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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.4.1 - phosphodiesterase I and Organism(s) Escherichia coli and UniProt Accession P39300

for references in articles please use BRENDA:EC3.1.4.1
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
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.1 phosphodiesterase I
IUBMB Comments
Hydrolyses both ribonucleotides and deoxyribonucleotides. Has low activity towards polynucleotides. A 3'-phosphate terminus on the substrate inhibits hydrolysis.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P39300
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
enpp1, pde4a, phosphodiesterase i, pde i, tyrosyl-dna phosphodiesterase 1, ectonucleotide pyrophosphatase/phosphodiesterase 1, nucleotide phosphodiesterase, cpsf-73, 5'-phosphodiesterase, ectonucleotide pyrophosphatase phosphodiesterase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-exonuclease
-
-
-
-
5'-nucleotide phosphodiesterase
-
-
-
-
5'-phosphodiesterase
-
-
-
-
orthophosphoric diester phosphohydrolase
-
-
-
-
phosphodiesterase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoric ester hydrolysis
-
-
-
-
hydrolysis of phosphoric esters
-
SYSTEMATIC NAME
IUBMB Comments
oligonucleotide 5'-nucleotidohydrolase
Hydrolyses both ribonucleotides and deoxyribonucleotides. Has low activity towards polynucleotides. A 3'-phosphate terminus on the substrate inhibits hydrolysis.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-82-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bis-p-nitrophenyl phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
show the reaction diagram
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
p-nitrophenyl phosphate + nitrophenol
show the reaction diagram
-
-
-
-
?
p-nitrophenyl 5'-thymidine monophosphate + H2O
p-nitrophenol + 5'-thymidine monophosphate
show the reaction diagram
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
enzyme carries two zinc ions per active site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.74 - 18.3
bis-p-nitrophenyl phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.8 - 20.3
bis-p-nitrophenyl phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
79400
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
crystallitazion data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.25 A resolution, in presence and absence of sulfate inhibitor. Protein has a beta-sandwich architecture and is a tetramer with two zinc ions per active site
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4oC, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuznetsova, E.; Proudfoot, M.; Sanders, S.A.; Reinking, J.; Savchenko, A.; Arrowsmith, C.H.; Edwards, A.M.; Yakunin, A.F.
Enzyme genomics: Application of general enzymatic screens to discover new enzymes
FEMS Microbiol. Rev.
29
263-279
2005
Escherichia coli (P37049), Escherichia coli (P39300), Escherichia coli (P67095)
Manually annotated by BRENDA team
Miller, D.J.; Shuvalova, L.; Evdokimova, E.; Savchenko, A.; Yakunin, A.F.; Anderson, W.F.
Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene
Protein Sci.
16
1338-1348
2007
Escherichia coli
Manually annotated by BRENDA team