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

for references in articles please use BRENDA:EC3.2.2.9
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This record set is specific for:
Staphylococcus aureus
UNIPROT: Q99TQ0


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota


The taxonomic range for the selected organisms is: Staphylococcus aureus

EC NUMBER
COMMENTARY hide
3.2.2.9
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RECOMMENDED NAME
GeneOntology No.
adenosylhomocysteine nucleosidase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
autoinducer AI-2 biosynthesis I
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autoinducer AI-2 biosynthesis II (Vibrio)
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L-cysteine biosynthesis VI (from L-methionine)
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S-adenosyl-L-methionine cycle I
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methionine metabolism
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Cysteine and methionine metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-homocysteine homocysteinylribohydrolase
Also acts on S-methyl-5'-thioadenosine to give adenine and S-methyl-5-thioribose (cf. EC 3.2.2.16, methylthioadenosine nucleosidase).
CAS REGISTRY NUMBER
COMMENTARY hide
9055-10-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
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
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-
-
?
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
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-
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?
5'-methylthioadenosine + H2O
?
show the reaction diagram
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-
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S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
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S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
show the reaction diagram
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-
-
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?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
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-
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
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S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methylthio-DADMe-immucillin-A
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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
SUBUNITS
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
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli DH5alpha cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E173Q
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inactive
F104C/C186S
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the mutations give an enzyme with steady-state kinetic properties similar to the native enzyme