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3.2.2.9: adenosylhomocysteine nucleosidase

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

Word Map on EC 3.2.2.9

Reaction

5'-deoxyadenosine
+
H2O
=
5-deoxy-D-ribose
 +
adenine

Synonyms

(adoHcy)/methylthioadenosine nucleosidase, 5'-dAdo nucleosidase, 5'-deoxyadenosine/5'-methylthioadenosine nucleosidase, 5'-methyladenosine nucleosidase, 5'-methylthioadenosine nucleosidase, 5'-methylthioadenosine nucleosidases, 5'-methylthioadenosine/S-adenosylhomocysteine, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 2, 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase, adenosylhomocysteine/methylthioadenosine nucleosidase, adoHcy/MeSAdo nucleosidase, adoHcy/MTA nucleosidase, Bgp, Bgp protein, BW246_00770, Cj0117, glycosaminoglycan-binding protein, K. pneumoniae MTA/SAH nucleosidase, methylthioadenosine nucleosidase, methylthioadenosine/S-adenosylhomocysteine nucleosidase, MKIGIIGA, MTA nucleosidase, MTA/AdoHcy nucleosidase, MTA/SAH nucleosidase, MTAN, Mtan-1, MTAN1, MTAN2, MTN1, MTN2, MtnN, nucleosidase, Pfs, Pfs protein, Pfs-2, Rv0091, S-adenosylhomocysteine nucleosidase, S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase, SAHN

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.9 adenosylhomocysteine nucleosidase

Crystallization

Crystallization on EC 3.2.2.9 - adenosylhomocysteine nucleosidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with S-adenosyl-L-homocysteine, to 1.4 A resolution
-
to 1.4 A resolution, trigonal space group P3121 or P3221, with unit-cell parameters a = b = 102.6, c = 118.7 A
-
structures of MtaN-1 in its apo form and in complex with substrates S-adenosyl-L-homocysteine, 5'-methylthioadenosine, and 5'-deoxyadenosine. MtaN-1 has an extension of the binding pocket and a tryptophan in the active site (Trp199) may play a major role in substrate binding
hanging drop vapor diffusion method, using 100 mM Bis-Tris (pH 6.5) and 26-32% (w/v) PEG MME 2000
isoform MTAN1 in complex with S-adenosyl-L-homocysteine, hanging drop vapor diffusion method, using 0.2 M NH4Cl, 18% (w/v) PEG3350, 15% (v/v) ethylene glycol
isozyme AtMTAN1 in complex with S-adenosyl-L-homocysteine, mixing of 0.004 ml of 10 mg/ml protein with 0.002 ml of precipitant solution containing 0.2 M NH4Cl, 18% w/v PEG 3350, 15% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.2 A resolution
isozyme AtMTAN2, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement, modelling
in complex with adenine, hanging drop vapor diffusion method, using 20% (w/v) PEG 1000, 0.1 M phosphate–citrate (pH 4.2) and 0.2 M Li2SO4
-
enzyme in complex with transition state analogue methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A. Enzyme forms a dimer with the methylthio group in a flexible hydrophobic pocket
-
hanging-drop vapor diffusion method. Three structures along the reaction coordinate of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase are solved: Asp197Asn 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5'-methylthioadenosine complex, Glu12Gln 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5-methylthioribose/adenine complex, and wild-type 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/glycerol complex. These structures provide insight into the conformational flexibility of the enzyme and nucleoside during catalysis
in complex with the transition-state analogue formycin A, hanging drop vapour diffusion method, using 50 mM potassium phosphate with 20% (w/v) PEG 8000
in complex with transition state analog formycin A and with substrate analog 5’-methylthiotubercidin
enzyme alone, in complex with formycin A and in complex with adenine, hanging drop vapor diffusion method, using 0.1 M Tris pH 8.5 and 16% (w/v) polyethyleneglycol 8000, at 18°C
enzyme only or in complex with formycin A or adenine, hanging drop vapor diffusion method, using 0.1 M Tris pH 8.5 and 16% (w/v) polyethyleneglycol 8000, at 18°C
hanging drop vapor diffusion method. Inactive D198N mutant bound to S-adenosyl-L-homocysteine and active enzyme bound to S-(5-deoxy-D-ribos-5-yl)-L-homocysteine and adenine using 0.05 M magnesium chloride hexahydrate, 0.1 M HEPES (pH 7.5), and 30% (v/v) PEG-MME 550
-
structure in complex with transition state analogue inhibitors
molecular modeling of structure and docking of inhibitors
in complex with the transition-state analogue formycin A, hanging drop vapour diffusion method, using 50 mM potassium phosphate with 20% (w/v) PEG 8000
enzyme in complex with transition state analogue methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A. Enzyme forms a dimer with the methylthio group in a flexible hydrophobic pocket
-
in complex with transition state analogues
5'-butylthio-DADMe-immucillinA-MTAN complex, by sitting drop vapor diffusion, at 18°C, to 2.3 A resolution. Structure of the MTAN monomer is a single mixed alpha/beta domain with central twisted nine-stranded mixed beta-sheet surrounded by six alpha-helices. Catalytic site is situated in a pocket formed by residues from beta10, a loop between beta8 and alpha4 and a loop contributed by the adjacent subunit. The catalytic site consists of the base binding site, the ribose binding site and the 5'-alkylthio-binding site
-
in complex with But-dadme-imma A, sitting drop vapour diffusion method, with 0.2 M potassium iodide and 20% (w/v) PEG3350
-