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Information on EC 3.1.3.74 - pyridoxal phosphatase and Organism(s) Mus musculus and UniProt Accession Q8CHP8

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.74 pyridoxal phosphatase
IUBMB Comments
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.
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Mus musculus
UNIPROT: Q8CHP8
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
plpp/cin, plp phosphatase, pyridoxal phosphatase, pyridoxal phosphate phosphatase, plpase, pyridoxine phosphate phosphatase, pyridoxal-5'-phosphate phosphatase, pyridoxal-5'-phosphate phosphatase/chronophin, pnp phosphatase, pyridoxine 5'-phosphate phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyridoxal phosphate phosphatase
-
PLP phosphatase
-
-
pyridoxal-5'-phosphate phosphatase
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
pyridoxal-5'-phosphate phosphohydrolase
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-92-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + 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
pyridoxal-5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[(E)-2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethenyl]phosphonic acid
compound increases the Km up to 6fold at 2 mM. The catalytic efficiency is reduced to 10% in the presence of 2 mM of the compound
[2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethyl]phosphonic acid
compound increases the Km up to 6fold at 2 mM. The catalytic efficiency is reduced to 10% in the presence of 2 mM of the compound
[2-[5-hydroxy-4-(hydroxymethyl)-6-methylpyridin-3-yl]ethyl]phosphonic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.039
pyridoxal 5'-phosphate
pH 7.4, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
pyridoxal 5'-phosphate
pH 7.4, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50
pyridoxal 5'-phosphate
pH 7.4, 22°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.246
[(E)-2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethenyl]phosphonic acid
Mus musculus
pH 7.4, 22°C
0.079
[2-(4-formyl-5-hydroxy-6-methylpyridin-3-yl)ethyl]phosphonic acid
Mus musculus
pH 7.4, 22°C
1.3
[2-[5-hydroxy-4-(hydroxymethyl)-6-methylpyridin-3-yl]ethyl]phosphonic acid
Mus musculus
pH 7.4, 22°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains C57BL and 129S2
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGP_MOUSE
321
0
34541
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31512
x * 31512, sequence calculation
33000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 31512, sequence calculation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in presence of inhibitor [2-[5-hydroxy-4-(hydroxymethyl)-6-methylpyridin-3-yl]ethyl]phosphonic acid. The overall structure of murine PDXP remains unaltered by ligand binding
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length cDNA, from brain, sequencing, ORF is located on chromosome 15.E1, genomic organization
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jang, Y.M.; Kim, D.W.; Kang, T.C.; Won, M.H.; Baek, N.I.; Moon, B.J.; Choi, S.Y.; Kwon, O.S.
Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution
J. Biol. Chem.
278
50040-50046
2003
Homo sapiens (Q96GD0), Homo sapiens, Mus musculus (P60487), Mus musculus
Manually annotated by BRENDA team
Kim, D.W.; Eum, W.S.; Choi, H.S.; Kim, S.Y.; An, J.J.; Lee, S.H.; Sohn, E.J.; Hwang, S.I.; Kwon, O.S.; Kang, T.C.; Won, M.H.; Cho, S.W.; Lee, K.S.; Park, J.; Choi, S.Y.
Human brain pyridoxal-5'-phosphate phosphatase: production and characterization of monoclonal antibodies
J. Biochem. Mol. Biol.
38
703-708
2005
Bos taurus, Brachylagus idahoensis, Canis lupus familiaris, Felis catus, Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Afjehi-Sadat, L.; Yang, J.W.; Pollak, A.; Kim, D.W.; Choi, S.Y.; Lubec, G.
Structural and functional analysis of hypothetical proteins in mouse hippocampus from two-dimensional gel electrophoresis
J. Proteome Res.
6
711-723
2007
Homo sapiens (Q96GD0), Mus musculus (Q8CHP8), Mus musculus
Manually annotated by BRENDA team
Knobloch, G.; Jabari, N.; Stadlbauer, S.; Schindelin, H.; Koehn, M.; Gohla, A.
Synthesis of hydrolysis-resistant pyridoxal 5-phosphate analogs and their biochemical and X-ray crystallographic characterization with the pyridoxal phosphatase chronophin
Bioorg. Med. Chem.
23
2819-2827
2015
Mus musculus (P60487), Mus musculus
Manually annotated by BRENDA team