Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.6 - 3'-nucleotidase and Organism(s) Escherichia coli and UniProt Accession P08331

for references in articles please use BRENDA:EC3.1.3.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.6 3'-nucleotidase
IUBMB Comments
Wide specificity for 3'-nucleotides.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P08331
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3'-nucleotidase, 3'-nucleotidase/nuclease, 3'nt/nu, 3'-n'ase, ld3'nt/nu, 3'-nt/nu, la3'-nucleotidase, ecto-3'-nucleotidase, 3'nucleotidase/nuclease, 3'-nt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CpdB
the protein has 3 '-nucleotidase and 2 ',3 '-cyclic-mononucleotide phosphodiesterase activities
3'-mononucleotidase
-
-
-
-
3'-phosphatase
-
-
-
-
3'-ribonucleotidase
-
-
-
-
Deoxyribonuclease PA3
-
-
-
-
Endonuclease PA3
-
-
-
-
nucleotidase, 3'-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
phosphorous acid anhydride hydrolysis
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3'-ribonucleotide phosphohydrolase
Wide specificity for 3'-nucleotides.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-84-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
highly efficient substrate
-
-
?
(polyphosphate)n + H2O
(polyphosphate)(n-1) + phosphate
show the reaction diagram
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
3'-CMP + H2O
cytosine + phosphate
show the reaction diagram
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
the bifunctional enzyme with 3'-nucleotidase and cyclic diadenylate phosphodiesterase activities also exhibits very high efficiencies for 2 ',3 '-cyclic mononucleotides, c-di-GMP, c-di-AMP, 2',3'-cAMP and bis-4-nitrophenylphosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the enzyme activity is enhanced by 2 mM Co2+
Co2+
the enzyme activity is strongly enhanced by 2 mM Co2+
Mn2+
2 mM used in assay conditions
Co2+
KD: 46.9 +/- 5.66 microM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
Mg2+
KD: 224.7 +/- 35.1 microM Mg2+ with p-nitrophenyl phosphate, KD: 140.0 +/- 9.99 microM Mg2+ with 5'-AMP
Mn2+
KD: 7.24 +/- 0.71 microM Mn2+ with p-nitrophenyl phosphate, KD: 2.23 +/- 0.14 micorM Mn2+ with 5'-AMP
Ni2+
KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
3'-AMP
at pH 7.5 and 37°C
0.02
(Polyphosphate)n
+/- 0.003
0.1
3'-AMP
+/- 0.01
0.37
3'-CMP
+/- 0.08
0.32
5'-AMP
+/- 0.04
0.28
5'-dGMP
+/- 0.04
0.26
5'-GMP
+/- 0.05
2.49
p-nitrophenyl phosphate
+/- 0.4
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
176
3'-AMP
at pH 7.5 and 37°C
0.05
(Polyphosphate)n
+/- 0.005
9.84
3'-AMP
+/- 0.37
5.93
3'-CMP
+/- 0.44
4.9
5'-AMP
+/- 0.3
8.04
5'-dGMP
+/- 0.39
11
5'-GMP
+/- 0.87
3.55
p-nitrophenyl phosphate
+/- 0.16
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13000
3'-AMP
at pH 7.5 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.1
ATP
with 3'-AMP as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
+/- 0.01, polyphosphate
10
+/- 0.61, 5'-AMP
12.1
+/- 0.90, 3'-CMP
16.4
+/- 0.80, 5'-dGMP
20.1
+/- 0.76, 3'-AMP
22.4
+/- 1.78, 5'-GMP
7.24
+/- 0.34, p-nitrophenyl phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 69000, fusion protein with glutathione S-transferase, SDS-PAGE
monomer
in solution
oligomer
at least four identical subunits in solution
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography, Q-Sepharose column chromatography and Sephadex G-100 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 and JM109 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Proudfoot, M.; Kuznetsova, E.; Brown, G.; Rao, N.N.; Kitagawa, M.; Mori, H.; Savchenko, A.; Yakunin, A.F.
General Enzymatic Screens Identify Three New Nucleotidases in Escherichia coli. Biochemical Characterization of SurE, YfbR, and Yjjg
J. Biol. Chem.
279
54687-54694
2004
Escherichia coli (P0A840)
Manually annotated by BRENDA team
Lopez-Villamizar, I.; Cabezas, A.; Pinto, R.; Canales, J.; Ribeiro, J.; Cameselle, J.; Costas, M.
The characterization of Escherichia coli CpdB as a recombinant protein reveals that, besides having the expected 3'-nucleotidase and 2,3-cyclic mononucleotide phosphodiesterase activities, it is also active as cyclic dinucleotide phosphodiesterase
PLoS ONE
11
e0148508
2016
Escherichia coli (P08331)
Manually annotated by BRENDA team