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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.4.17 - 3',5'-cyclic-nucleotide phosphodiesterase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P22434

for references in articles please use BRENDA:EC3.1.4.17
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
                3.1.4.17 3',5'-cyclic-nucleotide phosphodiesterase
IUBMB Comments
Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP, 3',5'-cyclic GMP and 3',5'-cyclic CMP.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P22434
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: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
pde4d, cyclic nucleotide phosphodiesterase, pde10a, camp phosphodiesterase, pde3a, pde3b, pde2a, camp-pde, phosphodiesterase 3, pde11a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphodiesterase-1
-
3',5'-cyclic nucleoside monophosphate phosphodiesterase
-
-
-
-
3',5'-cyclonucleotide phosphodiesterase
-
-
-
-
3',5'-nucleotide phosphodiesterase
-
-
-
-
3':5'-CNP
-
-
-
-
3':5'-cyclic nucleotide 5'-nucleotidohydrolase
-
-
-
-
61 kDa Cam-PDE
-
-
-
-
63 kDa Cam-PDE
-
-
-
-
Cam-PDE 1A
-
-
-
-
Cam-PDE 1B
-
-
-
-
Cam-PDE 1C
-
-
-
-
CGB-PDE
-
-
-
-
CGIP1
-
-
-
-
CGIPDE1
-
-
-
-
cGMP-binding cGMP-specific phosphodiesterase
-
-
-
-
CGS-PDE
-
-
-
-
cGSPDE
-
-
-
-
cyclic 3',5'-mononucleotide phosphodiesterase
-
-
-
-
cyclic 3',5'-nucleotide phosphodiesterase
-
-
-
-
cyclic 3',5'-phosphodiesterase
-
-
-
-
cyclic 3',5-nucleotide monophosphate phosphodiesterase
-
-
-
-
Cyclic GMP stimulated phosphodiesterase
-
-
-
-
cyclic nucleotide phosphodiesterase
-
-
-
-
DPDE1
-
-
-
-
DPDE2
-
-
-
-
DPDE3
-
-
-
-
DPDE4
-
-
-
-
Dunce protein
-
-
-
-
GMP-PDE alpha
-
-
-
-
GMP-PDE beta
-
-
-
-
GMP-PDE delta
-
-
-
-
GMP-PDE gamma
-
-
-
-
HCP1
-
-
-
-
High-affinity cAMP phosphodiesterase
-
-
-
-
Learning/ memory process protein
-
-
-
-
Low-affinity cAMP phosphodiesterase
-
-
-
-
MMPDE8
-
-
-
-
nucleoside 3',5'-cyclic phosphate diesterase
-
-
-
-
nucleoside-3',5-monophosphate phosphodiesterase
-
-
-
-
p17 protein
-
-
-
-
P2A
-
-
-
-
PDE V-B1
-
-
-
-
PDE V-C1
-
-
-
-
PDE21
-
-
-
-
PDE32
-
-
-
-
PDE43
-
-
-
-
PDE46
-
-
-
-
PDEase
-
-
-
-
PDEase regA
-
-
-
-
phosphodiesterase, cyclic 3',5'-nucleotide
-
-
-
-
TM22
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3',5'-cyclic-nucleotide 5'-nucleotidohydrolase
Acts on 3',5'-cyclic AMP, 3',5'-cyclic dAMP, 3',5'-cyclic IMP, 3',5'-cyclic GMP and 3',5'-cyclic CMP.
CAS REGISTRY NUMBER
COMMENTARY hide
9040-59-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3',5'-cAMP + H2O
5'-AMP
show the reaction diagram
-
-
-
?
3',5'-cGMP + H2O
5'-GMP
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0773 - 0.1175
3',5'-cAMP
0.0968 - 0.1913
3',5'-cGMP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.1 - 21
3',5'-cAMP
10.8 - 15.1
3',5'-cGMP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
100 - 213
3',5'-cAMP
75 - 156
3',5'-cGMP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
unliganded enzyme, and in complex with cGMP, both to 1.3 A resolution. For the massive interactions between two monomers, the dimeric form of the enzyme is a biologic unit for its function
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tian, Y.; Cui, W.; Huang, M.; Robinson, H.; Wan, Y.; Wang, Y.; Ke, H.
Dual specificity and novel structural folding of yeast phosphodiesterase-1 for hydrolysis of second messengers cyclic adenosine and guanosine 3,5-monophosphate
Biochemistry
53
4938-4945
2014
Saccharomyces cerevisiae (P22434), Saccharomyces cerevisiae
Manually annotated by BRENDA team