Any feedback?
Information on EC 2.4.2.28 - S-methyl-5'-thioadenosine phosphorylase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97W94
for references in articles please use BRENDA:EC2.4.2.28Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.2.28 S-methyl-5'-thioadenosine phosphorylaseIUBMB Comments
Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
Specify your search results
Word Map
- 2.4.2.28
- purine
- polyamine
-
salvage
-
mtap-deficient
-
cdkn2a
- mesothelioma
-
phosphorolysis
-
mesothelial
- nucleosidase
-
codeleted
-
l-alanosine
-
co-deletion
-
mtap-deleted
-
phosphorylase-deficient
- p15ink4b
- 5'-deoxyadenosine
- 5-methylthioribose
-
mtans
-
p14arf
-
enzyme-deficient
- diagnostics
- drug development
- medicine
- analysis
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
methylthioadenosine phosphorylase, 5'-methylthioadenosine phosphorylase, mta phosphorylase, mtap protein, 5'-deoxy-5'-methylthioadenosine phosphorylase, ssmtapii, ssmtap, mtapase, mesado phosphorylase, pfmtap, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-deoxy-5'-methylthioadenosine phosphorylase II
-
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
-
-
-
-
5'-deoxy-5'-methylthioadenosine phosphorylase
-
-
-
-
5'-methylthioadenosine phosphorylase
-
-
-
-
MTA phosphorylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
sequential mechanism
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
catalytic mechanism
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
active and substrate-binding sites, three-dimensional structures
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
subunit structure, model
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
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
61970-06-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
substrate-induced conformational change involving Glu163, which is located at the interface between subunits and swings in toward the active site upon nucleoside binding
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
the transition state is stabilized in different ways for 6-amino versus 6-oxo substrates
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
binding of phosphate and 5-methylthioribose 1-phosphate to the enzyme induces a conformational transition that stabilizes the folded structure of the enzyme
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
5'-methylthioadenosine and adenine form ternary complexes with the enzyme only in presence of phosphate and methylthioribose 1-phosphate, respectively
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
?
guanosine + phosphate
guanine + D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
most effective substrate
-
-
?
additional information
?
-
-
no activity with S-adenosyl-L-methionine
-
-
?
additional information
?
-
no activity with S-adenosyl-L-methionine
-
-
?
additional information
?
-
-
no activity with S-adenosylhomocysteine
-
-
?
additional information
?
-
no activity with S-adenosylhomocysteine
-
-
?
additional information
?
-
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
additional information
?
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
?
guanosine + phosphate
guanine + D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
-
-
-
?
additional information
?
-
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
additional information
?
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
proteinase K
-
recombinant enzyme, 10% remaining activity after 4 h at 37°C, phosphate protects
-
Subtilisin
-
recombinant enzyme, 24% remaining activity after 4 h at 37°C, phosphate protects
-
iodoacetate
incorporation of 12 mol iodoactate per mol of enzyme
additional information
-
no inhibition by S-adenosyl-L-methionine
-
additional information
no inhibition by S-adenosyl-L-methionine
-
additional information
-
activity is not affected by alkylating, mercaptide-forming and oxidizing thiol reagents
-
additional information
activity is not affected by alkylating, mercaptide-forming and oxidizing thiol reagents
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.024
5'-methylthioadenosine
wild-type and recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.86
70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S
5.28
70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S/C164S
6.24
70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S
2.12
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
114
mutant enzyme C259S/C261S/C262S/C200S/C205S and mutant enzyme C259S/C261S/C262S
120
70
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 120
60°C: about 40% of maximal activity, 120°C: about 40% of maximal activity, recombinant enzyme
90 - 130
90°C: about 50% of maximal activity, 130°C: about 70% of maximal activity
95 - 140
-
95°C: about 50% of maximal activity, 140°C: about 45% of maximal activity, wild-type enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
isoelectric focusing on polyacrylamide gel in the pH ranges 3-10 and 4.5-6.0
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
27000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
hexamer
additional information
hexamer
dimer-of-trimers with one active site per monomer, crystallization data
hexamer
SsMTAP II is a hexamer formed from trimers packed face to face
hexamer
-
6 * 27000, recombinant enzyme, crystal structure analysis
additional information
-
enzyme is formed by a trimer of dimers with three symmetric intersubunit disulfide bonds linking the dimers to one another, each monomer contains one active site, which is located near a dimer interface
additional information
enzyme is formed by a trimer of dimers with three symmetric intersubunit disulfide bonds linking the dimers to one another, each monomer contains one active site, which is located near a dimer interface
additional information
-
secondary structure by circular dichroism spectra
additional information
secondary structure by circular dichroism spectra
additional information
-
presence of 6 disulfide bonds, organisation in 2 trimers
additional information
presence of 6 disulfide bonds, organisation in 2 trimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal packing. Space group is C2, unit-cell parameters are a = 135.16, b = 138.09, c = 96.56 A, beta = 92.21°. The asymmetric unit contains two independent half-hexamers, the other half of each of which is generated by a crystallographic twofold axis
hanging-drop, vapor-diffusion method at 22°C, the crystal structure of the enzyme in complex with 5'-deoxy-5'-methylthioadenosine and sulfate is determined to 1.45 A resolution
the structure of SsMTAP II is originally determined in space group P1 and shows R32 pseudosymmetry. Post-analysis using phenix.xtriage shows that the correct space group is C2. The structure refined in space group C2 is reported and the factors that initially led to the incorrect space-group assignment are discussed
crystals are grown at either room temperature or 18°C using the hanging drop vapor diffusion technique. Determination of the structure of 5'-deoxy-5'-methylthioadenosine phosphorylase alone, as ternary complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog formycin B and as binary complexes with phosphate or sulfate alone. The structure of unliganded SsMTAP is refined at 2.5 A resolution and the structures of the complexes are refined at resolutions ranging from 1.6 A to 2.0 A
from recombinant enzyme, hanging drop-vapour diffusion method, protein solution, 7-10 mg/ml, 18°C, reservoir solution for native crystals: Tris-HCl 10 mM, pH 7.4, 28-30% dioxane, 12% 2-methyl-2,4-pentanediol, 0.12 M MgCl2, 0,04 M NaCl, for crystals of enzyme complexed with substrates or sulfate and phosphate ions, substrates are added and NaCl is exchanged for MgSO4 or NH4Cl and KH2PO4, respectively, X-ray structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C259S/C261S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 102°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S/C262S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 91°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S/C262S/C200S/C205S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S/C262S/C200S/C205S/C138S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 78°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S/C262S/C200S/C205S/C138S/C164S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme
C262S
mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 106°C. Specific activity is similar to the activity of the wild-type enzyme
C259S/C261S
C262S
C259S/C261S
-
mutant enzyme shows thermophilic and thermostable features significantly lower than those of the wild-type enzyme
C259S/C261S
-
in contrast wo wild-type C262S and C259S/C261S mutants show complete thermal denaturation curves with sigmoidal transitions centered at 102°C and 99°C respectively. Under reducing conditions these values decrease by 4°C and 8°C respectively, highlighting the important role exerted by the CXC disulfide on enzyme thermostability. The double mutant (the mutant lacking the structural CXC motif), has more impact on the thermostability of SsMTAPII than the single mutant
C262S
-
mutant enzyme shows thermophilic and thermostable features significantly lower than those of the wild-type enzyme
C262S
-
in contrast wo wild-type C262S and C259S/C261S mutants show complete thermal denaturation curves with sigmoidal transitions centered at 102°C and 99°C respectively. Under reducing conditions these values decrease by 4°C and 8°C respectively, highlighting the important role exerted by the CXC disulfide on enzyme thermostability
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102
5 min, 50% residual activity, mutant enzyme C259S/C261S
73
5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S/C200S/C205S and mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S/C164S
78
5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S
91
5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S
100
110
111
118
recombinant enzyme in presence of 100 mM phosphate, melting temperature
120
130
132
140
90
additional information
100
-
recombinant enzyme, 1 h, 95% remainig activity in presence of 100 mM phosphate
100
1 h, 15% loss of activity of recombinant enzyme, wild-type enzyme remains stable
110
-
recombinant enzyme, 10 min, 50% remaining activity in absence and 90% remaining activity in presence of 100 mM phosphate
120
-
recombinant enzyme, 10 min, no activity in absence and 50% remaining activity in presence of 100 mM phosphate
90
recombinant enzyme, 0.8 M DTT, 2 h, loss of 38% activity
90
-
1 h, wild-type enzyme is completely stable, mutant enzyme C262S loses 32% of its activity, mutant enzyme c259S/C261A loses 63% of its activity
additional information
the hexameric hyperthermophilic protein contains in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. All cysteine pairs and especially the CXC motif significantly contribute to the enzyme thermal stability
additional information
-
the hexameric hyperthermophilic protein contains in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. All cysteine pairs and especially the CXC motif significantly contribute to the enzyme thermal stability
additional information
-
disulfide linkages play a key role in thermal stability
additional information
disulfide linkages play a key role in thermal stability
additional information
-
the recombinant enzyme, expressed in Escherichia coli, is less thermostable and thermophilic than the native enzyme due to incorrect positioning of disulfide bonds
additional information
the recombinant enzyme, expressed in Escherichia coli, is less thermostable and thermophilic than the native enzyme due to incorrect positioning of disulfide bonds
additional information
-
the recombinant 5'-methylthioadenosine phosphorylase is less thermophilic and thermostable than the Sulfolobus solfataricus enzyme, since an incorrect positioning of disulfide bonds within the molecule generates structures less stable to thermal unfolding
additional information
the recombinant 5'-methylthioadenosine phosphorylase is less thermophilic and thermostable than the Sulfolobus solfataricus enzyme, since an incorrect positioning of disulfide bonds within the molecule generates structures less stable to thermal unfolding
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
elimination of the disulfide bond Cys138Cys205 leads to an increased protease susceptibility
after 40 min exposure to 10.4 GHz microwave radiation at 90°C the enzyme retains 78% activity compared to a control incubated at the same temperature without irradiation. KCl or NaCl increases the susceptibility to microwave irradiation. Protection against microwave inactivation by phosphate or sulfate.
-
no loss of activity after 24 h at room temperature in presence of 9 M urea, 4 M guanidine hydrochloride, 0.075% SDS, 50% methanol, 50% ethanol, 50% dimethylformamide, 1 M NaCl, and 1% Triton X-100
no loss of activity after treatment with thermolysin, trypsin, and chymotrypsin for 24 h at 37°C
phosphate, and less efficiently also arsenate and sulfate, stabilize the recombinant enzyme against inactiviation by temperature, SDS, urea, and proteolytic enzymes
-
recombinant enzyme, 90°C in 2% SDS, 30 min, loss of 60% activity
-
recombinant enzyme, 90°C in 8 M urea, 30 min, loss of 70% activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1-propanol
no loss of activity after 24 h at room temperature in presence of 50% methanol, loss of 90% activity at 90°C after 1 h
dimethylformamide
no loss of activity after 24 h at room temperature in presence of 50% dimethylformamide, loss of 21% activity at 90°C after 1 h
Ethanol
guanidine-HCl
4 M, 24 h at room temperature, no loss of activity
Methanol
N,N-dimethylformamide
50%, 24 h at room temperature, no loss of activity
SDS
0.075%, 24 h at room temperature, no loss of activity. After 60 min of incubation in 2% SDS the enzyme remains fully active at 70°C and retains 20% residual activity at 90°C. Complete inactivation after 5 min at 100°C in 0.5% SDS
tetrahydrofuran
loss of 76% activity at 70°C after 30 min, complete loss of activity after 1 h at 70°C
Triton X-100
9 M, 24 h at room temperature, no loss of activity
Ethanol
no loss of activity after 24 h at room temperature in presence of 50% ethanol, loss of 88% activity at 90°C after 1 h
Methanol
no loss of activity after 24 h at room temperature in presence of 50% methanol, loss of 80% activity at 90°C after 1 h
Methanol
50%, 24 h at room temperature, no loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM Tris-HC1, pH 7.4, containing 1 mM EDTA, stable for at least 1 year
-20°C, purified enzyme, Tris-HCl 10 mM, pH 7.4, 1 mM EDTA, stable at least 1 year
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli strain RB791, amino acid determination, incorrect positioning of disulfide bonds, the recombinant enzyme is less thermostable and thermophilic than the native enzyme
recombinant SsMTAPII and its C262S and C259S/C261S mutant forms are expressed in Escherichia coli BL21 (lDE3) cells
-
overexpression in Escherichia coli strain RB791, amino acid determination, incorrect positioning of disulfide bonds, the recombinant enzyme is less thermostable and thermophilic than the native enzyme
overexpression in Escherichia coli strain RB791, amino acid determination, incorrect positioning of disulfide bonds, the recombinant enzyme is less thermostable and thermophilic than the native enzyme
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cacciapuoti, G.; Porcelli, M.; Bertoldo, C.; Zappia, V.
Thermophilicity and thermostability of 5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus
Life Chem. Rep.
10
75-81
1992
Saccharolobus solfataricus
-
Cacciapuoti, G.; Porcelli, M.; Bertoldo, C.; De Rosa, M.; Zappia, V.
Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds
J. Biol. Chem.
269
24762-24769
1994
Saccharolobus solfataricus, Saccharolobus solfataricus (P50389)
Cacciapuoti, G.; Fusco, S.; Caiazzo, N.; Zappia, V.; Porcelli, M.
Heterologous expression of 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus: characterization of the recombinant protein and involvement of disulfide bonds in thermophilicity and thermostability
Protein Expr. Purif.
16
125-135
1999
Saccharolobus solfataricus, Saccharolobus solfataricus (P50389)
Cacciapuoti, G.; Servillo, L.; Moretti, M.A.; Porcelli, M.
Conformational changes and stabilization induced by phosphate binding to 5'-methylthioadenosine phosphorylase from the thermophilic archaeon Sulfolobus solfataricus
Extremophiles
5
295-302
2001
Saccharolobus solfataricus
Appleby, T.C.; Mathews, I.I.; Porcelli, M.; Cacciapuoti, G.; Ealick, S.E.
Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus
J. Biol. Chem.
276
39232-39242
2001
Saccharolobus solfataricus, Saccharolobus solfataricus (P50389)
Cacciapuoti, G.; Forte, S.; Moretti, M.A.; Brio, A.; Zappia, V.; Porcelli, M.
A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus
FEBS J.
272
1886-1899
2005
Saccharolobus solfataricus
Cacciapuoti, G.; Porcelli, M.; Bertoldo, C.; Fusco, S.; De Rosa, M.; Zappia, V.
Extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Gene cloning and amino acid sequence determination.
Eur. J. Biochem.
239
632-637
1996
Saccharolobus solfataricus (P50389), Saccharolobus solfataricus
Zhang, Y.; Porcelli, M.; Cacciapuoti, G.; Ealick, S.E.
The crystal structure of 5-deoxy-5-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds
J. Mol. Biol.
357
252-262
2006
Saccharolobus solfataricus (Q97W94), Saccharolobus solfataricus
Zhang, Y.; Zwart, P.H.; Ealick, S.E.
A corrected space group for Sulfolobus sulfataricus 5'-deoxy-5'-methylthioadenosine phosphorylase II
Acta Crystallogr. Sect. D
68
249-252
2012
Saccharolobus solfataricus (Q97W94), Saccharolobus solfataricus P2 (Q97W94)
Cacciapuoti, G.; Fuccio, F.; Petraccone, L.; Del Vecchio, P.; Porcelli, M.
Role of disulfide bonds in conformational stability and folding of 5-deoxy-5-methylthioadenosine phosphorylase II from the hyperthermophilic archaeon Sulfolobus solfataricus
Biochim. Biophys. Acta
1824
1136-1143
2012
Saccharolobus solfataricus
Porcelli, M.; Cacciapuoti, G.; Fusco, S.; Massa, R.; d'Ambrosio, G.; Bertoldo, C.; De Rosa, M.; Zappia, V.
Non-thermal effects of microwaves on proteins: thermophilic enzymes as model system
FEBS Lett.
402
102-106
1997
Saccharolobus solfataricus
Bagarolo, M.L.; Porcelli, M.; Martino, E.; Feller, G.; Cacciapuoti, G.
Multiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase
Biochim. Biophys. Acta
1854
1458-1465
2015
Saccharolobus solfataricus (Q97W94), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97W94)
EXTERNAL LINKS (specific for EC-Number 2.4.2.28)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
