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Information on EC 3.2.2.30 - aminodeoxyfutalosine nucleosidase and Organism(s) Helicobacter pylori and UniProt Accession O24915

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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:
Helicobacter pylori
UNIPROT: O24915
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The taxonomic range for the selected organisms is: Helicobacter pylori
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
methylthioadenosine nucleosidase
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
6-amino-6-deoxyfutalosine hydrolase
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futalosine hydrolase
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-
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
adenine + dehypoxanthinyl futalosine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
additional information
?
-
-
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is a multifunctional enzyme that catalyzes the hydrolysis of the N-ribosidic bond of at least four different adenosine-based metabolites: S-adenosyl-L-homocysteine, 5'-methylthioadenosine, 5'-deoxyadenosine, and 6-amino-6-deoxyfutalosine
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-
?
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
adenine + dehypoxanthinyl futalosine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
additional information
?
-
-
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is a multifunctional enzyme that catalyzes the hydrolysis of the N-ribosidic bond of at least four different adenosine-based metabolites: S-adenosyl-L-homocysteine, 5'-methylthioadenosine, 5'-deoxyadenosine, and 6-amino-6-deoxyfutalosine
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tris
weak inhibitor, about 20% residual activity at 250 mM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
homodimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, mutants E14Q (0.1 M HEPES pH 7.5, 25% (w/v) PEG 3350, 0.2 M NaCl), D199N (0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M MgCl2-6H2O) and D199A (0.1 M bis-tris pH 6.5, 25% (w/v) PEG 3350, 0.2 M Li2SO4-H2O)
wild type and mutant enzymes E14Q, D199N, and D199A, sitting drop vapor diffusion method, using 4.0 M NaH2PO4/K2HPO4 pH 7.0 (wild type), 0.1 M HEPES pH 7.5, 25% PEG 3350, 0.2 M NaCl (E14Q), 0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M MgCl2-6H2O (D199N), and 0.1 M bis-Tris pH 6.5, 25% (w/v) PEG 3350, 0.2 M Li2SO4-H2O (D199A)
enzyme only or in complex with formycin A or adenine, hanging drop vapor diffusion method, using 0.1 M Tris pH 8.5 and 16% (w/v) polyethyleneglycol 8000, at 18°C
hanging drop vapor diffusion method. Inactive D198N mutant bound to 5'-methylthioadenosine using 0.2 M magnesium chloride, 0.1 M HEPES (pH 7.5), and 25% (w/v) PEG 3350
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structures of wild-type cocrystallized with S-adenosylhomocysteine, formycin A, and (3R,4S)-4-(4-chlorophenylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine as well as one structure of inactive variant D198N cocrystallized with S-adenosylhomocysteine. Mechanism of D198 pKa elevation is through the sharing of a proton with atom N7 of the adenine moiety possessing unconventional hydrogen-bond geometry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D199A
D199N
D198N
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
HisTrap column chromatography and Superdex 75 gel filtration
HisTrap column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Rosetta cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arakawa, C.; Kuratsu, M.; Furihata, K.; Hiratsuka, T.; Itoh, N.; Seto, H.; Dairi, T.
Diversity of the early step of the futalosine pathway
Antimicrob. Agents Chemother.
55
913-916
2011
Helicobacter pylori
Manually annotated by BRENDA team
Ronning, D.R.; Iacopelli, N.M.; Mishra, V.
Enzyme-ligand interactions that drive active site rearrangements in the Helicobacter pylori 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Protein Sci.
19
2498-2510
2010
Helicobacter pylori (Q9ZMY2)
Manually annotated by BRENDA team
Kim, R.Q.; Offen, W.A.; Davies, G.J.; Stubbs, K.A.
Structural enzymology of Helicobacter pylori methylthioadenosine nucleosidase in the futalosine pathway
Acta Crystallogr. Sect. D
70
177-185
2014
Helicobacter pylori (O24915)
Manually annotated by BRENDA team
Mishra, V.; Ronning, D.R.
Crystal structures of the Helicobacter pylori MTAN enzyme reveal specific interactions between S-adenosylhomocysteine and the 5-alkylthio binding subsite
Biochemistry
51
9763-9772
2012
Helicobacter pylori
Manually annotated by BRENDA team
Evans, G.B.; Tyler, P.C.; Schramm, V.L.
Immucillins in infectious diseases
ACS Infect. Dis.
4
107-117
2018
Helicobacter pylori
Manually annotated by BRENDA team
Banco, M.T.; Mishra, V.; Ostermann, A.; Schrader, T.E.; Evans, G.B.; Kovalevsky, A.; Ronning, D.R.
Neutron structures of the Helicobacter pylori 5-methylthioadenosine nucleosidase highlight proton sharing and protonation states
Proc. Natl. Acad. Sci. USA
113
13756-13761
2016
Helicobacter pylori (Q9ZMY2)
Manually annotated by BRENDA team