 100 mM sodium acetate, pH 5.2, 15% PEG 400, and 100 mM NaCl, 20C, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution
analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
-
sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD
-
purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, sitting drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein solution with 0.0015 ml of mother liquor containing 1.7 malonate, pH 7.0, 20C, X-ray diffraction structure determination and analysis at 1.4 A-2.0 A resolution, molecular replacement using the three-dimensional structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR