Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.2.2.16: methylthioadenosine nucleosidase

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

Word Map on EC 3.2.2.16

Reaction

S-methyl-5'-thioadenosine
+
H2O
=
S-methyl-5-thio-D-ribose
 +
adenine

Synonyms

5'-deoxy-5'-methylthioadenosine nucleosidase, 5'-methylthioadenosine nucleosidase, 5'-methylthioadenosine/S-adenosyl-L-homocysteine nucleosidase, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, 5-methylthioadenosine nucleosidase, 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase, 50-methylthioadenosine/S-adenosylhomocysteine nucleosidase, adoHcy/MTA nucleosidase, Bgp protein, glycosaminoglycan-binding protein, HpyMqnB, lupin MeSAdo nucleosidase, MeSAdo nucleosidase, methylthioadenosine nucleosidase, methylthioadenosine/S-adenosylhomocysteine nucleosidase, MqnB, MTA nucleosidase, MTA ribohydrolase, MTA/SAH nucleosidase, MTAN, MTAN1, MTAN2, MTN, Pfs, Pfs protein, plant specific MTA nucleosidase, S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.16 methylthioadenosine nucleosidase

Crystallization

Crystallization on EC 3.2.2.16 - methylthioadenosine nucleosidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme as well as in complex with substrate-and transition-state-analogues 5'-methylthiotubercidin and formycin A, at 2.0-1.8 A resolution. Comparison with isoform MTAN2
-
at 1.5 A resolution, comparison with Escherichia coli enzyme structure
-
crystal structure comparison of MTAN from Escherichia coli with the isozyme AtMTAN1 from Arabidopsis thaliana, overview
-
homology model of structure based on isoform MTAN1
-
in complex with 5'-methylthiotubercidin or formycin A, hanging drop vapour diffusion method, in 70 mM sodium acetate trihydrate, pH 4.6, 5.6% (w/v) PEG 4000, 30% (v/v) glycerol
-
isozymes AtMTAN1 and AtMTAN2, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement, modelling
-
in complex with its product 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
crystal structure analysis, PDB entry 1Y6Q and PDB entry 1Z5P
-
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
-
hanging drop vapor diffusion method, complexed with formycin A and 5'-methylthiotubercidin
-
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
sitting drop vapor diffusion method, using
hanging drop vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M HEPES pH 7.5 and 25% (w/v) PEG 3350 or 0.05 M magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5 and 30% (v/v) PEG-MME 550
purified recombinant wild-type and mutant enzymes, sitting drop vapour diffusion method, mixing of 50 mg/ml protein in 10 mM Tris-HCl, pH 8.0, with 4.0 M NaH2PO4/K2HPO4, pH 7.0, using a 1:1 ratio of protein to mother liquor, X-ray diffraction structure determination and analysis at 1.65-2.11 A resolution, molecular replacement. for the mutant enzymess th following crystallization slutions are used: for E14Q 0.1 M HEPES, pH 7.5, 25% PEG 3350, 0.2 M NaCl, for D199N 0.1 M bis-Tris, pH 5.5, 25% PEG 3350, 0.2 M MgCl2 x 6H2O, and for D199A 0.1 M bis-Tris, pH 6.5, 25% PEG 3350, 0.2 M Li2SO4 xH2O
sitting drop vapor diffusion method, over 4.0 M NaH2PO4/K2HPO4 pH 7.0
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
sitting drop vapor diffusion method
in complex with But-dadme-imma A, sitting drop vapour diffusion method, with 0.2 M potassium iodide and 20% (w/v) PEG3350
-