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

glycolate
+
NADP+
=
glyoxylate
+
NADPH
+
H+

Synonyms

AtGR1, AtGR2, D-2-hydroxy-acid 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, More, 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 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
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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
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