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Information on EC 3.4.24.B15 - PHEX peptidase and Organism(s) Mus musculus and UniProt Accession P70669

for references in articles please use BRENDA:EC3.4.24.B15
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B15 PHEX peptidase
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This record set is specific for:
Mus musculus
UNIPROT: P70669
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic degradation of proteins
Synonyms
phex enzyme, phosphate-regulating neutral endopeptidase, dphex, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M13.091
Merops-ID
metalloendopeptidase homolog PEX
-
phosphate regulating neutral endopeptidase
-
phosphate-regulating gene with homologies to endopeptidases on the X chromosome
-
vitamin D-resistant hypophosphatemic rickets protein
-
X-linked hypophosphatemia protein
-
M13.091
-
Merops-ID
matrix metalloprotease 2 hemopexin domain
-
-
-
-
phosphate-regulating gene with homologies to endopeptidases on the X chromosome
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
enzyme is an endopeptidase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
263550-81-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protein + H2O
peptides
show the reaction diagram
-
-
?
protein FGF-23 + H2O
?
show the reaction diagram
-
-
-
?
aspartate-rich matrix extracellular phosphoglycoprotein-associated motif peptide + H2O
?
show the reaction diagram
-
-
-
-
?
NH2-RDDSSESSDSGS(PO3H2)SS(PO3H2)ES(PO3H2)DGD-OH + H2O
?
show the reaction diagram
-
-
-
-
?
protein + H2O
peptides
show the reaction diagram
ZAAL-4-nitroanilide + H2O
Z-Ala-Ala-Leu + 4-nitroaniline
show the reaction diagram
-
recombinant wild-type enzyme, not the recombinant mutant
-
?
additional information
?
-
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
protein + H2O
peptides
show the reaction diagram
-
-
?
protein FGF-23 + H2O
?
show the reaction diagram
-
-
-
?
aspartate-rich matrix extracellular phosphoglycoprotein-associated motif peptide + H2O
?
show the reaction diagram
-
-
-
-
?
NH2-RDDSSESSDSGS(PO3H2)SS(PO3H2)ES(PO3H2)DGD-OH + H2O
?
show the reaction diagram
-
-
-
-
?
protein + H2O
peptides
show the reaction diagram
additional information
?
-
-
enzyme-deficiency is involved in X-linked hypophosphatemia, Hyp, the enzyme inactivates a phosphaturic factor, which may be fibroblast growth factor 23
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
-
type II membrane-bound zinc metalloprotease
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
inhibits proteolyic activity but not the protease inhibiting activity of the enzyme
additional information
-
the major regulator of bone development and turnover PTH, commercial preperation from rat, decreases osteoblastic Phex expression and matrix mineralization in vitro and in vivo, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
6.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MC3T3-E1 clonal osteoblast, not in immature MC3T3-E1 preosteoblasts
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
inactivation of PHEX results in equivalent intrinsic bone mineralization defects and increased fibroblastic growth factor 23 expression in osteocytes
physiological function
-
PHEX and DMP1 control a common pathway regulating bone mineralization and fibroblastic growth factor 23 production, the latter involving activation of the fibroblastic growth factor receptor signaling in osteocytes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHEX_MOUSE
749
0
86419
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
x * 60000, recombinant C-terminally truncated mutant, SDS-PAGE, x * 86000, deglycosylated recombinant enzyme, SDS-PAGE, x * 100000, glycosylated recombinant enzyme, SDS-PAGE
60000
-
x * 60000, recombinant C-terminally truncated mutant, SDS-PAGE, x * 86000, deglycosylated recombinant enzyme, SDS-PAGE, x * 100000, glycosylated recombinant enzyme, SDS-PAGE
86000
-
x * 60000, recombinant C-terminally truncated mutant, SDS-PAGE, x * 86000, deglycosylated recombinant enzyme, SDS-PAGE, x * 100000, glycosylated recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 60000, recombinant C-terminally truncated mutant, SDS-PAGE, x * 86000, deglycosylated recombinant enzyme, SDS-PAGE, x * 100000, glycosylated recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
6 N-glycosylation sites, recombinant and wild-type enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K496X
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from SF9 insect cells as His-tagged protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA determination and analysis, expression of wild-type and C-terminally truncated mutant as His-tagged protein in Spodoptera frugiperda Sf9 cells via baculovirus infection
-
expression of wild-type and mutant enzyme in Spodoptera frugiperda Sf9 cells via baculovirus infection, recombinant enzyme is located in the membranes of the Sf9 cells
-
the gene is localized on the X chromosome
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
both male and female hypophosphatemic mice at 9 months of age have a mineral phenotype that is corrected by osteoblast-specific expression of the hPHEX gene. The morphometric phenotype and the serum chemistry, however, are not fully corrected
medicine
-
alterations in the PHEX expression underlie X-linked hypophosphatemia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (P78562), Mus musculus (P70669)
Manually annotated by BRENDA team
Guo, R.; Liu, S.; Spurney, R.F.; Quarles, L.D.
Analysis of recombinant Phex: an endopeptidase in search of a substrate
Am. J. Physiol.
281
E837-847
2001
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Guo, R.; Rowe, P.S.; Liu, S.; Simpson, L.G.; Xiao, Z.S.; Darryl Quarles, L.D.
Inhibition of MEPE cleavage by Phex
Biochem. Biophys. Res. Commun.
297
38-45
2002
Mus musculus
Manually annotated by BRENDA team
Alos, N.; Ecarot, B.
Downregulation of osteoblast Phex expression by PTH
Bone
37
589-598
2005
Mus musculus, Mus musculus C57/BL6J
Manually annotated by BRENDA team
Erben, R.G.; Mayer, D.; Weber, K.; Jonsson, K.; Jueppner, H.; Lanske, B.
Overexpression of human PHEX under the human beta-actin promoter does not fully rescue the Hyp mouse phenotype
J. Bone Miner. Res.
20
1149-1160
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Yuan, B.; Takaiwa, M.; Clemens, T.L.; Feng, J.Q.; Kumar, R.; Rowe, P.S.; Xie, Y.; Drezner, M.K.
Aberrant Phex function in osteoblasts and osteocytes alone underlies murine X-linked hypophosphatemia
J. Clin. Invest.
118
722-734
2008
Mus musculus
Manually annotated by BRENDA team
Boskey, A.; Frank, A.; Fujimoto, Y.; Spevak, L.; Verdelis, K.; Ellis, B.; Troiano, N.; Philbrick, W.; Carpenter, T.
The PHEX transgene corrects mineralization defects in 9-month-old hypophosphatemic mice
Calcif. Tissue Int.
84
126-137
2009
Mus musculus (P70669)
Manually annotated by BRENDA team
Guo, R.; Quarles, L.D.
Cloning and sequencing of human PEX from a bone cDNA library: evidence for its developmental stage-specific regulation in osteoblasts
J. Bone Miner. Res.
12
1009-1017
1997
Homo sapiens (P78562), Mus musculus (P70669)
Manually annotated by BRENDA team
David, V.; Martin, A.; Hedge, A.M.; Drezner, M.K.; Rowe, P.S.
ASARM peptides: PHEX-dependent and -independent regulation of serum phosphate
Am. J. Physiol. Renal Physiol.
300
F783-F791
2011
Mus musculus
Manually annotated by BRENDA team
Martin, A.; Liu, S.; David, V.; Li, H.; Karydis, A.; Feng, J.Q.; Quarles, L.D.
Bone proteins PHEX and DMP1 regulate fibroblastic growth factor Fgf23 expression in osteocytes through a common pathway involving FGF receptor (FGFR) signaling
FASEB J.
25
2551-2562
2011
Mus musculus
Manually annotated by BRENDA team
Ichikawa, S.; Austin, A.; Gray, A.; Econs, M.
A Phex mutation in a murine model of X-linked hypophosphatemia alters phosphate responsiveness of bone cells
J. Bone Miner. Res.
27
453-460
2012
Mus musculus (P70669)
Manually annotated by BRENDA team
Owen, C.; Chen, F.; Flenniken, A.M.; Osborne, L.R.; Ichikawa, S.; Adamson, S.L.; Rossant, J.; Aubin, J.E.
A novel Phex mutation in a new mouse model of hypophosphatemic rickets
J. Cell. Biochem.
113
2432-2441
2012
Mus musculus (P70669)
Manually annotated by BRENDA team