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Information on EC 3.2.2.9 - adenosylhomocysteine nucleosidase and Organism(s) Staphylococcus aureus and UniProt Accession Q99TQ0

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.9 adenosylhomocysteine nucleosidase
IUBMB 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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Staphylococcus aureus
UNIPROT: Q99TQ0
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nucleosidase, pfs-2, mta/adohcy nucleosidase, s-adenosylhomocysteine nucleosidase, rv0091, 5'-methylthioadenosine/s-adenosylhomocysteine, mtan-1, 5'-methylthioadenosine nucleosidases, adenosylhomocysteine nucleosidase, adohcy/mesado nucleosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
MTAN
MTAN is a dual substrate-specific enzyme that irreversibly hydrolyzes the glycosidic bond of 5'-methylthioadenosine or S-adenosyl-L-homocysteine
5'-methyladenosine nucleosidase
-
-
-
-
adoHcy/MTA nucleosidase
-
-
-
-
methylthioadenosine nucleosidase
-
-
methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
-
MTA/SAH nucleosidase
S-adenosylhomocysteine nucleosidase
-
-
-
-
S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
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 hide
9055-10-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
5'-methylthioadenosine + H2O
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
-
-
-
-
?
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
5'-methylthioadenosine + H2O
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methylthio-DADMe-immucillin-A
-
i.e. (3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(methylsulfanyl)methyl]pyrrolidin-3-ol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00252
S-adenosyl-L-homocysteine
recombinant enzyme, in 50 mM potassium phosphate, pH 7.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00873
S-adenosyl-L-homocysteine
recombinant enzyme, in 50 mM potassium phosphate, pH 7.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme is essential for the virulence of Staphylococcus aureus and contributes to sepsis infection of mice. The enzyme is not essential for growth under nutrient-rich conditions, but is essential for autoinducer-2 production
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
biologically active dimer, X-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 hide
LITERATURE
E173Q
-
inactive
F104C/C186S
-
the mutations give an enzyme with steady-state kinetic properties similar to the native enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration
Ni-NTA 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) cells
-
expressed in Escherichia coli DH5alpha cells
-
REF.
AUTHORS
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Wang, S.; Thomas, K.; Schramm, V.L.
Catalytic site cooperativity in dimeric methylthioadenosine nucleosidase
Biochemistry
53
1527-1535
2014
Staphylococcus aureus
Manually annotated by BRENDA team
Bao, Y.; Li, Y.; Jiang, Q.; Zhao, L.; Xue, T.; Hu, B.; Sun, B.
Methylthioadenosine/S-adenosylhomocysteine nucleosidase (Pfs) of Staphylococcus aureus is essential for the virulence independent of LuxS/AI-2 system
Int. J. Med. Microbiol.
303
190-200
2013
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
Manually annotated by BRENDA team