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Information on EC 3.2.2.9 - adenosylhomocysteine nucleosidase and Organism(s) Escherichia coli and UniProt Accession P0AF12
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3.2.2.9 adenosylhomocysteine nucleosidaseIUBMB Comments
This enzyme, found in bacteria and plants, acts on three different substrates. It is involved in the S-adenosyl-L-methionine (SAM, AdoMet) cycle, which recycles S-adenosyl-L-homocysteine back to SAM, and in salvage pathways for 5'-deoxyadenosine and S-methyl-5'-thioadenosine, which are produced from SAM during the action of many enzymes. cf. the plant enzyme EC 3.2.2.16, methylthioadenosine nucleosidase.
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Word Map
- 3.2.2.9
-
mtans
- formycin
- medicine
- autoinducer-2
-
adomet-dependent
-
n-ribosidic
-
5\'-methylthiotubercidin
- 5-methylthioribose
- analysis
- drug development
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(3 overall reactions are displayed. Show all (4)>>)
Synonyms
nucleosidase, pfs-2, mta/adohcy nucleosidase, rv0091, s-adenosylhomocysteine nucleosidase, 5'-methylthioadenosine/s-adenosylhomocysteine, mtan-1, 5'-methylthioadenosine nucleosidases, 5'-deoxyadenosine/5'-methylthioadenosine nucleosidase, adenosylhomocysteine nucleosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-methyladenosine nucleosidase
-
-
-
-
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
adoHcy/MTA nucleosidase
MTA/SAH nucleosidase
MTAN
S-adenosylhomocysteine nucleosidase
-
-
-
-
S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
-
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
dual substrate enzyme
adoHcy/MTA nucleosidase
-
-
-
-
MTA/SAH nucleosidase
-
-
-
-
MTAN
MTAN is a dual substrate-specific enzyme that irreversibly hydrolyzes the glycosidic bond of 5'-methylthioadenosine or S-adenosyl-L-homocysteine
S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-homocysteine homocysteinylribohydrolase
This enzyme, found in bacteria and plants, acts on three different substrates. It is involved in the S-adenosyl-L-methionine (SAM, AdoMet) cycle, which recycles S-adenosyl-L-homocysteine back to SAM, and in salvage pathways for 5'-deoxyadenosine and S-methyl-5'-thioadenosine, which are produced from SAM during the action of many enzymes. cf. the plant enzyme EC 3.2.2.16, methylthioadenosine nucleosidase.
CAS REGISTRY NUMBER
COMMENTARY
9055-10-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
-
-
-
?
2'-deoxy-2'-fluoro-5'-deoxy-5'-(methylthio)adenosine + H2O
adenine + ?
-
F-MeSAdo, slow substrate
-
-
?
2'-deoxymethylthioadenosine + H2O
adenine + 2-deoxymethylthioribose
-
fairly good substrate
-
-
?
5'-ethylthioadenosine + H2O
adenine + 5-ethylthio-D-ribose
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 118%
-
-
?
5'-isobutylthioadenosine + H2O
adenine + 5-isobutylthioribose
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 52%
-
-
?
5'-methylthioadenosine + H2O
?
-
-
-
-
?
5'-n-propylthioadenosine + H2O
adenine + 5-n-propylthioribose
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 106%
-
-
?
S-2-aza-adenosylhomocysteine + H2O
2-azaadenine + 5-(S-L-homocysteinyl)ribose
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 27%
-
-
?
S-adenosyl-D-homocysteine + H2O
adenine + 5-(S-D-homocysteinyl)ribose
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 26%
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + 5-ribosyl-L-homocysteine
-
-
-
-
?
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
-
-
-
?
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
-
-
137135, 171850, 171851, 171852, 171854, 171856, 171858, 171859, 667625, 669334, 678158, 715849, 716263
-
-
?
S-adenosyl-L-homocysteine + H2O
?
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
?
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 35%
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 35%
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 42%
-
-
?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
-
42% activity compared to 5'-methylthioadenosine
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is involved in quorum sensing, recycling 5'-methylthioadenosine from the polyamine pathway via adenine phosphoribosyltransferase and recycling 5-methylthioribose to methionine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
-
-
-
-
?
5'-methylthioadenosine + H2O
?
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + 5-ribosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
-
-
-
-
?
additional information
?
-
-
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is involved in quorum sensing, recycling 5'-methylthioadenosine from the polyamine pathway via adenine phosphoribosyltransferase and recycling 5-methylthioribose to methionine
-
-
?
S-adenosyl-L-homocysteine + H2O
?
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
?
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 35%
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(1H-1,2,3-triazol-4-yl)pyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(penta-3-yl)pyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-isobutylpyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-phenylpyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethynyl-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-(1-benzyl-1H-1,2,3-triazol-4-yl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-(cyclohexylmethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-cyclopentyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-cyclopropyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-[3-(benzylthio)propyl]-1-[(9-deazaadenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenylthio)-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenylthio)-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
-
-
(1S)-5-(4-chlorophenylthio)-1-(9-deaza-adenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
-
-
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
-
-
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
-
(2R,3R)-2-([[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]methyl)-4-(methylsulfanyl)butane-1,3-diol
-
-
(2R,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
-
(2R,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
-
(2R,3S)-4-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-3-[(methylsulfanyl)methyl]butane-1,2-diol
-
-
(2S)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-2-ol
-
-
(2S)-2-[[(1S)-1-(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)-2-hydroxyethyl]amino]-3-(methylsulfanyl)propan-1-ol
-
-
(2S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
-
(2S,3R)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-4-(methylsulfanyl)butane-2,3-diol
-
-
(2S,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
-
(2S,3R)-N-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-3,4-dihydroxy-2-[(methylsulfanyl)methyl]butan-1-aminium trifluoroacetate
-
-
(2S,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
-
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]3-hydroxy-4-methylthiomethylpyrrolidine
-
-
(3R,4S)-4-(1-butylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(3R,4S)-4-(4-chlorophenyl-thiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
potential antibiotic to interfere with the metabolic pathways involved in methylation, polyamine biosynthesis, methionine recycling, and quorum sensing pathways
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-2-[(methylsulfanyl)methyl]propane-1,3-diol
-
-
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
-
-
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
-
additional information
-
the transition state structure of the enzyme predictes that transition state analogue inhibitors resembling 5'-methylthioadenosine with riboxacarbenium features in the ribosyl group and elevated pKa values in the leaving group adenine analogue would be powerful inhibitors
-
additional information
-
not inhibited by 5'-methylthioinosine, S-inosyl-L-homocysteine, S-guanosyl-L-homocysteine, S-N6-methyl-3-deaza-adenosyl-L-homocysteine, S-adenosyl-L-homocysteine dialdehyde, acyclic adenosyl-L-homocysteine, S-cytidylhomocysteine, hypoxanthine, guanine, and AMP
-
additional information
-
not inhibited by 5-methylthioribose, 5-trifluoromethylthioribose, 5-(4-iodophenyl)thioribose, adenosine, erythro-9-(2-hydroxy-3-nonyl)adenine, and inosine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics and thermodynamics of wild-type and mutant enzyme, overview
-
0.00143
5'-methylthioadenosine
-
rMTAN-8, truncated enzyme, lacking first 8 amino acids
0.0043
S-adenosyl-L-homocysteine
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0053
S-adenosyl-L-homocysteine
recombinant enzyme, in 50 mM potassium phosphate, pH 7.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
S-adenosyl-L-homocysteine
recombinant enzyme, in 50 mM potassium phosphate, pH 7.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
(+/-)-cis-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.002
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(1H-1,2,3-triazol-4-yl)pyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.0007
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(penta-3-yl)pyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000047
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-isobutylpyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00003
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-phenylpyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00065
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-vinylpyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00039
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethynyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000064
(+/-)-trans-4-(1-benzyl-1H-1,2,3-triazol-4-yl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000059
(+/-)-trans-4-(cyclohexylmethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00035
(+/-)-trans-4-allyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000009
(+/-)-trans-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000013
(+/-)-trans-4-cyclopentyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000063
(+/-)-trans-4-cyclopropyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000054
(+/-)-trans-4-[3-(benzylthio)propyl]-1-[(9-deazaadenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00084
(+/-)trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000000009 - 0.000000015
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenylthio)-D-ribitol
0.000000008 - 0.000000018
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenylthio)-D-ribitol
0.00000008
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
-
pH and temperature not specified in the publication
0.000000002 - 0.000000006
(1S)-5-(4-chlorophenylthio)-1-(9-deaza-adenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
0.0000017
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
-
pH and temperature not specified in the publication
0.00000023
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
pH and temperature not specified in the publication
0.000401
(2R,3R)-2-([[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]methyl)-4-(methylsulfanyl)butane-1,3-diol
-
pH and temperature not specified in the publication
0.00001
(2R,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
pH and temperature not specified in the publication
0.0000008
(2R,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
pH and temperature not specified in the publication
0.0023
(2R,3S)-4-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-3-[(methylsulfanyl)methyl]butane-1,2-diol
-
pH and temperature not specified in the publication
0.00004
(2S)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-2-ol
-
pH and temperature not specified in the publication
0.00172
(2S)-2-[[(1S)-1-(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)-2-hydroxyethyl]amino]-3-(methylsulfanyl)propan-1-ol
-
pH and temperature not specified in the publication
0.0000011
(2S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
pH and temperature not specified in the publication
0.000202
(2S,3R)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-4-(methylsulfanyl)butane-2,3-diol
-
pH and temperature not specified in the publication
0.0000039
(2S,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
pH and temperature not specified in the publication
0.000009
(2S,3R)-N-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-3,4-dihydroxy-2-[(methylsulfanyl)methyl]butan-1-aminium trifluoroacetate
-
pH and temperature not specified in the publication
0.0000021
(2S,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
pH and temperature not specified in the publication
0.000000002 - 0.000000048
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
0.00031
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000000002
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]3-hydroxy-4-methylthiomethylpyrrolidine
-
pH and temperature not specified in the publication
0.0000000003
(3R,4S)-4-(1-butylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH and temperature not specified in the publication
0.000000000047 - 0.000000026
(3R,4S)-4-(4-chlorophenyl-thiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
0.00000000046 - 0.000000028
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
0.0000034
(3R,4S)-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.0000058
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-2-[(methylsulfanyl)methyl]propane-1,3-diol
-
pH and temperature not specified in the publication
0.00000036
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
-
pH and temperature not specified in the publication
0.00000036
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
pH 7.5, 25°C
0.00017
5'-(4-iodophenyl)thioadenosine
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00002
5'-(4-nitrophenyl)thioadenosine
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.000322
5'-Chloroformycin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.000027
5'-Methylthioformycin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.000024
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
pH 7.5, 25°C
0.000928
S-8-aza-adenosyl-L-homocysteine
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0024
S-adenosyl-L-homocysteine
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0000097
S-formycinylhomocysteine
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0019
S-Tubercidinylhomocysteine
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.000000009
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenylthio)-D-ribitol
-
25°C, pH 7.0,dissociation constant for the equilibrium complex of enzyme-inhibitor following slow-onset inhibition
0.000000015
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenylthio)-D-ribitol
-
25°C, pH 7.0, dissociation constant for the equilibrium between enzyme and inhibitor before slow-onset inhibition
0.000000008
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenylthio)-D-ribitol
-
25°C, pH 7.0, dissociation constant for the equilibrium between enzyme and inhibitor before slow-onset inhibition
0.000000018
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenylthio)-D-ribitol
-
25°C, pH 7.0, dissociation constant for the equilibrium between enzyme and inhibitor before slow-onset inhibition
0.000000002
(1S)-5-(4-chlorophenylthio)-1-(9-deaza-adenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
-
25°C, pH 7.0,dissociation constant for the equilibrium complex of enzyme-inhibitor following slow-onset inhibition
0.000000006
(1S)-5-(4-chlorophenylthio)-1-(9-deaza-adenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
-
25°C, pH 7.0, dissociation constant for the equilibrium between enzyme and inhibitor before slow-onset inhibition
0.000000002
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
-
25°C, pH 7.0, dissociation constant for the equilibrium complex of enzyme-inhibitor following slow-onset inhibition
0.000000048
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
-
25°C, pH 7.0, dissociation constant for the equilibrium between enzyme and inhibitor before slow-onset inhibition
0.000000000047
(3R,4S)-4-(4-chlorophenyl-thiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
25°C, pH 7.0, dissociation constant for the equilibrium complex of enzyme-inhibitor following slow-onset inhibition
0.000000026
(3R,4S)-4-(4-chlorophenyl-thiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
25°C, pH 7.0, dissociation constant for the equilibrium between enzyme and inhibitor before slow-onset inhibition
0.00000000046
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
25°C, pH 7.0, dissociation constant for the equilibrium complex of enzyme-inhibitor following slow-onset inhibition
0.000000028
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
25°C, pH 7.0, dissociation constant for the equilibrium between enzyme and inhibitor before slow-onset inhibition
0.00075
5'-methylthiotubercidin
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0041
5'-methylthiotubercidin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00037
5'-(4-aminophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00085
5'-(4-bromophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0002
5'-(4-chlorophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0009
5'-(4-fluorophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00022
5'-(4-iodophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00013
5'-(4-nitrophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00068
5'-butylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0004
5'-Chloroformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0068
5'-dimethylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0009
5'-ethylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.013
5'-isobutylthio-3-deaza-adenosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00074
5'-isobutylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.132
5'-Isobutylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0011
5'-Isopropylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0045
5'-Methylselenoadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.079
5'-methylthio-3-deaza-adenosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.001
5'-methylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00006
5'-Methylthioformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.094
5'-n-butylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00088
5'-phenylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00058
5'-propylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0047
5'-purinothioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.027
carbocyclic 5'-methylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0018
S-8-aza-adenosyl-L-homocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.002 - 4
S-adenosyl-L-homocysteine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.069
S-adenosyl-L-homocysteine sulfoxide
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00002
S-formycinylhomocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.02
S-N6-dimethyl-3-deaza-adenosyl-L-homocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0032
S-Tubercidinylhomocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0033
5'-methylthiotubercidin
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0077
5'-methylthiotubercidin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0152
-
crude extract, with S-adenosyl-L-homocysteine as substrate, in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
156
additional information
-
enzyme-coupled continuous spectrophotometric assay to quantitatively characterize S-adenosyl-L-methionine (AdoMet/SAM)-dependent methyltransferase activity. In this assay, S-adenosyl-L-homocysteine, the transmethylation product of AdoMet-dependent methyltransferases, is hydrolyzed to S-ribosylhomocysteine and adenine by recombinant S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Subsequently, adenine generated from AdoHcy is further hydrolyzed to hypoxanthine and ammonia by recombinant adenine deaminase
156
-
after 9810fold purification, with S-adenosyl-L-homocysteine as substrate, in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
optimal pH for both natural substrates, 5'-methylthioadenosine and S-adenosyl-L-homocysteine, with little variation from pH 5.7-7.1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
deletion of the SAHN gene abolishes the production of the quorum sensing signal AI-2 and biofilm formation
metabolism
-
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase plays a key role in the methionine-recycling pathway of bacteria and plants
physiological function
-
the enzyme is involved in the synthesis of 4,5-dihdroxy-2,3-pentanedione from methionine. S-adenosyl-L-homocysteine hydrolysis by MTA/SAH nucleosidase yields S-(5-deoxy-D-ribos-5-yl)-L-homocysteine, a precursor of autoinducer-2 synthesis, a quorum-sensing signal that governs a variety of bacterial phenotypes such as virulence and biofilm formation
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26030
-
2 * 26030, calculated from amino acid sequence and acquired by nanoESI-QTOF mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
2 * 26030, calculated from amino acid sequence and acquired by nanoESI-QTOF mass spectrometry
additional information
-
structure comparison of MTAN from Escherichia coli with the isozyme AtMTAN1 of Arabidopsis thaliana, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 transition state analog formycin A and with substrate analog 5-methylthiotubercidin
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 the transition-state analogue formycin A, hanging drop vapour diffusion method, using 50 mM potassium phosphate with 20% (w/v) PEG 8000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D197A
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
D197N
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
E12A
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
E12Q
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
E174A
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
E174Q
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
F105A
kcat/Km for 5'-methylthioadenosine is 87.4% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 128% of wild-type value
F151A
kcat/Km for 5'-methylthioadenosine is 0.5% of wild-type value kcat/Km for S-adenosyl-L-homocysteine is 0.2% of wild-type value
F207A
kcat/Km for 5'-methylthioadenosine is 2.2% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 2.7% of wild-type value
I50A
kcat/Km for 5'-methylthioadenosine is 11.8% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 23.3% of wild-type value
M173A
kcat/Km for 5'-methylthioadenosine is 0.6% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 0.1% of wild-type value
M9A
kcat/Km for 5'-methylthioadenosine is 12.6% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 18.6% of wild-type value
R193A
kcat/Km for 5'-methylthioadenosine is 12.9% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 28.1% of wild-type value
S196A
kcat/Km for 5'-methylthioadenosine is 2.3% of wild-type value kcat/Km for S-adenosyl-L-homocysteine is 4% of wild-type value
S76A
kcat/Km for 5'-methylthioadenosine is 13.4% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 22.9% of wild-type value
V102A
kcat/Km for 5'-methylthioadenosine is 95% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 233% of wild-type value
Y107F
kcat/Km for 5'-methylthioadenosine is 32.2% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 58.1% of wild-type value
E174Q
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 55
-
significant substrate conversion is seen even at 4°C. Activity is also seen at higher temperatures than 45°C, however the enzyme is rapidly inactivated (about 90%) after incubation at 55°C for 10 min
60
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°, repeatedly frozen and thawed without loss of activity over a 9 months period, upon storage at 4°C only 50% of activity retained after 3 weeks
-
-20°C, 50 mM potassium phosphate buffer (pH 7.0), at least 2 months, no significant loss of activity
-
0°C, 0.1 M phosphate buffer containing 0.009 M 2-mercaptoethanol and 0.0005 M EDTA stable for 2 weeks, retains 80% of its total activity after 2 weeks at -40°C
-
0°C, loses 50% activity in 48 h, -20°C very unstable, lost nearly all activity when stored for 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sephadex gel filtration, hydroxyapatite column chromatography, S-formycinylhomocysteine-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration
recombinant wild-type and mutant His-tagged MTAN from strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene encoding the enzyme cloned and recombinant MTA/SAH nucleosidase rMTAN expressed
-
overexpression of wild-type and mutant His-tagged enzyme in strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is thought to be an ideal target for therapeutic drug design as the enzyme is present in many microbes but not in mammals. The inhibition of MTAN leads to a build-up of toxic byproducts that affect various microbial pathways such as quorum sensing, biological methylation, polyamine biosynthesis, and methionine recycling. The design of nucleosidase-specific inhibitors is complicated by its structural similarity to the human MTA phosphorylase. Structural comparison of 5'-methylthioadenosine phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
analysis
medicine
analysis
-
adaptation of an enzyme-coupled colorimetric assay based on the quantification of homocysteine produced from S-adenosyl-L-homocysteine in presence of enzyme and S-ribosylhomocysteinase to cyclopropane fatty acid synthase for high-throughput screening of compound libraries
analysis
-
enzyme-coupled continuous spectrophotometric assay to quantitatively characterize S-adenosyl-L-methionine (AdoMet/SAM)-dependent methyltransferase activity. In this assay, S-adenosyl-L-homocysteine, the transmethylation product of AdoMet-dependent methyltransferases, is hydrolyzed to S-ribosylhomocysteine and adenine by recombinant S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Subsequently, adenine generated from AdoHcy is further hydrolyzed to hypoxanthine and ammonia by recombinant adenine deaminase. Application of the assay to other enzymes that produce S-adenosylhomocysteine
medicine
-
potential target for chemotherapeutic intervention, nucleoside analogues which inhibit the nucleosidase could kill invading microorganisms by perturbing methylation processes and polyamine levels
medicine
-
inhibitors of methylthioadenosine/S-adenosylhomocysteine nucleosidase are anti-infective drugs against various bacterial pathogens
REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walker, R.D.; Duerre, J.A.
S-Adenosylhomocysteine metabolism in various species
Can. J. Biochem.
53
312-319
1975
Alcaligenes faecalis, Bacillus mycoides, Citrobacter freundii, Escherichia coli, Escherichia coli W-ATCC 963, Klebsiella aerogenes, Micrococcus luteus, Proteus vulgaris, Rattus rattus, Staphylococcus aureus
Duerre, J.A.
A hydrolytic nucleosidase acting on S-adenosylhomocysteine and on 5'-methylthioadenosine
J. Biol. Chem.
237
3737-3741
1962
Escherichia coli, Escherichia coli B / ATCC 11303, Klebsiella aerogenes, Salmonella enterica subsp. enterica serovar Typhimurium
-
Ferro, A.J.; Barrett, A.; Shapiro, S.K.
Kinetic properties and the effect of substrate analogues on 5'-methylthioadenosine nucleosidase from Escherichia coli
Biochim. Biophys. Acta
438
487-494
1976
Escherichia coli, Escherichia coli B / ATCC 11303, Rattus rattus
Duerre, J.A.
S-Adenosylhomocysteine nucleosidase (Escherichia coli)
Methods Enzymol.
17
411-415
1971
Klebsiella aerogenes, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
-
Della Ragione, F.; Porcelli, M.; Carteni-Farina, M.; Zappia, V.
Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidasepurification, substrate specificity and mechanisms of action
Biochem. J.
232
335-341
1985
Escherichia coli
Cornell, K.A.; Winter, R.W.; Tower, P.A.; Riscoe, M.K.
Affinity purification of 5-methylthioadenosine kinase and 5-methylthioribose/S-adenosylhomocysteine nucleosidase from Klebsiella pneumoniae
Biochem. J.
317
285-290
1996
Escherichia coli, Klebsiella aerogenes, Klebsiella pneumoniae, Lupinus luteus
Cornell, K.A.; Swarts, W.E.; Barry, R.D.; Riscoe, M.K.
Characterization of recombinant Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: Analysis of enzymatic activity and substrate specificity
Biochem. Biophys. Res. Commun.
228
724-732
1996
Escherichia coli, Escherichia coli XL1-Blue
Allart, B.; Gatel, M.; Guillerm, D.; Guillerm, G.
The catalytic mechanism of adenosylhomocysteine/methylthioadenosine nucleosidase from Escherichia coli
Eur. J. Biochem.
256
155-162
1998
Escherichia coli
Cornell, K.A.; Riscoe, M.K.
Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: Identification of the pfs gene product
Biochim. Biophys. Acta
1396
8-14
1998
Escherichia coli, Klebsiella pneumoniae
Allart, B.; Guillerm, D.; Guillerm, G.
On the catalytic mechanism of adenosylhomocysteine/methylthioadenosine nucleosidase from E. coli
Nucleosides Nucleotides
18
861-862
1999
Escherichia coli
Lee, J.E.; Cornell, K.A.; Riscoe, M.K.; Howell, P.L.
Structure of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis
J. Biol. Chem.
278
8761-8770
2003
Escherichia coli (P0AF12), Escherichia coli
Lee, J.E.; Settembre, E.C.; Cornell, K.A.; Riscoe, M.K.; Sufrin, J.R.; Ealick, S.E.; Howell, P.L.
Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
Biochemistry
43
5159-5169
2004
Escherichia coli (P0AF12), Escherichia coli
Lee, J.E.; Luong, W.; Huang, D.J.; Cornell, K.A.; Riscoe, M.K.; Howell, P.L.
Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis
Biochemistry
44
11049-11057
2005
Escherichia coli (P0AF12)
Singh, V.; Lee, J.E.; Nunez, S.; Howell, P.L.; Schramm, V.L.
Transition state structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues
Biochemistry
44
11647-11659
2005
Escherichia coli
Singh, V.; Evans, G.B.; Lenz, D.H.; Mason, J.M.; Clinch, K.; Mee, S.; Painter, G.F.; Tyler, P.C.; Furneaux, R.H.; Lee, J.E.; Howell, P.L.; Schramm, V.L.
Femtomolar transition state analogue inhibitors of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli
J. Biol. Chem.
280
18265-18273
2005
Escherichia coli
Lee, J.E.; Smith, G.D.; Horvatin, C.; Huang, D.J.; Cornell, K.A.; Riscoe, M.K.; Howell, P.L.
Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis
J. Mol. Biol.
352
559-574
2005
Escherichia coli (P0AF12)
Dorgan, K.M.; Wooderchak, W.L.; Wynn, D.P.; Karschner, E.L.; Alfaro, J.F.; Cui, Y.; Zhou, Z.S.; Hevel, J.M.
An enzyme-coupled continuous spectrophotometric assay for S-adenosylmethionine-dependent methyltransferases
Anal. Biochem.
350
249-255
2006
Escherichia coli
Singh, V.; Shi, W.; Almo, S.C.; Evans, G.B.; Furneaux, R.H.; Tyler, P.C.; Painter, G.F.; Lenz, D.H.; Mee, S.; Zheng, R.; Schramm, V.L.
Structure and inhibition of a quorum sensing target from Streptococcus pneumoniae
Biochemistry
45
12929-12941
2006
Escherichia coli, Streptococcus pneumoniae
Guianvarch, D.; Drujon, T.; Leang, T.E.; Courtois, F.; Ploux, O.
Identification of new inhibitors of E. coli cyclopropane fatty acid synthase using a colorimetric assay
Biochim. Biophys. Acta
1764
1381-1388
2006
Escherichia coli
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
Siu, K.K.; Asmus, K.; Zhang, A.N.; Horvatin, C.; Li, S.; Liu, T.; Moffatt, B.; Woods, V.L.; Howell, P.L.
Mechanism of substrate specificity in 5-methylthioadenosine/S-adenosylhomocysteine nucleosidases
J. Struct. Biol.
173
86-98
2011
Arabidopsis thaliana (Q9T0I8), Escherichia coli
Longshaw, A.I.; Adanitsch, F.; Gutierrez, J.A.; Evans, G.B.; Tyler, P.C.; Schramm, V.L.
Design and synthesis of potent sulfur-free transition state analogue inhibitors of 5'-methylthioadenosine nucleosidase and 5'-methylthioadenosine phosphorylase
J. Med. Chem.
53
6730-6746
2010
Escherichia coli
Parveen, N.; Cornell, K.A.
Methylthioadenosine/S-adenosylhomocysteine nucleosidase, a critical enzyme for bacterial metabolism
Mol. Microbiol.
79
7-20
2011
Borreliella burgdorferi, Escherichia coli
Clinch, K.; Evans, G.B.; Froehlich, R.F.; Gulab, S.A.; Gutierrez, J.A.; Mason, J.M.; Schramm, V.L.; Tyler, P.C.; Woolhouse, A.D.
Transition state analogue inhibitors of human methylthioadenosine phosphorylase and bacterial methylthioadenosine/S-adenosylhomocysteine nucleosidase incorporating acyclic ribooxacarbenium ion mimics
Bioorg. Med. Chem.
20
5181-5187
2012
Escherichia coli, Neisseria meningitidis
Wang, S.; Lim, J.; Thomas, K.; Yan, F.; Angeletti, R.H.; Schramm, V.L.
A complex of methylthioadenosine/S-adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry
J. Am. Chem. Soc.
134
1468-1470
2012
Escherichia coli
Han, T.; Li, Y.; Shan, Q.; Liang, W.; Hao, W.; Li, Y.; Tan, X.; Gu, J.
Characterization of S-adenosylhomocysteine/Methylthioadenosine nucleosidase on secretion of AI-2 and biofilm formation of Escherichia coli
Microb. Pathog.
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2017
Escherichia coli (P0AF12), Escherichia coli, Mycobacterium tuberculosis (P9WJM3), Mycobacterium tuberculosis H37Rv (P9WJM3)
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