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Information on EC 3.2.2.9 - adenosylhomocysteine nucleosidase and Organism(s) Helicobacter pylori and UniProt Accession Q9ZMY2
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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: Helicobacter pylori
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, adenosylhomocysteine nucleosidase, adohcy/mesado nucleosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-methyladenosine nucleosidase
-
-
-
-
adoHcy/MTA nucleosidase
-
-
-
-
MTA/SAH nucleosidase
-
-
-
-
S-adenosylhomocysteine nucleosidase
-
-
-
-
S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase
-
-
-
-
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
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
-
-
-
ir
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
-
-
-
-
?
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
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
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(ethynylsulfanyl)methyl]pyrrolidin-3-ol
transition-state analogue, shows significant overlap in specificity with human 5'-methylthioadenosine phosphorylase MTAP
(4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[[(pent-4-yn-1-yl)sulfanyl]methyl]pyrrolidin-3-ol
transition-state analogue, best binding inhibitor tested, shows significant overlap in specificity with human 5'-methylthioadenosine phosphorylase MTAP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0449
5'-methylthioadenosine
at 37°C in 100 mM HEPES, 50 mM KCl, pH 7.5
0.01
S-adenosyl-L-homocysteine
-
wild type enzyme, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
0.014
S-adenosyl-L-homocysteine
-
mutant enzyme H109A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
0.019
S-adenosyl-L-homocysteine
-
mutant enzyme F107A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.92
5'-methylthioadenosine
at 37°C in 100 mM HEPES, 50 mM KCl, pH 7.5
0.44
S-adenosyl-L-homocysteine
-
mutant enzyme F107A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
0.74
S-adenosyl-L-homocysteine
-
mutant enzyme H109A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
1.8
S-adenosyl-L-homocysteine
-
wild type enzyme, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
S-adenosyl-L-homocysteine
-
mutant enzyme F107A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
51
S-adenosyl-L-homocysteine
-
mutant enzyme H109A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
170
S-adenosyl-L-homocysteine
-
wild type enzyme, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme alone, in complex with formycin A and in complex with adenine, hanging drop vapor diffusion method, using 0.1 M Tris pH 8.5 and 16% (w/v) polyethyleneglycol 8000, at 18°C
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 S-adenosyl-L-homocysteine and active enzyme bound to S-(5-deoxy-D-ribos-5-yl)-L-homocysteine and adenine using 0.05 M magnesium chloride hexahydrate, 0.1 M HEPES (pH 7.5), and 30% (v/v) PEG-MME 550
-
structure in complex with transition state analogue inhibitors
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Helicobacter pylori (Q9ZMY2)
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
Harijan, R.K.; Hoff, O.; Ducati, R.G.; Firestone, R.S.; Hirsch, B.M.; Evans, G.B.; Schramm, V.L.; Tyler, P.C.
Selective inhibitors of Helicobacter pylori methylthioadenosine nucleosidase and human methylthioadenosine phosphorylase
J. Med. Chem.
62
3286-3296
2019
Helicobacter pylori (A0A1W0VQJ9), Helicobacter pylori
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Release 2023.1 (January 2023)
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