Information on EC 3.4.24.B15 - PHEX peptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.B15
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
PHEX peptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
263550-81-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
three isozymes dPHEX1-3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-Gly-Phe-Ser-Asp-Tyr-Lys(Dnp)-OH + H2O
2-aminobenzoyl-Gly-Phe-Ser + Asp-Tyr-Lys(Dnp)-OH
show the reaction diagram
-
-
-
-
?
ASARM peptide + H2O
?
show the reaction diagram
-
-
-
-
?
aspartate-rich matrix extracellular phosphoglycoprotein-associated motif peptide + H2O
?
show the reaction diagram
-
-
-
-
?
bone sialoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
DDSHQ(pS)DESHH(pS)DE(pS)DEL + 2 H2O
DDSHQ(pS) + DESHH(pS) + DE(pS)DEL
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
dentin sialophosphoprotein + H2O
dentin sialoprotein + dentin phosphoprotein + dentin glycoprotein
show the reaction diagram
-
-
-
-
?
enamelin + H2O
?
show the reaction diagram
-
-
-
-
?
matrix extracellular phosphoglycoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
NH2-RDDSSESSDSGS(PO3H2)SS(PO3H2)ES(PO3H2)DGD-OH + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-A110WLDSGVQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-A110WL + DSGVQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
sequence is based on residues 107-139 sequence of the enzyme, cleavage site is the Leu-Asp bond
-
?
o-aminobenzoyl-D124HLSDTSTQN-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-D124HLS + DTSTQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
sequence is based on the MEPE protein sequence
-
?
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-NH2 + H2O
o-aminobenzoyl-GFS + DYK-(2,4-dinitrophenyl)-NH2
show the reaction diagram
-
cleavage site is the Ser-Asp bond
-
?
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-GFS + DYK-(2,4-dinitrophenyl)-OH
show the reaction diagram
o-aminobenzoyl-GFSDYQ-N-(2,4-dinitrophenyl)ethylene diamine + H2O
o-aminobenzoyl-GFS + DYQ-N-(2,4-dinitrophenyl)ethylene diamine
show the reaction diagram
-
cleavage site is the Ser-Asp bond
-
?
o-aminobenzoyl-GFSEY-(2,4-dinitrophenyl)K + H2O
o-aminobenzoyl-GFS + EY-(2,4-dinitrophenyl)K
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
sequence is based on the MEPE protein sequence
-
?
osteopontin + H2O
?
show the reaction diagram
-
-
-
-
?
parathyroid-hormone-related peptide 107-139 + H2O
fragments
show the reaction diagram
-
-
product determination
?
protein + H2O
peptides
show the reaction diagram
protein FGF-23 + H2O
?
show the reaction diagram
statherin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Ala-Ala-Leu-4-nitroanilide + H2O
Z-Ala-Ala-Leu + 4-nitroaniline
show the reaction diagram
-
chromogenic substrate
-
?
ZAAL-4-nitroanilide + H2O
?
show the reaction diagram
-
recombinant wild-type enzyme, not the recombinant mutant
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ASARM peptide + H2O
?
show the reaction diagram
-
-
-
-
?
aspartate-rich matrix extracellular phosphoglycoprotein-associated motif peptide + H2O
?
show the reaction diagram
-
-
-
-
?
bone sialoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
dentin matrix protein-1 + H2O
?
show the reaction diagram
-
-
-
-
?
dentin sialophosphoprotein + H2O
dentin sialoprotein + dentin phosphoprotein + dentin glycoprotein
show the reaction diagram
-
-
-
-
?
enamelin + H2O
?
show the reaction diagram
-
-
-
-
?
matrix extracellular phosphoglycoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
NH2-RDDSSESSDSGS(PO3H2)SS(PO3H2)ES(PO3H2)DGD-OH + H2O
?
show the reaction diagram
-
-
-
-
?
osteopontin + H2O
?
show the reaction diagram
-
-
-
-
?
protein + H2O
peptides
show the reaction diagram
protein FGF-23 + H2O
?
show the reaction diagram
statherin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
complete inhibition at 1 mM
chondroitin sulfate
-
-
diphosphate
-
50% inhibition at 2.5 mM
heparan sulfate
-
-
heparin
-
-
NaCl
-
2fold lower kcat/Km, but required for stability
osteocalcin
-
50% inhibition at 0.0036 mM, Ca2+ reverses the effect
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no effect of Ca2+ alone
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
o-aminobenzoyl-A110WLDSGVQ-N-(2,4-dinitrophenyl)ethylene diamine
-
recombinant soluble enzyme, pH 5.5, 37°C
0.0013
o-aminobenzoyl-D124HLSDTSTQN-(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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
o-aminobenzoyl-A110WLDSGVQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.1
o-aminobenzoyl-D124HLSDTSTQN-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.2
o-aminobenzoyl-G197QRDSQAQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.01
o-aminobenzoyl-G337SNDIMGQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.3
o-aminobenzoyl-G386SSDAAEQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
1.3
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-NH2
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.5
o-aminobenzoyl-GFSDYK-(2,4-dinitrophenyl)-OH
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.6
o-aminobenzoyl-GFSDYQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.05
o-aminobenzoyl-L134ELDSRQ-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.8
o-aminobenzoyl-L94MMDFRGQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.01
o-aminobenzoyl-N122GYDVYHQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.3
o-aminobenzoyl-N449EMDSFNQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.15
o-aminobenzoyl-R175RHTQSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.2
o-aminobenzoyl-R175RHTRSAEDDSERQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.03
o-aminobenzoyl-R441GLDNEIQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.5
o-aminobenzoyl-R506RDDSSEQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.06
o-aminobenzoyl-R76SEDAGFQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.3
o-aminobenzoyl-S212AEDNSPQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.2
o-aminobenzoyl-S513SDSGSQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
0.02
o-aminobenzoyl-T294HLDTKKQ-N-(2,4-dinitrophenyl)ethylene diamine
Homo sapiens
-
recombinant soluble enzyme, pH 5.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000869
chondroitin sulfate
-
-
0.000306
heparan sulfate
-
-
0.0000025
heparin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8.5
-
-
5 - 9
-
activity rapidly decreases at more basic pH values
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
associated on the surface of
Manually annotated by BRENDA team
-
osteoblast cell culture
Manually annotated by BRENDA team
-
isozymes dPHEX1-3
Manually annotated by BRENDA team
-
osteoblast cell culture
Manually annotated by BRENDA team
-
osteoblast cell culture
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isozymes dPHEX1 and dPHEX2
Manually annotated by BRENDA team
-
isozymes dPHEX3 and dPHEX2
Manually annotated by BRENDA team
additional information
-
enzyme is possibly an ectoenzyme, membrane-spanning region towards the N-terminus
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
95000
-
x * 95000, recombinant soluble, deglycosylated mutant, SDS-PAGE, x * 100000, recombinant soluble mutant, SDS-PAGE, x * 105000, native wild-type, SDS-PAGE
100000
105000
-
x * 95000, recombinant soluble, deglycosylated mutant, SDS-PAGE, x * 100000, recombinant soluble mutant, SDS-PAGE, x * 105000, native wild-type, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
the 29 kDa hemopexin domain of MMP-2 is cleaved of its C-terminus during processing of MMP-2, as well as a 80 amino acid sequence of the N-terminus
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
PHEX is protected by glycosaminoglycans against thermal denaturation. The presence of heparin stabilizes the overall PHEX tertiary structure against denaturation at high temperature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NaCl required for stability of the purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant from SF9 insect cells as His-tagged protein
-
recombinant soluble enzyme form from porcine kidney cells
-
recombinant soluble secreted mutant enzyme forms
-
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
-
dPHEX1-3, localization on the X-chromosome, genomic organization, DNA and amino acid sequence determination and analysis, expression profiles of the isozymes in embryonic developmental stages, expression of FLAG-tagged isozymes in S2 cells
-
expression as V5-epitope tagged enzyme in an in vitro rabbit reticulocyte lysate system
-
expression in CHO cells
-
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
-
functional in vitro expression by a reticulocyte lysate expression system, protein expressed in COS-7 cells is not functional
-
gene PEX mapps to chromosome region Xp22.1
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gene PHEX, localization on the X chromosome, overexpression under control of the human beta-actin promoter in transgenic mice in all tissue except for pancreas, ovary and brain
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PHEX gene, expression of wild-type and mutants in LLC-PK1 porcine kidney cells
-
PHEX gene, i.e. phosphate-regulating gene with homologies to endopeptidase on the X-chromosome, expression as soluble secreted mutant form secPHEX, lacking residues 1-45, in LLC-PK1 porcine kidney cells, deletion mutant enzyme shows catalytic properties similar to the wild-type enzyme
-
the gene is localized on the X chromosome
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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medicine