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2-aminobenzoyl-Gly-Phe-Ser-Asp-Tyr-Lys(Dnp)-OH + H2O
2-aminobenzoyl-Gly-Phe-Ser + Asp-Tyr-Lys(Dnp)-OH
-
-
-
-
?
ASARM peptide + H2O
?
-
-
-
?
aspartate-rich matrix extracellular phosphoglycoprotein-associated motif peptide + H2O
?
-
-
-
-
?
bone sialoprotein + H2O
?
-
-
-
?
DDSHQ(pS)DESHH(pS)DE(pS)DEL + 2 H2O
DDSHQ(pS) + DESHH(pS) + DE(pS)DEL
-
synthetic peptide derived from human osteopontin ASARM motif sequence, cleavage of DDSHQSDESHHSDESDEL and DD(pS)HQ(pS)DE(pS)HH(pS)DE(pS)DEL is also observed
-
-
?
dentin matrix protein 1 + H2O
8 peptides
-
cleavage sites are Phe173-Asp174, Ser180-Asp181, Ser217-Asp218, and Gln221-Asp222
product analysis: four pieces of about 220 amino acid residues and four pieces of about 300 amino acid residues
?
dentin matrix protein-1 + H2O
?
-
-
-
?
dentin sialophosphoprotein + H2O
dentin sialoprotein + dentin phosphoprotein + dentin glycoprotein
-
-
-
?
matrix extracellular phosphoglycoprotein + H2O
?
-
-
-
?
NH2-RDDSSESSDSGS(PO3H2)SS(PO3H2)ES(PO3H2)DGD-OH + H2O
?
-
-
-
-
?
o-aminobenzoyl-A110WLDSGVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-A110WL + DSGVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on residues 107-139 sequence of the enzyme, cleavage site is the Leu-Asp bond
-
?
o-aminobenzoyl-D124HLSDTSTQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-D124HLS + DTSTQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on residues 107-139 sequence of the enzyme, cleavage site is the Ser-Asp bond
-
?
o-aminobenzoyl-G197QRDSQAQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-G197QR + DSQAQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-G337SNDIMGQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-G337SN + DIMGQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-G386SSDAAEQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-G386SS + DAAEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-NH2 + H2O
o-aminobenzoyl-GFS + DYK-(2,4-dinitrophenyl)-NH2
-
cleavage site is the Ser-Asp bond
-
?
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-GFS + DYK-(2,4-dinitrophenyl)-OH
o-aminobenzoyl-GFSDYQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFS + DYQ-N-(2,4-dinitrophenyl)ethylene diamine
-
cleavage site is the Ser-Asp bond
-
?
o-aminobenzoyl-GFSEY-(2,4-dinitrophenyl)K + H2O
o-aminobenzoyl-GFS + EY-(2,4-dinitrophenyl)K
-
low activity, cleavage site is the Ser-Asp bond
-
?
o-aminobenzoyl-IPSDFEGQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-IPS + DFEGQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-L134ELDSRQ-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-L134EL + DSRQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on residues 107-139 sequence of the enzyme, cleavage site is the Leu-Asp bond
-
?
o-aminobenzoyl-L94MMDFRGQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-L94MM + DFRGQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the FGF-23 protein sequence, cleavage site is the Met-Asp bond
-
?
o-aminobenzoyl-N122GYDVYHQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-N122GY + DVYHQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the FGF-23 protein sequence, cleavage site is the Tyr-Asp bond
-
?
o-aminobenzoyl-N449EMDSFNQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-N449EM + DSFNQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-R175RHTQSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-R175RHTQSAED + DSERQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the FGF-23 protein sequence, cleavage site is the Asp-Asp bond
-
?
o-aminobenzoyl-R175RHTRSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-R175RHTRSAED + DSERQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the FGF-23 protein sequence, cleavage site is the Asp-Asp bond
-
?
o-aminobenzoyl-R441GLDNEIQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-R441GL + DNEIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-R506RDDSSEQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-R506RD + DSSEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-R76SEDAGFQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-R76SE + DAGFQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the FGF-23 protein sequence, cleavage site is the Glu-Asp bond
-
?
o-aminobenzoyl-S212AEDNSPQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-S212AE + DNSPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the FGF-23 protein sequence, cleavage site is the Glu-Asp bond
-
?
o-aminobenzoyl-S513SDSGSQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-S513S + DSGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-T294HLDTKKQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-T294HL + DTKKQ-N-(2,4-dinitrophenyl)ethylene diamine
-
sequence is based on the MEPE protein sequence
-
?
osteopontin + H2O
?
-
-
-
?
parathyroid-hormone-related peptide 107-139 + H2O
L-threonyl-L-arginyl-L-seryl-L-alanyl-L-tryptophyl-L-leucyl-L-alpha-aspartyl-L-serylglycyl-L-valyl-L-threonylglycyl-L-serylglycyl-L-leucyl-L-alpha-glutamylglycyl-L-a-aspartyl-L-histidyl-L-leucyl-L-serine + L-alpha-aspartyl-L-threonyl-L-seryl-L-threonyl-L-threonyl-L-seryl-L-leucyl-L-alpha-glutamyl-L-leucyl-L-alpha-aspartyl-L-seryl-L-arginine + L-threonyl-L-arginyl-L-seryl-L-alanyl-L-tryptophyl-L-leucine + L-alpha-aspartyl-L-threonyl-L-seryl-L-threonyl-L-threonyl-L-seryl-L-leucyl-L-alpha-glutamyl-L-leucine + L-alpha-aspartyl-L-seryl-L-arginine
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-
product determination
?
statherin + H2O
?
-
-
-
?
Z-Ala-Ala-Leu-4-nitroanilide + H2O
Z-Ala-Ala-Leu + 4-nitroaniline
-
chromogenic substrate
-
?
ZAAL-4-nitroanilide + H2O
Z-Ala-Ala-Leu + 4-nitroaniline
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recombinant wild-type enzyme, not the recombinant mutant
-
?
additional information
?
-
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-GFS + DYK-(2,4-dinitrophenyl)-OH
-
-
-
?
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-GFS + DYK-(2,4-dinitrophenyl)-OH
-
best substrate, cleavage site is the Ser-Asp bond
-
?
protein + H2O
peptides
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-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
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-
?
protein + H2O
peptides
-
enzyme is involved in pathology of oncogenic osteomalacia, X-linked hypophosphatemia, and autosomal dominant hypophosphatemic rickets
-
?
protein + H2O
peptides
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enzyme mutations are responsible for X-chromosome linked hypophosphataemia
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?
protein + H2O
peptides
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enzyme mutations are responsible for X-chromosome linked hypophosphataemia by increasing levels of circulating phosphaturic factor
-
?
protein + H2O
peptides
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participates in postsecretory processing, enzyme is involved in regulation of phosphate levels and in bone metabolism
-
?
protein + H2O
peptides
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-
-
?
protein + H2O
peptides
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-
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?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
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inactivating mutations cause X-linked hypophosphatemia, i.e. XLH, which results in the local accumulation of an unknown autocrine/paracrine factor in bone that inhibits mineralization of extracellular matrix
-
?
protein + H2O
peptides
-
-
-
?
protein FGF-23 + H2O
?
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i.e. fibroblastic growth factor 23
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?
protein FGF-23 + H2O
?
-
recombinant wild-type substrate, but not the recombinant mutant FGF-23(R179Q)
-
?
protein FGF-23 + H2O
?
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i.e. fibroblastic growth factor 23, loss of enzyme activity results in either diminished degradation or increased biosynthesis of FGF-23
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?
protein FGF-23 + H2O
?
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-
-
?
additional information
?
-
-
enzyme domain prevents the matrix metalloprotease 2 of binding to integrin alphavbeta3 and blocks cell surface collagenolytic activity
-
?
additional information
?
-
-
interacts with integrin alphavbeta3, natural inhibitor of matrix metalloprotease 2, i.e. MMP-2, thereby regulating the invasive behavior of new blood vessels, enzyme domain disrupts angiogenesis and tumor growth
-
?
additional information
?
-
-
human stanniocalcin STC-1, casein and wild-type as well as mutant FGF-23 proteins are no substrates, recombinant rat parathyroid hormone is no substrate for the wild-type and mutant recombinant enzyme
-
?
additional information
?
-
-
no activity of wild-type and soluble enzyme form with o-aminobenzoyl-RL-N-(2,4-dinitrophenyl)ethylene diamine, no activity with o-aminobenzoyl-GFSEYK-(2,4-dinitrophenyl)-NH2
-
?
additional information
?
-
-
no activity with [Leu]enkephalin, alpha-endorphin, substance P, bradykinin, big-endothelin-1, endothelin-1, alpha-calcitonin, gene-related peptide alpha-CGRP, calcitonin, osteocalcin, parathyroid-hormone-related peptide 1-84, parathyroid-hormone-related peptide 1-34, and osteogenic growth peptide
-
?
additional information
?
-
-
recombinant protein FGF-23, i.e. fibroblastic growth factor 23 seems to be no direct substrate for the enzyme
-
?
additional information
?
-
-
enzyme-deficiency is involved in X-linked hypophosphatemia, XLH, the enzyme inactivates a phosphaturic factor, which may be fibroblast growth factor 23
-
-
?
additional information
?
-
-
glycosaminoglycans interact with PHEX, interfering with its enzyme activity, protein stability and cellular trafficking. This interaction may regulate PHEX function influencing the mineralization process
-
-
?
additional information
?
-
major role of PHEX in X-linked dominant hypophosphatemic rickets
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-
?
additional information
?
-
-
human stanniocalcin STC-1 is no substrate, recombinant rat parathyroid hormone is no substrate for the wild-type and mutant recombinant enzyme
-
?
additional information
?
-
-
the recombinant enzyme, but not the C-terminal deletion mutant, inhibited the cleavage of recombinant human matrix phosphoglycoprotein MEPE by endogenous cathepsin-like enzyme activity in SF9 insect cells, MEPE is no substrate for PHEX
-
?
additional information
?
-
-
enzyme-deficiency is involved in X-linked hypophosphatemia, Hyp, the enzyme inactivates a phosphaturic factor, which may be fibroblast growth factor 23
-
-
?
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0.0015
o-aminobenzoyl-A110WLDSGVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.0013
o-aminobenzoyl-D124HLSDTSTQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.047
o-aminobenzoyl-G197QRDSQAQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.013
o-aminobenzoyl-G337SNDIMGQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.0024
o-aminobenzoyl-G386SSDAAEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.053
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-NH2
-
pseudo-first-order conditions, recombinant soluble enzyme, pH 5.5, 37°C
0.003
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-OH
-
pseudo-first-order conditions, recombinant soluble enzyme, pH 5.5, 37°C
0.013
o-aminobenzoyl-GFSDYQ-N-(2,4-dinitrophenyl)ethylene diamine
-
pseudo-first-order conditions, recombinant soluble enzyme, pH 5.5, 37°C
0.0009
o-aminobenzoyl-L134ELDSRQ-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.017
o-aminobenzoyl-L94MMDFRGQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.009
o-aminobenzoyl-N122GYDVYHQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.037
o-aminobenzoyl-N449EMDSFNQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.0017
o-aminobenzoyl-R175RHTQSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.003
o-aminobenzoyl-R175RHTRSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.007
o-aminobenzoyl-R441GLDNEIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.005
o-aminobenzoyl-R506RDDSSEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.004
o-aminobenzoyl-R76SEDAGFQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.022
o-aminobenzoyl-S212AEDNSPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.032
o-aminobenzoyl-S513SDSGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.015
o-aminobenzoyl-T294HLDTKKQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
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0.04
o-aminobenzoyl-A110WLDSGVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.1
o-aminobenzoyl-D124HLSDTSTQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.2
o-aminobenzoyl-G197QRDSQAQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.01
o-aminobenzoyl-G337SNDIMGQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.3
o-aminobenzoyl-G386SSDAAEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
1.3
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-NH2
-
recombinant soluble enzyme, pH 5.5, 37°C
0.5
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-OH
-
recombinant soluble enzyme, pH 5.5, 37°C
0.6
o-aminobenzoyl-GFSDYQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.05
o-aminobenzoyl-L134ELDSRQ-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.8
o-aminobenzoyl-L94MMDFRGQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.01
o-aminobenzoyl-N122GYDVYHQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.3
o-aminobenzoyl-N449EMDSFNQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.15
o-aminobenzoyl-R175RHTQSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.2
o-aminobenzoyl-R175RHTRSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.03
o-aminobenzoyl-R441GLDNEIQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.5
o-aminobenzoyl-R506RDDSSEQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.06
o-aminobenzoyl-R76SEDAGFQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.3
o-aminobenzoyl-S212AEDNSPQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.2
o-aminobenzoyl-S513SDSGSQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.02
o-aminobenzoyl-T294HLDTKKQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
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C95X
deletion in exon 2 of the PHEX gene 177delC results in a premature stop codon (C59X), suggesting an inactivating truncation of the PHEX protein
E581V
-
site-directed mutagenesis, soluble secreted mutant secPHEXE581V, inactive
L206W
-
missense mutation responsible for X-linked hypophosphatemic rickets
K496X
mice carrying a point mutation in exon 14 of the Phex gene that introduces a stop codon at amino acid 496 of the coding sequence exhibit the classic clinical manifestations of XLH, including growth retardation, skeletal abnormalities (rickets/osteomalacia), hypophosphatemia, and increased serum alkaline phosphatase levels
K496X
mutant mice have increased Fgf23 expression and reduced proteolytic cleavage of intact Fgf23 protein, resulting in markedly elevated intact Fgf23 levels and consequent hypophosphatemia
additional information
-
dPHEX1 inactivation by P-element insertion, homozygous mutant fly embryos show complete lethality in the early stages
additional information
-
construction of an active soluble secreted mutant enzyme form secPHEX, enzyme mutations are responsible for X-chromosome linked hypophosphataemia
additional information
-
overexpression of human PHEX in enzyme-deficient transgenic mutant Hyp mice does not fully rescue the Hyp mouse phenotype, overview
additional information
-
a frameshift mutation (nucleotide 1826-1830delAAAAG, stop after codon 610) in exon 18 is responsible for X-linked hypophosphatemic rickets
additional information
creation and analysis of splice-site mutations. Among 22 splice-site mutations, exon skipping accounts for 73% (16/22). Non-canonical splice-site mutations can result in splicing errors to the same extent as canonical splice-site mutations such as c.436+3G>C, c.436+4A>C, c.436+6T>C, c.437-3C>G, c.850-3C>G, c.1080-3C>A, c.1482+5G>C, c.1586+6T>C, c.1645+5G>A, c.1645+6T>C, c.1701-16T>A, c.1768+5G>A, and c.1899+5G>A. Non-canonical (c.436+6T>C and c.1586+6T>C) and canonical splice-site mutations (c.1769-1G>C) can generate partial splicing errors (both wild-type and mutant transcripts are detected), resulting in incomplete inactivation of PHEX gene. Mutation c.1645C>T (p.R549*) has no impact on pre-mRNA splicing
additional information
-
construction of an inactive C-terminal deletion mutant of the enzyme
additional information
-
construction of C-terminally truncated enzyme version
additional information
-
generation of two mouse lines overexpressing human PHEX, the expression of the hunan gene in transgenic mutant Hyp mice does not fully rescue the Hyp mouse phenotype, heterozygous mice show normal bone and mineral ion homeostasis, Hyp mice show reduced body weight, hypophosphatemia, hyperphosphaturia, and rickets, detailed overview
additional information
-
mutation of Phex leads to the dominant disorder hypophosphatemia which is associated with a renal waste of phosphate and defective bone mineralization
additional information
-
mutation of Phex leads to the dominant disorder hypophosphatemia which is associated with a renal waste of phosphate and defective bone mineralization
-
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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
Mus musculus (P70669), Homo sapiens (P78562)
brenda
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
brenda
Bowe, A.E.; Finnegan, R.; Jan de Beur, S.M.; Cho, J.; Levine, M.A.; Kumar, R.; Schiavi, S.C.
FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate
Biochem. Biophys. Res. Commun.
284
977-981
2001
Homo sapiens
brenda
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
brenda
Boileau, G.; Tenenhouse, H.S.; Desgroseillers, L.; Crine, P.
Characterization of PHEX endopeptidase catalytic activity: identification of parathyroid-hormone-related peptide107-139 as a substrate and osteocalcin, PPi and phosphate as inhibitors
Biochem. J.
355
707-713
2001
Homo sapiens
brenda
Campos, M.; Couture, C.; Hirata, I.Y.; Juliano, M.A.; Loisel, T.P.; Crine, P.; Juliano, L.; Boileau, G.; Carmona, A.K.
Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein
Biochem. J.
373
271-279
2003
Homo sapiens
brenda
Brooks, P.C.; Silletti, S.; von Schalscha, T.L.; Friedlander, M.; Cheresh, D.A.
Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
Cell
92
391-400
1998
Gallus gallus
brenda
Turner, A.J.; Tanzawa, K.
Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX
FASEB J.
11
355-364
1997
Homo sapiens
brenda
Qin, C.; Brunn, J.C.; Cook, R.G.; Orkiszewski, R.S.; Malone, J.P.; Veis, A.; Butler, W.T.
Evidence for the proteolytic processing of dentin matrix protein 1: Identification and characterization of processed fragments and cleavage sites
J. Biol. Chem.
278
34700-34708
2003
Rattus norvegicus
brenda
Liu, S.; Guo, R.; Simpson, L.G.; Xiao, Z.S.; Burnham, C.E.; Quarles, L.D.
Regulation of fibroblastic growth factor 23 expression but not degradation by PHEX
J. Biol. Chem.
278
37419-37426
2003
Homo sapiens
brenda
Alos, N.; Ecarot, B.
Downregulation of osteoblast Phex expression by PTH
Bone
37
589-598
2005
Mus musculus, Mus musculus C57/BL6J
brenda
Ito, M.; Akai, E.; Izuka, M.; Segawa, H.; Kuwahata, M.; Miyamoto, K.
Cloning and characterization of three PHEX homologues in Drosophila
J. Bone Miner. Metab.
22
3-11
2004
Drosophila melanogaster
brenda
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
brenda
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
brenda
Lo, F.S.; Kuo, M.T.; Wang, C.J.; Chang, C.H.; Lee, Z.L.; Van, Y.H.
Two novel PHEX mutations in Taiwanese patients with X-linked hypophosphatemic rickets
Nephron. Physiol.
103
p157-p163
2006
Homo sapiens
brenda
Roetzer, K.M.; Varga, F.; Zwettler, E.; Nawrot-Wawrzyniak, K.; Haller, J.; Forster, E.; Klaushofer, K.
Novel PHEX mutation associated with hypophosphatemic rickets
Nephron. Physiol.
106
8-12
2007
Homo sapiens (P78562)
brenda
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)
brenda
Clausmeyer, S.; Hesse, V.; Clemens, P.C.; Engelbach, M.; Kreuzer, M.; Becker-Rose, P.; Spital, H.; Schulze, E.; Raue, F.
Mutational analysis of the PHEX gene: novel point mutations and detection of large deletions by MLPA in patients with X-linked hypophosphatemic rickets
Calcif. Tissue Int.
85
211-220
2009
Homo sapiens (P78562)
brenda
Gaucher, C.; Walrant-Debray, O.; Nguyen, T.M.; Esterle, L.; Garabedian, M.; Jehan, F.
PHEX analysis in 118 pedigrees reveals new genetic clues in hypophosphatemic rickets
Hum. Genet.
125
401-411
2009
Homo sapiens (P78562)
brenda
Sabbagh, Y.; Jones, A.O.; Tenenhouse, H.S.
PHEXdb, a locus-specific database for mutations causing X-linked hypophosphatemia
Hum. Mutat.
16
1-6
2000
Homo sapiens (P78562)
brenda
Barros, N.M.; Nascimento, F.D.; Oliveira, V.; Juliano, M.A.; Juliano, L.; Loisel, T.; Nader, H.B.; Boileau, G.; Tersariol, I.L.; Carmona, A.K.
The critical interaction of the metallopeptidase PHEX with heparan sulfate proteoglycans
Int. J. Biochem. Cell Biol.
40
2781-2792
2008
Homo sapiens
brenda
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
Mus musculus (P70669), Homo sapiens (P78562)
brenda
Addison, W.N.; Masica, D.L.; Gray, J.J.; McKee, M.D.
Phosphorylation-dependent inhibition of mineralization by osteopontin ASARM peptides is regulated by PHEX cleavage
J. Bone Miner. Res.
25
695-705
2010
Homo sapiens
brenda
Chandran, M.; Chng, C.L.; Zhao, Y.; Bee, Y.M.; Phua, L.Y.; Clarke, B.L.
Novel PHEX Gene Mutation Associated with X Linked Hypophosphatemic Rickets
Nephron. Physiol.
116
17-21
2010
Homo sapiens
brenda
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
brenda
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
brenda
Rowe, P.S.
The chicken or the egg: PHEX, FGF23 and SIBLINGs unscrambled
Cell Biochem. Funct.
30
355-375
2012
Homo sapiens (P78562)
brenda
Rowe, P.S.
Regulation of bone-renal mineral and energy metabolism: the PHEX, FGF23, DMP1, MEPE ASARM pathway
Crit. Rev. Eukaryot. Gene Expr.
22
61-86
2012
Homo sapiens (P78562)
brenda
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)
brenda
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)
brenda
BinEssa, H.; Zou, M.; Al-Enezi, A.; Alomrani, B.; Al-Faham, M.; Al-Rijjal, R.; Meyer, B.; Shi, Y.
Functional analysis of 22 splice-site mutations in the PHEX, the causative gene in X-linked dominant hypophosphatemic rickets
Bone
125
186-193
2019
Homo sapiens (P78562)
brenda
Neves, R.L.; Chiarantin, G.M.D.; Nascimento, F.D.; Pesquero, J.B.; Nader, H.B.; Tersariol, I.L.S.; McKee, M.D.; Carmona, A.K.; Barros, N.M.T.
Expression and inactivation of osteopontin-degrading PHEX enzyme in squamous cell carcinoma
Int. J. Biochem. Cell Biol.
77
155-164
2016
Homo sapiens (P78562), Homo sapiens
brenda
Ma, S.; Vega-Warner, V.; Gillies, C.; Sampson, M.; Kher, V.; Sethi, S.; Otto, E.
Whole exome sequencing reveals novel PHEX splice site mutations in patients with hypophosphatemic rickets
PLoS ONE
10
e0130729
2015
Homo sapiens (P78562)
brenda
Acar, S.; BinEssa, H.; Demir, K.; Al-Rijjal, R.; Zou, M.; Catli, G.; Anik, A.; Al-Enezi, A.; Oezisik, S.; Al-Faham, M.; Abaci, A.; Duendar, B.; Kattan, W.; Alsagob, M.; Kavukcu, S.; Tamimi, H.; Meyer, B.; Boeber, E.; Shi, Y.
Clinical and genetic characteristics of 15 families with hereditary hypophosphatemia Novel mutations in PHEX and SLC34A3
PLoS ONE
13
e0193388
2018
Homo sapiens (P78562)
brenda