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Information on EC 3.2.2.16 - methylthioadenosine nucleosidase and Organism(s) Streptococcus pneumoniae and UniProt Accession Q8DQ16

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.16 methylthioadenosine nucleosidase
IUBMB Comments
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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This record set is specific for:
Streptococcus pneumoniae
UNIPROT: Q8DQ16
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The taxonomic range for the selected organisms is: Streptococcus pneumoniae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-methylthioadenosine nucleosidase
-
-
-
-
MeSAdo nucleosidase
-
-
-
-
MTA nucleosidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
50812-28-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
show the reaction diagram
-
-
-
?
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
ethylthio-immucillin-A
-
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
methylthio-immucillin-A
weak
p-tolylthio-immucillin-A
-
phenylthio-immucillin-A
-
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine
-
transition state analogue inhibitor, comparison with inhibition of Escherichia coli enzyme and several methylthioadenosine phosphorylases
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine-3-methanol
-
transition state analogue inhibitor, comparison with inhibition of Escherichia coli enzyme and several methylthioadenosine phosphorylases
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
analysis of Kd value, comparison with inhibition of Neisseria meningitides, Helicobacter pylori, Staphylococcus aureus, Escherichia coli and human enzyme
benzylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
analysis of Kd value, comparison with inhibition of Neisseria meningitides, Helicobacter pylori, Staphylococcus aureus, Escherichia coli and human enzyme
ethylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
analysis of Kd value, comparison with inhibition of Neisseria meningitides, Helicobacter pylori, Staphylococcus aureus, Escherichia coli and human enzyme
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
5'-methylthioadenosine
pH 7.5, 25°C
0.013
S-adenosyl-L-homocysteine
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
5'-methylthioadenosine
pH 7.5, 25°C
0.37
S-adenosyl-L-homocysteine
pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000036
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
pH 7.5, 25°C
0.00004
ethylthio-immucillin-A
pH 7.5, 25°C
0.000024
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
pH 7.5, 25°C
0.001
methylthio-immucillin-A
pH 7.5, 25°C
0.00006
p-tolylthio-immucillin-A
pH 7.5, 25°C
0.000335
phenylthio-immucillin-A
pH 7.5, 25°C
0.000084
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine
-
-
0.00015
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine-3-methanol
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Uniprot
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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 (Q8DQ16)
Manually annotated by BRENDA team
Singh, V.; Schramm, V.L.
Transition-state analysis of S. pneumoniae 5-methylthioadenosine nucleosidase
J. Am. Chem. Soc.
129
2783-2795
2007
Streptococcus pneumoniae
Manually annotated by BRENDA team
Evans, G.B.; Furneaux, R.H.; Greatrex, B.; Murkin, A.S.; Schramm, V.L.; Tyler, P.C.
Azetidine based transition state analogue inhibitors of N-ribosyl hydrolases and phosphorylases
J. Med. Chem.
51
948-956
2008
Escherichia coli, Streptococcus pneumoniae
Manually annotated by BRENDA team
Luo, M.; Schramm, V.L.
Ribosyl geometry in the transition state of Streptococcus pneumoniae methylthioadenosine nucleosidase from the 3'-2H kinetic isotope effect
J. Am. Chem. Soc.
130
11617-11619
2008
Streptococcus pneumoniae
Manually annotated by BRENDA team