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Information on EC 3.2.2.30 - aminodeoxyfutalosine nucleosidase and Organism(s) Escherichia coli and UniProt Accession P0AF12

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.30 aminodeoxyfutalosine nucleosidase
IUBMB Comments
The enzyme, found in several bacterial species, catalyses a step in a modified futalosine pathway for menaquinone biosynthesis. While the enzyme from some organisms also has the activity of EC 3.2.2.9, adenosylhomocysteine nucleosidase, the enzyme from Chlamydia trachomatis is specific for 6-amino-6-deoxyfutalosine .
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This record set is specific for:
Escherichia coli
UNIPROT: P0AF12
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 2, 6-amino-6-deoxyfutalosine hydrolase, adoHcy/MTA nucleosidase, AFL nucleosidase, aminofutalosine nucleosidase, Cj0117, futalosine hydrolase, methylthioadenosine nucleosidase, methylthioadenosine/S-adenosylhomocysteine nucleosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
adoHcy/MTA nucleosidase
-
-
methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
-
S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase
-
-
SYSTEMATIC NAME
IUBMB Comments
6-amino-6-deoxyfutalosine ribohydrolase
The enzyme, found in several bacterial species, catalyses a step in a modified futalosine pathway for menaquinone biosynthesis. While the enzyme from some organisms also has the activity of EC 3.2.2.9, adenosylhomocysteine nucleosidase, the enzyme from Chlamydia trachomatis is specific for 6-amino-6-deoxyfutalosine [7].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
-
-
-
-
?
deaminated S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
-
33% activity compared to 5'-methylthioadenosine
-
-
?
decarboxylated S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
-
18% activity compared to 5'-methylthioadenosine
-
-
?
S-2-aza-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
-
27% activity compared to 5'-methylthioadenosine
-
-
?
S-adenosyl-D-homocysteine + H2O
?
show the reaction diagram
-
26% activity compared to 5'-methylthioadenosine
-
-
?
additional information
?
-
-
no activity toward 5'-methylthioinosine, 5'-isobutylthioinosine, 5'-isobutylthio-3-deaza-adenosine, 5'-methylthio-3-deaza-adenosine, 5'-chloroformycin, 5'-methylthioformycin, 5'-ethylthiotubercidin, S-tubercidinylhomocysteine, S-inosyl-L-homocysteine, S-guanosyl-L-homocysteine, S-cytidylhomocysteine, S-8-aza adenosyl-L-homocysteine, S-n-methyl-3-deaza-adenosyl-L-homocysteine, S-n6-dimethyl-3-deaza-adenosyl-L-homocysteine, sinefungin, S-adenosyl-L-homocysteine dialdehyde, and acyclic adenosyl-L-homocysteine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-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-methylthiomethylpyrrolidine
-
-
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
-
-
5'-Chloroformycin
-
powerful inhibitor
5'-isobutylthio-3-deaza-adenosine
-
poor inhibitor
5'-Isobutylthioinosine
-
-
5'-methylthio-3-deaza-adenosine
-
poor inhibitor
5'-Methylthioformycin
-
powerful inhibitor
5'-methylthiotubercidin
-
powerful inhibitor
5'-n-butylthioinosine
-
-
adenine
-
poor inhibitor
S-8-aza-adenosyl-L-homocysteine
-
powerful inhibitor
S-adenosyl-L-homocysteine sulfoxide
-
poor inhibitor
S-formycinylhomocysteine
-
powerful inhibitor
S-N6-dimethyl-3-deaza-adenosyl-L-homocysteine
-
poor inhibitor
S-Tubercidinylhomocysteine
-
powerful inhibitor
sinefungin
-
poor inhibitor
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0000017
(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
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]3-hydroxy-4-methylthiomethylpyrrolidine
-
pH and temperature not specified in the publication
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
0.000322
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
0.0041
5'-methylthiotubercidin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.000928
S-8-aza-adenosyl-L-homocysteine
-
in 50 mM potassium phosphate buffer, 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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
5'-Chloroformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, 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
0.132
5'-Isobutylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, 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
0.00006
5'-Methylthioformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0077
5'-methylthiotubercidin
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
0.216
adenine
Escherichia coli
-
in 50 mM potassium phosphate buffer, 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
0.069
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
0.024
sinefungin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 3.2.2.9
Uniprot
Manually annotated by BRENDA team
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
the enzyme is rapidly inactivated after exposure for 15 min at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate buffer (pH 7.0), at least 2 months, no significant loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity column chromatography and gel filtration
ammonium sulfate precipitation, DEAE-Sephadex gel filtration, hydroxyapatite column chromatography, S-formycinylhomocysteine-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Escherichia coli (P0AF12)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team