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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.3 - phosphoserine phosphatase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC3.1.3.3
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
                3.1.3.3 phosphoserine phosphatase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
psp, serine/threonine protein phosphatase, phosphoserine phosphatase, pspase, ctd phosphatase fcp1, serb653, serb2, l-phosphoserine phosphatase, 3-phosphoserine phosphatase, ipsp1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-phosphoserine phosphatase
-
-
-
-
CTD phosphatase fcp1
-
-
-
-
HPSP
-
-
O-phosphoserine phosphohydrolase
-
-
-
-
phosphatase, phosphoserine
-
-
-
-
phosphoserine phosphatase
-
-
PSPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
O-phosphoserine phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-73-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
?
D-phosphoserine + H2O
D-Ser + phosphate
show the reaction diagram
-
-
-
?
L-3-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
-
?
L-O-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
L-phosphoserine + H2O
L-Ser + phosphate
show the reaction diagram
-
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-D-serine + H2O
D-serine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-tyrosine + H2O
L-Tyr + phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
L-O-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
-
enzyme is responsible for the third and final step of the L-serine biosynthetic pathway
-
?
O-phospho-D-serine + H2O
D-serine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chlorpromazine
-
-
Mn2+
-
-
Trifluorperazine
-
-
vanadate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chlordiazepoxide
-
activation
diazepam
-
activation
sucrose
-
activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
D-phosphoserine
-
-
0.036
L-phosphoserine
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 6.6
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cortex, brain stem, cerebellum, striatum, thalamus hippocampus
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
highly induced in squamous cell carcinoma
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cytoplasmic protein in keratinocytes that primarily localizes to endosomes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knock down of PSPH dramatically diminishes squamous cell carcinoma cell proliferation and cyclin D1 levels in the presence of exogenous of L-serine production suggesting a non-canonical role for PSPH in epithelial carcinogenesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SERB_HUMAN
225
0
25008
Swiss-Prot
other Location (Reliability: 2)
Q53EY1_HUMAN
225
0
24949
TrEMBL
other Location (Reliability: 2)
A0A024RDL3_HUMAN
225
0
25008
TrEMBL
other Location (Reliability: 2)
A0A024RDL9_HUMAN
252
0
28082
TrEMBL
Mitochondrion (Reliability: 2)
C9JBI3_HUMAN
187
0
20745
TrEMBL
other Location (Reliability: 2)
PLPP_HUMAN
296
0
31698
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour-diffusion method. A resolution of 1.53 A provides a detailed model of the active site in a completely open conformation and the water molecules bound to it
-
hanging-drop vapour diffusion method
-
hanging-drop vapour-diffusion method
-
replacement of sixfold coordinated Mg2+ in active site by Ca2+ results in sevenfold coordinated metal ion, explaining the inhibitory effect of Ca2+
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E29D
-
less than 5% of the activity of wild-type enzyme with L-phosphoserine as substrate
E29Q
-
inactive mutant enzyme
N133A
-
about 25% of the activity of wild-type enzyme with L-phosphoserine as substrate
N133D
-
about 130% of the activity of wild-type enzyme with L-phosphoserine as substrate
R202A
-
inactive mutant enzyme
R202K
-
less than 5% of the activity of wild-type enzyme with L-phosphoserine as substrate
R65A
-
inactive mutant enzyme
R65K
-
inactive mutant enzyme
S23A
-
about 50% of the activity of wild-type enzyme with L-phosphoserine as substrate
S23T
-
about 20% of the activity of wild-type enzyme with L-phosphoserine as substrate
T182S
-
about 5% of the activity of wild-type enzyme with L-phosphoserine as substrate
T182V
-
about 75% of the activity of wild-type enzyme with L-phosphoserine as substrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
highly induced in squamous cell carcinoma
-
in MDA-MB-231(SA) cell
-
the enzyme activity is elevated in patients with schizophrenia, especially in male patients
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shetty, V.; Shetty, K.T.
Phosphoserine phosphatase of human brain: partial purification, characterization, regional distribution, and effect of certain modulators including psychoactive drugs
Neurochem. Res.
16
1203-1210
1991
Homo sapiens
-
Manually annotated by BRENDA team
Peeraer, Y.; Rabijns, A.; Verboven, C.; Collet, J.F.; Van Schaftingen, E.; De Ranter, C.
Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase
Acta Crystallogr. Sect. D
58
133-134
2002
Homo sapiens
Manually annotated by BRENDA team
Peeraer, Y.; Rabijns, A.; Verboven, C.; Collet, J.F.; Van Schaftingen, E.; De Ranter, C.
High-resolution structure of human phosphoserine phosphatase in open conformation
Acta Crystallogr. Sect. D
59
971-977
2003
Homo sapiens
Manually annotated by BRENDA team
Kim, H.Y.; Heo, Y.S.; Kim, J.H.; Park, M.H.; Moon, J.; Kim, E.; Kwon, D.; Yoon, J.; Shin, D.; Jeong, E.J.; Park, S.Y.; Lee, T.G.; Jeon, Y.H.; Ro, S.; Cho, J.M.; Hwang, K.Y.
Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase
J. Biol. Chem.
277
46651-46658
2002
Homo sapiens
Manually annotated by BRENDA team
Peeraer, Y.; Rabijns, A.; Collet, J.F.; Van Schaftingen, E.; De Ranter, C.
How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase
Eur. J. Biochem.
271
3421-3427
2004
Homo sapiens
Manually annotated by BRENDA team
Pollari, S.; Kaekoenen, S.M.; Edgren, H.; Wolf, M.; Kohonen, P.; Sara, H.; Guise, T.; Nees, M.; Kallioniemi, O.
Enhanced serine production by bone metastatic breast cancer cells stimulates osteoclastogenesis
Breast Cancer Res. Treat.
125
421-430
2011
Homo sapiens
Manually annotated by BRENDA team
Bachelor, M.A.; Lu, Y.; Owens, D.M.
L-3-Phosphoserine phosphatase (PSPH) regulates cutaneous squamous cell carcinoma proliferation independent of L-serine biosynthesis
J. Dermatol. Sci.
63
164-172
2011
Homo sapiens
Manually annotated by BRENDA team
Sato, K.; Masuda, T.; Hu, Q.; Tobo, T.; Kidogami, S.; Ogawa, Y.; Saito, T.; Nambara, S.; Komatsu, H.; Hirata, H.; Sakimura, S.; Uchi, R.; Hayashi, N.; Iguchi, T.; Eguchi, H.; Ito, S.; Nakagawa, T.; Mimori, K.
Phosphoserine phosphatase is a novel prognostic biomarker on chromosome 7 in colorectal cancer
Anticancer Res.
37
2365-2371
2017
Homo sapiens (P78330)
Manually annotated by BRENDA team
Li, X.; Xun, Z.; Yang, Y.
Inhibition of phosphoserine phosphatase enhances the anticancer efficacy of 5-fluorouracil in colorectal cancer
Biochem. Biophys. Res. Commun.
477
633-639
2016
Homo sapiens (P78330), Homo sapiens
Manually annotated by BRENDA team
Ozeki, Y.; Sekine, M.; Fujii, K.; Watanabe, T.; Okayasu, H.; Takano, Y.; Shinozaki, T.; Aoki, A.; Akiyama, K.; Homma, H.; Shimoda, K.
Phosphoserine phosphatase activity is elevated and correlates negatively with plasma D-serine concentration in patients with schizophrenia
Psychiatry Res.
237
344-350
2016
Homo sapiens (P78330), Homo sapiens
Manually annotated by BRENDA team