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Literature summary extracted from

  • Siu, K.K.; Lee, J.E.; Smith, G.D.; Horvatin-Mrakovcic, C.; Howell, P.L.
    Structure of Staphylococcus aureus 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase (2008), Acta Crystallogr. Sect. F, 64, 343-350.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.9 expressed in Escherichia coli BL21 (DE3) cells Staphylococcus aureus
3.2.2.16 expressed in Escherichia coli BL21 (DE3) cells Staphylococcus aureus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.9 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 Staphylococcus aureus
3.2.2.9 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 Escherichia coli
3.2.2.16 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 Staphylococcus aureus
3.2.2.16 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 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.9 0.00252
-
 S-adenosyl-L-homocysteine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Staphylococcus aureus
3.2.2.9 0.0053
-
 S-adenosyl-L-homocysteine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Escherichia coli
3.2.2.16 0.00124
-
 5'-methylthioadenosine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Staphylococcus aureus
3.2.2.16 0.00738
-
 5'-methylthioadenosine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.9 Escherichia coli P0AF14
-
-
3.2.2.9 Staphylococcus aureus Q99TQ0
-
-
3.2.2.16 Escherichia coli P0AF14
-
-
3.2.2.16 Staphylococcus aureus Q99TQ0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.9 Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration Staphylococcus aureus
3.2.2.9 Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration Escherichia coli
3.2.2.16 Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration Staphylococcus aureus
3.2.2.16 Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.9 S-adenosyl-L-homocysteine + H2O
-
 Staphylococcus aureus adenine + S-ribosyl-L-homocysteine
-
 ?
3.2.2.9 S-adenosyl-L-homocysteine + H2O
-
 Escherichia coli adenine + S-ribosyl-L-homocysteine
-
 ?
3.2.2.16 5'-methylthioadenosine + H2O
-
 Staphylococcus aureus 5-methylthio-D-ribose + adenine
-
 ?
3.2.2.16 5'-methylthioadenosine + H2O
-
 Escherichia coli 5-methylthio-D-ribose + adenine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.2.9 dimer biologically active dimer, X-ray crystallography Staphylococcus aureus
3.2.2.16 dimer biologically active dimer, X-ray crystallography Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
3.2.2.9 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
 Staphylococcus aureus
3.2.2.9 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
 Escherichia coli
3.2.2.9 MTAN MTAN is a dual substrate-specific enzyme that irreversibly hydrolyzes the glycosidic bond of 5'-methylthioadenosine or S-adenosyl-L-homocysteine Staphylococcus aureus
3.2.2.9 MTAN MTAN is a dual substrate-specific enzyme that irreversibly hydrolyzes the glycosidic bond of 5'-methylthioadenosine or S-adenosyl-L-homocysteine Escherichia coli
3.2.2.16 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
 Staphylococcus aureus
3.2.2.16 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
 Escherichia coli
3.2.2.16 MTAN MTAN is a dual substrate-specific enzyme that irreversibly hydrolyzes the glycosidic bond of 5'-methylthioadenosine or S-adenosyl-L-homocysteine Staphylococcus aureus
3.2.2.16 MTAN MTAN is a dual substrate-specific enzyme that irreversibly hydrolyzes the glycosidic bond of 5'-methylthioadenosine or S-adenosyl-L-homocysteine Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.2.9 0.00873
-
 S-adenosyl-L-homocysteine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Staphylococcus aureus
3.2.2.9 0.45
-
 S-adenosyl-L-homocysteine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Escherichia coli
3.2.2.16 0.00973
-
 5'-methylthioadenosine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Staphylococcus aureus
3.2.2.16 0.49
-
 5'-methylthioadenosine recombinant enzyme, in 50 mM potassium phosphate, pH 7.0 Escherichia coli