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EC Tree
IUBMB Comments Unlike EC 3.2.2.9, adenosylhomocysteine nucleosidase, this plant enzyme has little or no activity with S-adenosyl-L-homocysteine.
The taxonomic range for the selected organisms is: Staphylococcus aureus The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
5'-methylthioadenosine/s-adenosylhomocysteine nucleosidase, 5'-methylthioadenosine nucleosidase, mta/sah nucleosidase, methylthioadenosine nucleosidase, mta nucleosidase, bgp protein, methylthioadenosine/s-adenosylhomocysteine nucleosidase, glycosaminoglycan-binding protein, s-adenosylhomocysteine/5'-methylthioadenosine nucleosidase, 5-methylthioadenosine/s-adenosylhomocysteine nucleosidase,
more
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
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5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
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5'-methylthioadenosine nucleosidase
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
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MeSAdo nucleosidase
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methylthioadenosine/S-adenosylhomocysteine nucleosidase
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MTAN
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MTAN
MTAN is a dual substrate-specific enzyme that irreversibly hydrolyzes the glycosidic bond of 5'-methylthioadenosine or S-adenosyl-L-homocysteine
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S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine
early dissociative transition state
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hydrolysis of N-glycosyl bond
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S-methyl-5'-thioadenosine adeninehyrolase
Unlike EC 3.2.2.9, adenosylhomocysteine nucleosidase, this plant enzyme has little or no activity with S-adenosyl-L-homocysteine.
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5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
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?
S-adenosyl-L-homocysteine + H2O
S-D-ribosyl-L-homocysteine + adenine
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-
-
ir
S-methyl-5'-thioadenosine + H2O
S-methyl-5-thio-D-ribose + adenine
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-
-
?
5'-deoxyadenosine + H2O
5-deoxy-D-ribose + adenine
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-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-ribosyl-L-homocysteine + adenine
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-
-
-
?
S-methyl-5'-thioadenosine + H2O
adenine + S-methyl-5-thio-D-ribose
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-
-
-
?
S-methyl-5'-thioadenosine + H2O
S-methyl-5-thio-D-ribose + adenine
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-
-
-
?
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S-adenosyl-L-homocysteine + H2O
S-D-ribosyl-L-homocysteine + adenine
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-
-
ir
S-methyl-5'-thioadenosine + H2O
S-methyl-5-thio-D-ribose + adenine
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-
-
?
5'-deoxyadenosine + H2O
5-deoxy-D-ribose + adenine
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-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-ribosyl-L-homocysteine + adenine
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-
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?
S-methyl-5'-thioadenosine + H2O
adenine + S-methyl-5-thio-D-ribose
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?
S-methyl-5'-thioadenosine + H2O
S-methyl-5-thio-D-ribose + adenine
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?
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(3R,4S)-1-[9-deazaadenin-(9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
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4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
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analysis of Kd value, comparison with inhibition of Neisseria meningitides, Helicobacter pylori, Escherichia coli, Streptococcus pneumoniae and human enzyme
benzylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
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analysis of Kd value, comparison with inhibition of Neisseria meningitides, Helicobacter pylori, Escherichia coli, Streptococcus pneumoniae and human enzyme
ethylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
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analysis of Kd value, comparison with inhibition of Neisseria meningitides, Helicobacter pylori, Escherichia coli, Streptococcus pneumoniae and human enzyme
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
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analysis of Kd value, comparison with inhibition of Neisseria meningitides, Helicobacter pylori, Escherichia coli, Streptococcus pneumoniae and human enzyme
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0.00124
5'-methylthioadenosine
recombinant enzyme, in 50 mM potassium phosphate, pH 7.0
0.0009 - 0.0029
S-methyl-5'-thioadenosine
0.0009
S-methyl-5'-thioadenosine
wild type enzyme, at pH 7.2 and 25°C
0.0029
S-methyl-5'-thioadenosine
mutant enzyme F104C/C186S, at pH 7.2 and 25°C
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0.00973
5'-methylthioadenosine
recombinant enzyme, in 50 mM potassium phosphate, pH 7.0
7.2 - 10.2
S-methyl-5'-thioadenosine
7.2
S-methyl-5'-thioadenosine
mutant enzyme F104C/C186S, at pH 7.2 and 25°C
10.2
S-methyl-5'-thioadenosine
wild type enzyme, at pH 7.2 and 25°C
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2480 - 11300
S-methyl-5'-thioadenosine
2480
S-methyl-5'-thioadenosine
mutant enzyme F104C/C186S, at pH 7.2 and 25°C
11300
S-methyl-5'-thioadenosine
wild type enzyme, at pH 7.2 and 25°C
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SwissProt
brenda
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malfunction
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the deletion of the enzyme gene reduces bacterial clumping ability and results in the decreased biofilm formation. The gene mutation also significantly decreases the amount of eDNA present in the biofilm and the cell autolysis
physiological function
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the enzyme is essential for the virulence of Staphylococcus aureus. The enzyme is not essential for growth under nutrient-rich conditions, but is essential for AI-2 production
physiological function
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the enzyme promotes autolysis-dependent release of eDNA and biofilm formation
physiological function
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the enzyme is not essential for growth under nutrient-rich conditions, but is essential for AI-2 production. The enzyme is associated with Staphylococcus aureus subcutaneous abscess infection of mice
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dimer
biologically active dimer, X-ray crystallography
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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
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F104C/C186S
the mutant shows reduced activity compared to the wild type
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Ni-NTA column chromatography and Superdex 200 gel filtration
Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration
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expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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Gutierrez, J.A.; Luo, M.; Singh, V.; Li, L.; Brown, R.L.; Norris, G.E.; Evans, G.B.; Furneaux, R.H.; Tyler, P.C.; Painter, G.F.; Lenz, D.H.; Schramm, V.L.
Picomolar inhibitors as transition-state probes of 5-methylthioadenosine nucleosidases
ACS Chem. Biol.
2
725-734
2007
Escherichia coli, Helicobacter pylori, Neisseria meningitidis, Staphylococcus aureus, Streptococcus pneumoniae
brenda
Siu, K.K.; Lee, J.E.; Smith, G.D.; Horvatin-Mrakovcic, C.; Howell, P.L.
Structure of Staphylococcus aureus 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Acta Crystallogr. Sect. F
64
343-350
2008
Escherichia coli (P0AF14), Escherichia coli, Staphylococcus aureus (Q99TQ0), Staphylococcus aureus
brenda
Wang, S.; Thomas, K.; Schramm, V.L.
Catalytic site cooperativity in dimeric methylthioadenosine nucleosidase
Biochemistry
53
1527-1535
2014
Escherichia coli (P0AF12), Staphylococcus aureus (Q99TQ0), Staphylococcus aureus, Vibrio cholerae (A5F5R2)
brenda
Bao, Y.; Li, Y.; Jiang, Q.; Zhao, L.; Xue, T.; Hu, B.; Sun, B.
Methylthioadenosine/S-adenosylhomocysteine nucleosidase (Pfs) of Staphylococcus aureus is essential for the virulence independent of LuxS/AI-2 system
Int. J. Med. Microbiol.
303
190-200
2013
Staphylococcus aureus, Staphylococcus aureus NCTC 8325, Staphylococcus aureus RN4220
brenda
Bao, Y.; Zhang, X.; Jiang, Q.; Xue, T.; Sun, B.
Pfs promotes autolysis-dependent release of eDNA and biofilm formation in Staphylococcus aureus
Med. Microbiol. Immunol.
204
215-226
2015
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
brenda