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Information on EC 3.2.2.9 - adenosylhomocysteine nucleosidase and Organism(s) Campylobacter jejuni and UniProt Accession Q0PC20

for references in articles please use BRENDA:EC3.2.2.9
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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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This record set is specific for:
Campylobacter jejuni
UNIPROT: Q0PC20
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The taxonomic range for the selected organisms is: Campylobacter jejuni
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nucleosidase, pfs-2, mta/adohcy nucleosidase, rv0091, s-adenosylhomocysteine nucleosidase, 5'-methylthioadenosine/s-adenosylhomocysteine, mtan-1, 5'-methylthioadenosine nucleosidases, 5'-deoxyadenosine/5'-methylthioadenosine nucleosidase, adenosylhomocysteine nucleosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-methylthioadenosine nucleosidase
-
5'-methyladenosine nucleosidase
-
-
-
-
adoHcy/MTA 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
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
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
5-methylthio-D-ribose + adenine
show the reaction diagram
-
-
-
?
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00093
5'-methylthioadenosine
in 50 mM potassium phosphate buffer, pH 7.0, at 25°C
0.00103
6-amino-6-deoxyfutalosine
in 50 mM potassium phosphate buffer, pH 7.0, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.7
5'-methylthioadenosine
in 50 mM potassium phosphate buffer, pH 7.0, at 25°C
0.53
6-amino-6-deoxyfutalosine
in 50 mM potassium phosphate buffer, pH 7.0, at 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme plays key roles in S-adenosylmethionine recycling, the biosynthesis of autoinducer molecules, and the biosynthesis of menaquinone
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, X.; Apel, D.; Gaynor, E.C.; Tanner, M.E.
5'-methylthioadenosine nucleosidase is implicated in playing a key role in a modified futalosine pathway for menaquinone biosynthesis in Campylobacter jejuni
J. Biol. Chem.
286
19392-19398
2011
Campylobacter jejuni (Q0PC20), Campylobacter jejuni, Campylobacter jejuni NCTC 11168 (Q0PC20)
Manually annotated by BRENDA team