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1.17.1.4: xanthine dehydrogenase

This is an abbreviated version!
For detailed information about xanthine dehydrogenase, go to the full flat file.

Word Map on EC 1.17.1.4

Reaction

xanthine
+
NAD+
 +
H2O
=
Urate
 +
NADH
 +
H+

Synonyms

AtXDH1, EC 1.1.1.204, EC 1.2.1.37, IAO1, More, NAD-xanthine dehydrogenase, PaoABC, Retinol dehydrogenase, Rosy locus protein, VvXDH, xanthine dehydrogenase, xanthine dehydrogenase-1, xanthine dehydrogenase-2, xanthine dehydrogenase/oxidase, xanthine oxidoreductase, xanthine-NAD oxidoreductase, xanthine/NAD+ oxidoreductase, xanthine:NAD+ oxidoreductase, XDH, XDH/XO, XDH1, XDH2, XdhC, XOR, YagR, YagS, YagT

ECTree

     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.1 With NAD+ or NADP+ as acceptor
                1.17.1.4 xanthine dehydrogenase

Crystallization

Crystallization on EC 1.17.1.4 - xanthine dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.1 A resolution for both xanthine oxidase and dehydrogenase forms, irreversible pancreatin cleaved xanthine oxidase form results in blocking access of substrate NAD+ to the FAD cofactor
-
batch method, 2.5 and 3.3 A resolution for irreversible proteolytically cleaved xanthine oxidase form, 2.1 A resolution for dehydrogenase form
-
crystal structure determination
-
high-resolution crystal structure of XDH at 1.65 A resolution confirms the overall fold of the dimeric protein, the location of the cofactors and the mobile stretches of the polypeptide chain. Crystal structures of the NAD(H) complexes of XDH reveal that, given the proper oxidation states, the nicotinamide rings of the dinucleotides locate at van der Waals distance to the flavin ring
highly active bovine XOR in its XDH form is soaked in a large excess of NADH under strictly anaerobic conditions in order to reduce both FAD cofactor and iron sulfur centers and to block any electron transfer from the Mo center. The Mo ions in the crystal are fully reduced by soaking in 4 mM titanium citrate solution followed by 0.25 mM urate, crystal structure determination and analysis, superimposition, modelling
-
in complex with inhibitor FYX051, which is slowly hydroxylated by the enzyme
in complex with inhibotrs allopurinol, febuxostat, and FYX-051
-
in complex with TEI-6720
reduced enzyme in complex with oxipurinol at 2.0 A resolution. Electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor. Oxipurinol forms hydrogen bonds with residues E802, R880, and E1261
-
to 1.7 A resolution. The active site of PaoABC is highly exposed to the surface with no aromatic residues and an arginine (subunit PaoC-R440) making a direct interaction with subunit PaoC-E692, which acts as a base catalyst
crystal structure determination
-
mutant E803V, decrease in activity towards purine substrates is not due to large conformational change in the mutant protein
-
C535A/C992R/C1324S triple mutant XDH crystal structure analysis
-
crystal structure determination
-
mutant C535A/C992R/C1324S
-
mutant W335A/F336L, showing two similar, but not identical subunits. The cluster involved in conformation-switching is completely disrupted in one subunit, but remains partly associated in the other. Xanthine oxidase and oxidoreductase forms of the mutant are in equilibrium that greatly favors the oxidase form, but upon incubation with dithiothreitol equilibrium is partly shifted towards the oxidoreductase form
purified recombinant C-terminally truncated mutant enzyme, crystals of the mutant protein are prepared in two ways: (a) crystallization of the protein directly after DTT treatment and (b) crystallization in the presence of DTT followed by extended soaks in mother liquor devoid of DTT to convert most of the protein to the XO form, X-ray diffraction structure determination and analysis at 2.0 A resolution. Comparisons of crystal structures of a stable wild-type XDH enzyme form, the triple mutant C535A/C992R/C1324, and the DELTAC truncated mutant XOR
XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution
2.7 A resolution, direct coordination of alloxanthine to the molybdenum via a nitrogen atom
-
crystal structure determination
-
crystal structure determination of the free enzyme and the enzyme in complex with inhibitor alloxanthine
-
purified recombinant wild-type enzyme and subunit beta mutants E232A and E232Q with or without molybdenum cofactor, hanging drop vapor diffusion method, 15 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM EDTA, 200 mM NaCl,and 2.5 mM dithiothreitol are mixed 1 mM NAD+ and inhibitor pterin-6-aldehyde and with the reservoir solution containing 6-8 mM BaCl2, 6-8% polyethylene glycol 8000, 100 mM Tris-HCl, pH 8.3, 5-25mM dithiothreitol, and 3-4% isopropanol, whereas the EB232Q variant is mixed in a 1:2 ratio with the same reservoir solution, X-ray diffraction structure determination and analysis at 2.6-3.4 A resolution, overview