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Information on EC 2.4.2.28 - S-methyl-5'-thioadenosine phosphorylase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U4Q8

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.28 S-methyl-5'-thioadenosine phosphorylase
IUBMB Comments
Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
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Select one or more organisms in this record: ?
This record set is specific for:
Pyrococcus furiosus
UNIPROT: Q8U4Q8
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
methylthioadenosine phosphorylase, 5'-methylthioadenosine phosphorylase, mta phosphorylase, mtap protein, 5'-deoxy-5'-methylthioadenosine phosphorylase, ssmtapii, ssmtap, mtapase, mesado phosphorylase, pfmtap, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-deoxy-5'-methylthioadenosine phosphorylase
-
5'-deoxy-5'-methylthioadenosine phosphorylase
-
-
-
-
5'-methylthioadenosine nucleosidase
-
-
-
-
5'-methylthioadenosine phosphorylase
-
-
-
-
MeSAdo phosphorylase
-
-
-
-
MeSAdo/Ado phosphorylase
-
-
-
-
methylthioadenosine nucleoside phosphorylase
-
-
-
-
methylthioadenosine phosphorylase
MTA phosphorylase
-
-
-
-
MTAPase
-
-
-
-
phosphorylase, methylthioadenosine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
S-methyl-5'-thioadenosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase
Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
CAS REGISTRY NUMBER
COMMENTARY hide
61970-06-7
-
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 + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
guanosine + phosphate
guanine + D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
0.8 M, reduction of thermostability
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.147
5'-methylthioadenosine
-
-
0.109
adenosine
-
-
0.916
guanosine
-
-
0.963
Inosine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.5
5'-methylthioadenosine
-
-
22.8
adenosine
-
-
7.31
guanosine
-
-
9.38
Inosine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.35
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86 - 95
-
2 different activation energy-dependent processes occur below and above 100°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
-
gel filtration
30000
-
6 * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 30000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
5 h, 98% remaining activity
130
-
half-life: 43 min
137
-
melting temperature
139
-
melting temperature in presence of 100 mM phosphate
140
-
half-life: 13 min
145
-
half-life: 5 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol 0.8 M, reduction of thermostability
-
enzyme is extremely stable to proteolytic cleavage
-
transition midpoint for guanidinium chloride-induced unfolding is 3.0 M after 22 h incubation. The value decreases to 2.0 M in presence of 30 mM dithiothreitol. The guanidinium chloride-induced unfolding is completely reversible
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-propanol
-
at 50%: 88% remaining activity after 60 min at 50°C, 58% remaining activity after 60 min at 70°C, 22% remaining activity after 60 min at 90°C
acetonitrile
-
at 50%: stable at 90°C for 30 min, loss of 62% activity after 60 min
dimethylformamide
-
at 50%: 48% remaining activity after 60 min at 50°C, 5% remaining activity after 60 min at 70°C, no activity at 90°C
Ethanol
-
at 50%: 90% remaining activity after 60 min at 50°C, 65% remaining activity after 60 min at 70°C, 30% remaining activity after 60 min at 90°C
Methanol
-
at 50%: stable at 90°C for 30 min, loss of 77% activity after 60 min
tetrahydrofuran
-
at 50%: 77% remaining activity after 60 min at 50°C, 50% remaining activity after 60 min at 70°C, 3% remaining activity after 60 min at 90°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, Tris-HCl 10 mM, pH 7.4, purified enzyme, stable for at least 1 year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
guanidinium chloride-induced unfolding is completely reversible
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cacciapuoti, G.; Bertoldo, C.; Brio, A.; Zappia, V.; Porcelli, M.
Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus. Substrate specificity and primary structure analysis
Extremophiles
7
159-168
2003
Pyrococcus furiosus
Manually annotated by BRENDA team
Cacciapuoti, G.; Moretti, M.A.; Forte, S.; Brio, A.; Camardella, L.; Zappia, V.; Porcelli, M.
Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds
Eur. J. Biochem.
271
4834-4844
2004
Pyrococcus furiosus
Manually annotated by BRENDA team
Cacciapuoti, G.; Marabotti, A.; Fuccio, F.; Porcelli, M.
Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5-deoxy-5-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus
Biochim. Biophys. Acta
1814
1358-1366
2011
Pyrococcus furiosus (Q8U4Q8), Pyrococcus furiosus
Manually annotated by BRENDA team