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Information on EC 3.1.3.3 - phosphoserine phosphatase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58989

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.3 phosphoserine phosphatase
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Methanocaldococcus jannaschii
UNIPROT: Q58989 not found.
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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
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CTD phosphatase fcp1
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O-phosphoserine phosphohydrolase
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phosphatase, phosphoserine
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PSP
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PSPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
O-phosphoserine phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-73-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-phospho-D-serine + H2O
D-serine + phosphate
show the reaction diagram
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-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
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-
?
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
O-phospho-D-serine + H2O
D-serine + phosphate
show the reaction diagram
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-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
at near-physiological ratios of aluminum to magnesium, aluminum can dominate over magnesium in the enzyme-metal fluoride inhibitory TSA complexes, aluminium is the more likely origin of some of the physiological effects of fluoride
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BeF3-
at 50°C, the hydrolytic activity of is markedly inhibited (more than 95%) in the presence of both BeCl2 and NaF. The latter is provided at concentrations that yield predominantly BeF3- in situ. Either BeCl2 or NaF alone has a much smaller inhibitory effect (35 or 20%, respectively). Similar inhibition by BeF3- is observed at room temperature or at 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 9.2
fluoride chemical shifts constant throughout the pH range examined
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown by using the hanging drop vapor diffusion method with seeding.1.5 A resolution the X-ray crystal structure of the complex of BeF3 2 with phosphoserine phosphatase. The structure is comparable to that of a phosphoenzyme intermediate: BeF3- is bound to Asp11 with the tetrahedral geometry of a phosphoryl group, is coordinated to Mg2+, and is bound to residues surrounding the active site that are conserved in the haloacid dehalogenase (HAD) superfamily
high-resolution, 1.5-1.9 A structures which define the open state prior to substrate binding, the complex with phosphoserine substrate bound, and the complex with AlF3, a transition-state analog for the phospho-transfer steps in the reaction
hanging-drop vapor-diffusion method, crystal structure determined at 1.8 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, W.; Cho, H.S.; Kim, R.; Jancarik, J.; Yokota, H.; Nguyen, H.H.; Grigoriev, I.V.; Wemmer, D.E.; Kim, S.H.
Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states
J. Mol. Biol.
319
421-431
2002
Methanocaldococcus jannaschii (Q58989), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Wang, W.; Kim, R.; Jancarik, J.; Yokota, H.; Kim, S.H.
Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution
Structure
9
65-71
2001
Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Baxter, N.J.; Blackburn, G.M.; Marston, J.P.; Hounslow, A.M.; Cliff, M.J.; Bermel, W.; Williams, N.H.; Hollfelder, F.; Wemmer, D.E.; Waltho, J.P.
Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes
J. Am. Chem. Soc.
130
3952-3958
2008
Methanocaldococcus jannaschii (Q58989), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Cho, H.; Wang, W.; Kim, R.; Yokota, H.; Damo, S.; Kim, S.H.; Wemmer, D.; Kustu, S.; Yan, D.
BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase
Proc. Natl. Acad. Sci. USA
98
8525-8530
2001
Methanocaldococcus jannaschii (Q58989), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58989)
Manually annotated by BRENDA team
Krachtus, D.; Smith, J.C.; Imhof, P.
Quantum mechanical/molecular mechanical analysis of the catalytic mechanism of phosphoserine phosphatase
Molecules
23
3342
2018
Methanocaldococcus jannaschii (Q58989), Methanocaldococcus jannaschii ATCC 43067 (Q58989)
Manually annotated by BRENDA team