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Information on EC 3.1.5.B1 - dNTPase and Organism(s) Mus musculus and UniProt Accession Q60710

for references in articles please use BRENDA:EC3.1.5.B1
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.5 Triphosphoric-monoester hydrolases
                3.1.5.B1 dNTPase
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Mus musculus
UNIPROT: Q60710 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
samhd1, dntpase, deoxynucleoside triphosphate triphosphohydrolase, hd domain protein, dntp triphosphorylase, deoxyribonucleotide triphosphohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxyribonucleotide triphosphohydrolase
-
SYSTEMATIC NAME
IUBMB Comments
dNTP triphosphorylase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dATP + H2O
deoxyadenosine + triphosphate
show the reaction diagram
-
-
-
?
dCTP + H2O
deoxycytidine + triphosphate
show the reaction diagram
-
-
-
?
dGTP + H2O
deoxyguanosine + triphosphate
show the reaction diagram
-
-
-
?
dTTP + H2O
deoxythymidine + triphosphate
show the reaction diagram
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GTP
low concentrations of either GTP or dGTP stimulate the reaction maximally, Km value for binding to allosteric site 1 is 0.0005 mM with substrate dATP. In quiescent cells where the enzyme is maximally expressed GTP binds to allosteric site 1 with very high affinity, stabilizing site 2 of the tetrameric structure. Any canonical dNTP can bind to site 2 and activate the enzyme, but in cells only dATP or dTTP are present at sufficient concentrations. Tetrameric enzyme is activated for the hydrolysis of any dNTP only after binding of a dNTP to site 2
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
dATP
pH 7.5, 37°C, presence of 0.02 mM GTP
0.2
dCTP
pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP
0.22
dGTP
pH 7.5, 37°C
0.28
dTTP
pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.4
dATP
pH 7.5, 37°C, presence of 0.02 mM GTP
2.2
dCTP
pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP
2.9
dGTP
pH 7.5, 37°C
4.1
dTTP
pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in the mouse, SAMHD1 is expressed as isoforms ISF1 and ISF2 that differ at the carboxyl terminus due to alternative splicing of the last coding exon. Both isoforms are antiviral in nondividing cells. Phosphomimetic mutation at Thr-634 of ISF1 ablates its antiviral activity but has little effect on phosphohydrolase activity in vitro. dGTP causes ISF1 to tetramerize, activating its catalytic activity. Isoform ISF2 lacks the phosphorylation site, is significantly more active, tetramerizes, and is active without added dGTP. Mouse SAMHD1 does not degrade HIV-1 genomic viral RNA
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SAMH1_MOUSE
658
0
75893
Swiss-Prot
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
isoform ISF1 is phosphorylated at amino acids Ser49, Thr52, Ser55, Thr56, Thr310, and Thr634 with frequencies ranging from 21% to 56%
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P635A
mutation retains antiviral activity of ISF1, and increased its catalytic activity to that of ISF2
T634A
mutation retains antiviral activity of ISF1
T634E
mutation in ISF1, mimics phosphorylated SAMHD1. Mutant is inactive
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in 293T cell
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
maximum expression in quiescent cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miazzi, C.; Ferraro, P.; Pontarin, G.; Rampazzo, C.; Reichard, P.; Bianchi, V.
Allosteric regulation of the human and mouse deoxyribonucleotide triphosphohydrolase sterile alpha-motif/histidine-aspartate domain-containing protein 1 (SAMHD1)
J. Biol. Chem.
289
18339-18346
2014
Mus musculus (Q60710), Mus musculus, Homo sapiens (Q9Y3Z3), Homo sapiens
Manually annotated by BRENDA team
Bloch, N.; Glaesker, S.; Sitaram, P.; Hofmann, H.; Shepard, C.N.; Schultz, M.L.; Kim, B.; Landau, N.R.
A highly active isoform of lentivirus restriction factor SAMHD1 in mouse
J. Biol. Chem.
292
1068-1080
2017
Mus musculus (Q60710), Mus musculus
Manually annotated by BRENDA team