Information on EC 2.4.2.7 - adenine phosphoribosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.4.2.7
-
RECOMMENDED NAME
GeneOntology No.
adenine phosphoribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenine and adenosine salvage I
-
-
adenine and adenosine salvage II
-
-
adenine salvage
-
-
aminomethylphosphonate degradation
-
-
glyphosate degradation III
-
-
purine metabolism
-
-
Purine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
AMP:diphosphate phospho-D-ribosyltransferase
5-Amino-4-imidazolecarboxamide can replace adenine.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-80-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Green Wave
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
APT2; subsp. indica, wild-type and TGMS mutant line Annong S-1 line, gene APT2
SwissProt
Manually annotated by BRENDA team
maintained in NMRI mice
-
-
Manually annotated by BRENDA team
cv. Danshaku
SwissProt
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
inbred line Qi319
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine ribotide + diphosphate
show the reaction diagram
4-amino-5-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
4-amino-5-imidazolecarboxamide ribotide + diphosphate
show the reaction diagram
-
-
-
-
?
4-aminopyrazolo-(3,4-d)-pyrimidine + 5-phospho-alpha-D-ribose 1-diphosphate
4-aminopyrazolo-(3,4-d)-pyrimidine ribotide + diphosphate
show the reaction diagram
-
-
-
-
?
4-carbamoylimidazolium 5-olate + 5-phospho-alpha-D-ribose 1-diphosphate
4-carbamoylimidazolium 5-olate 5'-phosphate + diphosphate
show the reaction diagram
-
low activity
-
-
?
5-amino-4-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
5-amino-4-imidazolecarboxamide ribotide + diphosphate
show the reaction diagram
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
show the reaction diagram
6-amino-2-hydroxypurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-amino-2-hydroxypurine ribotide + diphosphate
show the reaction diagram
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
show the reaction diagram
-
-
-
-
?
6-methylpurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-methylpurine ribotide + diphosphate
show the reaction diagram
-
-
-
-
?
8-azaadenine + 5-phospho-alpha-D-ribose 1-diphosphate
8-azaadenosine 5'-phosphate + diphosphate
show the reaction diagram
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
show the reaction diagram
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
benzyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
benzyladenosine 5'-phosphate + diphosphate
show the reaction diagram
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
show the reaction diagram
-
at about 5.7% of the conversion rate for adenine
-
-
?
isopentenyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
isopentenyladenosine 5'-phosphate + diphosphate
show the reaction diagram
N6-furfuryladenine + 5-phospho-alpha-D-ribose 1-diphosphate
N6-furfuryladenosine 5'-phosphate + diphosphate
show the reaction diagram
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
show the reaction diagram
-
-
-
-
?
zeatin + 5-phospho-alpha-D-ribose 1-diphosphate
zeatin ribotide + diphosphate
show the reaction diagram
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
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
show the reaction diagram
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
-
Ni2+
-
-
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-Diaminopurine
-
competitive
4-aminopteridine
-
-
4-aminopyrido(2,3-d)pyrimidine
-
-
4-aminopyrolo(2,3-d)pyrimidine
-
-
6-Mercaptopurine
-
competitive
adenine
alpha-D-5-phosphoribose 1-diphosphate
-
substrate inhibition
benzyladenine
-
competitive
citrate
-
-
Cu2+
-
strong
diphosphate
EDTA
-
reversible by 2-mercaptoethanol and excess Mg2+
formycin AMP
-
competitive against adenine and diphosphate
-
GDP
-
slightly at 5 mM
GTP
-
slightly at 5 mM
Guanine
hypoxanthine
-
weak
immucillin AB
-
does not bind at the active site
iodoacetate
-
-
isodutaduprine
-
alkaloid from Almeidea rubra, 21.6% inhibition at 0.0356 mM of the recombinant enzyme
isokokusagine
-
alkaloid from Almeidea rubra, 44.6% inhibition at 0.0412 mM of the recombinant enzyme
isopentenyladenine
-
-
isoskimmianine
-
alkaloid from Almeidea rubra, 39.1% inhibition at 0.0386 mM of the recombinant enzyme
N-ethylmaleimide
nucleotides
-
p-chloromercuribenzoate
p-hydroxymercuribenzoate
SO42-
succinate
-
-
sulfhydryl reagents
trinitrophenyl-AMP
-
-
xanthine
-
weak
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
nucleotides
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.89
2,6-Diaminopurine
-
-
0.036
4-aminopyrazolo-(3,4-d)pyrimidine
-
-
1
5-aminoimidazole-4-carboxamide
-
-
0.0007 - 0.29
5-phospho-alpha-D-ribose 1-diphosphate
1.4
6-Amino-2-hydroxypurine
-
-
3.7
6-Methylpurine
-
-
0.24
8-Azaadenine
-
-
0.0004 - 0.14
adenine
0.00523 - 0.087
AMP
0.015 - 2.4
benzyladenine
0.255 - 0.45
diphosphate
1.5
hypoxanthine
-
pH 7.4, temperature not specified in the publication
0.11 - 2.5
isopentenyladenine
0.3
Mg2+
-
-
0.2
Mn2+
-
-
0.13
N6-(DELTA2-isopentenyl)adenine
-
-
0.154
N6-benzyladenine
-
-
0.11
N6-furfuryladenine
-
-
0.076 - 1.8
zeatin
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0001 - 1000
5-phospho-alpha-D-ribose 1-diphosphate
2.8 - 9.33
adenine
0.0095
AMP
11.3
diphosphate
Leishmania donovani
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1090
adenine
Leishmania donovani
-
pH 7.4, temperature not specified in the publication
144
0.00035
hypoxanthine
Leishmania donovani
-
pH 7.4, temperature not specified in the publication
211
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
2,6-Diaminopurine
-
-
0.53
4-aminopteridine
-
-
0.017
4-aminopyrido(2,3-d)pyrimidine
-
-
0.95
4-aminopyrolo(2,3-d)pyrimidine
-
-
1.96
5-phosphoribose 1-diphosphate
-
at 37C
0.011
adenine
pH 7.5, 60C
0.019 - 3.2
ADP
0.018 - 23.5
AMP
0.344 - 0.574
ATP
0.002
Cu2+
-
-
0.51 - 1.79
diphosphate
0.059 - 0.062
formycin AMP
-
0.2
Guanine
-
above
0.8
hypoxanthine
-
above
0.0002
immucillin AB
-
-
0.7
Mercaptopurine
-
-
5.4
Mg2+
pH and temperature not specified in the publication
0.8
xanthine
-
above
0.005
Zn2+
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000004
-
-
0.0004 - 0.0006
-
wild-type erythrocytes
0.00086
-
HPRT F199C mutant erythrocytes
0.0073
-
wild-type MN9D cells
0.156
-
purified enzyme
1.1
-
purified enzyme
2.2
-
purified enzyme
9.58
-
purified enzyme
14
-
purified enzyme
14.2
-
purified enzyme
15.14
-
purified enzyme
20.6
-
purified enzyme
21.8
-
purified enzyme
300
-
purified enzyme, pH 8.8, 37C
1430
-
crude cell extract, pH 7.5, temperature not specified in the publication
2050
-
crude cell extract, pH 7.5, temperature not specified in the publication
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
the enzyme displays optima both at pH values around 4 and at pH 7-8
4.5
-
the enzyme shows two pH optima, i.e., around 8 and 4.5. The activity of APRTase is considerably higher at pH 8 than pH 4.5, when assayed at 35C, while the two activity peaks seems more equal, when assayed at 60C
7 - 8
the enzyme displays optima both at pH values around 4 and at pH 7-8
7.4 - 7.5
APT2 and 3, 37C; APT2 and 3, 37C
7.5 - 8.5
-
the enzyme shows two pH optima, i.e., around 8 and 4.5. The activity of APRTase is considerably higher at pH 8 than pH 4.5, when assayed at 35C, while the two activity peaks seems more equal, when assayed at 60C
8 - 9
-
-
8
-
around, broad, Escherichia coli
8.4 - 9.1
-
-
8.5
-
two zones of pH-optima at pH 7.5 and 8.5
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 9.5
the enzyme is active over a wide pH range
5.5 - 10
-
active over a broad range increasing progressively in activity from pH 5.5-10
7 - 9
-
active over a broad range increasing progressively in activity from pH 7.0-9.0
7.4 - 9.5
-
broad maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
recombinant enzyme, assay at
additional information
-
at 0C in the absence of Mg2+ but in presence of substrates enzyme catalyzes a rapid and limited synthesis of AMP
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
isoelectric focusing
6.53
calculated from sequence from cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
fetal
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
cell line derived from FM3A
Manually annotated by BRENDA team
-
mammary carcinoma cell line
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
-
gel filtration
22000
-
sucrose density gradient sedimentation
22760
calculated from sequence from cDNA
23000
-
gel filtration
25000
-
gel filtration
28000
-
gel filtration
38200
-
sedimentation equilibrium centrifugation
40000
-
gel filtration
45000
-
gel filtration
46000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
3 * 11100, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme, 10 mg/ml, in complex with 9-deazaadenine and sulfate or Mg-phosphoribosyldiphosphate, 50 mM Hepes, pH 6.0, 8 mM MgCl2, 1 mM DTT, 1:2 molar ratio of 9-deazaadenine and iminoribitol, 1 mM sodium diphosphate, after 45 min incubation preparation of crystallization drops, crystals are obtained from mother liquid 0.1 M sodium acetate, pH 4.6, 24% polyethylene glycol 4000, 0.2 M ammonium sulfate, 0.05 M urea, 18C, X-ray diffraction structure analysis, hydrogen bond network in the complexes
-
hanging drop vapour diffusion method, with 15% (v/v) glycerol, 25.5% (w/v) PEG 4000, 0.17 M sodium acetate, and 0.085 M Tris-HCl, pH 8.5
-
recombinant human APRT is crystallized in complex with adenosine 5'-monophosphate, hanging-drop vapour-diffusion method
-
vapour diffusion method, hanging drops from solution: 10 mg/ml purified apo-enzyme in 10 mM MES, pH 6.0, 1 mM dithiothreitol, 5 mM MgCl2, 4C, reservoir solution: 7-11% polyethylene glycol 5000 monomethyl ether, 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 4.9, 10 mM MgCl2, 1.2-1.6 M ammonium sulfate, for AMP- or adenine-bound crystals addition of 10 mM AMP or 5 mM adenine in the reservoir solution, structure analysis
enzyme in complex with adenosine-5'-monophosphate and a phosphate ion, crystallization at 4C by hanging-drop vapor-diffusion method
-
mixing of protein solution 13-15 mg/ml with an equal volume of mother liquid 0.1 M Hepes, pH 7.5, 1.5 M lithium sulfate, then equilibration against mother liquid at 18C, crystals appear after 3 days, X-ray diffraction structure analysis, also crystallization of the enzyme in presence of diphosphate, Mg2+ or inhibitor immucillin, which do not bind at the active site
-
four crystal structures: (1) a structure (the enzyme/Pi complex) refined at 2.4 A with inorganic phosphate or sulfate bound in the 5-phosphoribosyl binding pocket, (2) an adenine bound structure (the enzyme/adenine complex) refined at 2.4 A, which shows adenine together with phosphates both at the 5'-phosphoryl and PPi positions of the presumed PRPP binding site, (3) an AMP bound structure (the enzyme/AMP complex) refined at 2.4 A, and (4) an ADP bound structure (the enzyme/ADP complex), refined at 2.8 A containing the inhibitor ADP bound like AMP with both the alpha- and beta-phosphates occupying the 5'-phosphoribosyl binding site. No crystals of the enzyme in complex with 5-phosphoribosyl-alpha-1-pyrophosphate are obtained, likely because the enzyme catalyzes a slow breakdown of 5-phosphoribosyl-alpha-1-pyrophosphate to ribose 5-phosphate and PPi. The crystal structure suggests that the enzyme evolves from a 6-oxopurine phosphoribosyltransferase. The individual subunit adopts an overall structure that resembles a 6-oxopurine phosphoribosyltransferase (PRTase) more than known adenine phosphoribosyltransferases implying that adenine phosphoribosyltransferase functionality in Crenarchaeotae has its evolutionary origin in this family of 6-oxopurine phosphoribosyltransferases. The N-terminal two-thirds of the polypeptide chain folds as a traditional type I PRTase with a five-stranded beta-sheet surrounded by helices. The C-terminal third adopts an unusual three-helix bundle structure that together with the nucleobase-binding loop undergoes a conformational change upon binding of adenine and phosphate resulting in a slight contraction of the active site
purified recombinant native and selenomethionine-labeled enzymes, sitting drop vapour diffusion method, 0.001 ml of 20 mg/ml native protein in 20 mM Tris-HCl, 50 mM NaCl, pH 8.0, is mixed with an equal volume of reservoir solution containing 100 mM MES, pH 5.5, 100 mM calcium acetate, 3% w/v PEG 10000, and 3% v/v MeOH, 1 week, for the selenomethionine-labeled protein 40 mM calcium acetate, 1.5% w/v PEG 10000, and 3% v/v MeOH is used at a protein concentration of 29.4 mg/ml, X-ray diffraction structure determination and analysis at 1.9-2.6 A resolution, multiple wavelength anomalous dispersion method, asymmetric unit of two pairs of identical dimers, each related by noncrystallographic two-fold symmetry, a fifth monomer forms a similar dimer across a crystallographic two-fold axis, modeling
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
in absence of Mg2+ and donor substrate, loss of 50% activity after 18 min
37
-
in absence of Mg2+ and donor substrate, loss of 97% activity after 10 min
58
-
heat denaturation, 35% ammonium sulfate protects
70
-
complete inactivation of Propositus (HPRT-) after 20 min, complete inactivation of control(HPRT+) after 10 min
80
-
complete inactivation of Propositus (HPRT-) after 13 min, complete inactivation of control(HPRT+) after 7 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
5-phospho-alpha-D-ribose 1-diphosphate stabilizes Mycoplasma mycoides enzyme markedly
-
ammonium sulfate, 1 M, partially protects against inactivation during storage
-
bovine serum albumin or adenine stabilizes Mycoplasma mycoides enzyme slightly
-
dialysis against 20 mM Tris-HCl, pH 7.5, 20 mM (NH4)2SO4 + 5 mM 2-mercaptoethanol inactivates
-
dithiothreitol, 10 mM, or dimethylsulfoxide, 5%, or 5-phospho-alpha-D-ribose 1-diphosphate, 1 mM, protects against inactivation during storage
-
freezing and thawing have little effect on E. coli enzyme, but inactivate Mycoplasma mycoides enzyme
inactivation by isoelectric focusing
-
instability after calcium phosphate gel treatment
-
Mg2+ stabilizes
-
unstable in absence of Mg2+ and glycerol, loss 0f 70% activity during gel filtration
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, stable for months
-
-20C, purified enzyme, 2-3 weeks, considerable loss of activity
-
-20C, purified enzyme, 6 mM 5-phospho-alpha-D-ribose 1-diphosphate, 2 mM MgCl2, stable for at least a month
-
-70C, 50 mM Tris-HCl, pH 7.4, 5 mM MgCl2, 10 mM KCl, 10% glycerol, stable
-
-70C, purified enzyme, 5 mM MgCl2, 0.1 mM 5-phospho-alpha-D-ribose 1-diphosphate, stable for upt to 2 months
-
-70C, purified enzyme, at least 6 months
-
-79C, purified enzyme, 0.1 mg/ml protein, 0.1 M potassium phosphate buffer, pH 7, stable for several months
-
-80C, stable for at least 3 weeks
-
2-4C, purified enzyme in the ampholine gradient solution, half-life of 2-4 weeks, dilution inactivates
-
unstable at 4C or at -20C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 isoforms recombinant from Escherichia coli as His-tagged proteins; 3 isoforms recombinant from Escherichia coli as His-tagged proteins; 3 isoforms recombinant from Escherichia coli as His-tagged proteins
hydroxyapathite column chromatography
-
Ni affinity column chromatography; Ni affinity column chromatography; Ni affinity column chromatography; Ni affinity column chromatography
recombinant from Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant His-tagged wild-type and mutants from Escherichia coli
-
recombinant wild-type enzyme from Escherichia coli strain BL21(DE3) and recombinant selenomethionine-labeled enzyme from Escherichia coli strain B834 by two steps of anion exchange chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and DNA sequence determination, expression in Escherichia coli BL21 cells as C-terminally His-tagged protein
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
expressed in MN-9D cells
-
expression analysis after wounding
expression in Escherichia coli
expression of wild-type and mutants as His-tagged proteins in Escherichia coli B25 cells
-
expression of wild-type enzyme in Escherichia coli strain BL21(DE3) and of the selenomethionine-labeled enzyme in Escherichia coli strain B834
-
gene APT2, DNA and amino acid sequence determination and analysis, expression pattern analysis, recombinant expression in Arabidopsis thaliana plants using the Agrobacterium tumefaciens transfection system
genotyping, genetic screening for mutant genes APRT*Q0 and APRT*J in two families
-
overexpression of the 3 isoforms in Escherichia coli Bl21(DE3)pLysS as His-tagged proteins, the majority of the recombiannt enzyme is in the soluble fraction; overexpression of the 3 isoforms in Escherichia coli Bl21(DE3)pLysS as His-tagged proteins, the majority of the recombiannt enzyme is in the soluble fraction; overexpression of the 3 isoforms in Escherichia coli Bl21(DE3)pLysS as His-tagged proteins, the majority of the recombiannt enzyme is in the soluble fraction
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mutational HPRT deficiency leads to increased APRT expression and activity in MN9D cells, microarray analysis of HPRT-deficient MN9D cells, phenotype with increases in APRT and mRNAs for engrailed 1 and 2, En1 and En2, transcription factors, overview
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G168E
the mutant of isoform APT1 shows reduced activity with zeatin (about 14%) and adenine (about 28%), respectively, compared to the wild type enzyme
G195D
the mutant of isoform APT1 shows nearly no activity with zeatin and adenine, respectively, compared to the wild type enzyme
G196R
the mutant of isoform APT1 shows nearly no activity with zeatin and adenine, respectively, compared to the wild type enzyme
L96F
the mutant of isoform APT1 shows reduced activity with zeatin (about 11%) and adenine (about 8%), respectively, compared to the wild type enzyme
P85T
the mutant of isoform APT1 shows nearly no activity with zeatin and adenine, respectively, compared to the wild type enzyme
R149K
the mutant of isoform APT1 shows no activity with zeatin and adenine, respectively, compared to the wild type enzyme
F25W
-
site-directed mutagenesis, tryptophan at the adenine binding site, kinetic constants similar to the wild-type
G133D
-
mutation in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis, Japanese patient
L110P
-
mutation is associated with renal dysfunction
M136T
-
10.3% loss of activity
R67Q
-
mutation in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis, Japanese patient
V84W
-
mutation in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis, Japanese patient
E106L
-
site-directed mutagenesis, decreased turnover, increased Km value for adenine and decreased Km value for 5-phosphoribose 1-phosphate compared to the wild-type
E106Q
-
site-directed mutagenesis, decreased turnover and Km value for 5-phosphoribose 1-phosphate compared to the wild-type
G108A
-
site-directed mutagenesis, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
G108H
-
site-directed mutagenesis, decreased turnover, slightly increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
K90A
-
site-directed mutagenesis, decreased turnover compared to the wild-type
K93A
-
site-directed mutagenesis, decreased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
R69A
-
site-directed mutagenesis, decreased turnover, increased Km value for adenine compared to the wild-type
R89A
-
site-directed mutagenesis, decreased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
Y103F
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site-directed mutagenesis, increased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
Y107D
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site-directed mutagenesis, decreased turnover, increased Km value for adenine compared to the wild-type
Y107F
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site-directed mutagenesis, decreased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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the enzyme is a target for antileishmanicidal drug development
medicine
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expression of both Escherichia coli purine nucleoside phosphorylase and human adenine phosphoribosyl transferase in tumor cell lines. Purine nucleoside phosphorylase cleaves purine nucleoside analogs to generate toxic adenine analogs, which are activated by adenine phosphoribosyl transferase to metabolites that inhibit RNA and protein synthesis. In vivo studies with 6-methylpurine-2'-deoxyriboside, 2-fluoro-2'-deoxyadenosine or 9-beta-D-arabinofuranosyl-2-fluoroadenine 5'-phosphate indicate that increased adenine phosphoribosyl transferase in human tumor cells coexpressing Escherichia coli purine nucleoside phosphorylase does not enhance either the activation or the anti-tumor activity of any of the three prodrugs. Expression of excess adenine phosphoribosyl transferase in bystander cells improves the activity of 6-methylpurine-2'-deoxyriboside, but diminishes the activity of 9-beta-D-arabinofuranosyl-2-fluoroadenine 5'-phosphate. In vitro studies indicate that increasing the expression of adenine phosphoribosyl in the cells does not significantly increase the activation of 6-methylpurine
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