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Enzyme Nomenclature
Information on EC 2.4.2.8 - hypoxanthine phosphoribosyltransferase
for references in articles please use BRENDA:EC2.4.2.8
Word Map on EC 2.4.2.8
- 2.4.2.8
- hamster
- lymphocyte
- lesch-nyhan
-
genotoxic
- 6-thioguanine
-
carcinogen
-
salvage
-
x-linked
- ovary
- erythrocyte
- nucleoside
- gapdh
-
genorm
-
clonal
- t-cells
-
housekeeping
- thymidine
- t-lymphocytes
- lymphoblast
-
uric
-
lymphoblastoid
-
normfinder
-
micronuclei
-
chromatid
-
benzoapyrene
-
transversions
-
radiation-induced
-
x-chromosome
- hyperuricemia
-
bestkeeper
- allopurinol
- methanesulfonate
- comet
-
clastogenic
-
phosphoribosylpyrophosphate
- aminopterin
-
x-ray-induced
- lns
-
repair-deficient
-
32p-postlabeling
-
sister-chromatid
-
gouty
-
non-transcribed
-
n-ethyl-n-nitrosourea
-
mutable
-
micronucleated
- 1,3-butadiene
- o6-methylguanine
- medicine
-
x-inactivation
- biotechnology
- pharmacology
- analysis
-
mutability
- drug development
- synthesis
- molecular biology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.4.2.8
-
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RECOMMENDED NAME
GeneOntology No.
hypoxanthine phosphoribosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
guanine and 6-mercaptopurine can replace hypoxanthine
-
-
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
essential role of Ser95-Tyr96 dyade in catalysis
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
catalytic mechanism; kinetic mechanism
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
kinetic model; ordered bi-bi mechanism; Thr47 binds diphosphate
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
ordered bi-bi mechanism
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
active site structure; catalytic mechanism
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
catalytic mechanism; residues I99-L121 form the catalytic loop
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
active site structure; during catalysis a long flexible loop closes over the active site, functional role
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
active site structure; catalytic mechanism
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
active site structure
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
residue F36 is responsible for substrate specificity, structure-function relationship
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
residue L44 is responsible for substrate specificity, structure-function relationship
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
reaction mechanism, the flexible loop II, comprising 12 amino acid residues, closes over the active site of the enzyme as it approaches the transition state, the loop is required for full activity, structure-function relationship for the conserved residues
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
reaction mechanism, function and influence of invariant active site loop I residues on enzyme efficiency in forward and reverse reaction
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
ordered bi bi reaction mechanism, formation of dead-end complexes with purine substrates and diphosphate
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
ordered bi bi kinetic mechanism with 5-phospho-alpha-D-ribose 1-diphosphate binding first followed by the purine base
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
substrate binding structure and mechanism, a non-proline cis-peptide may be essential for activity
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
sequential mechanism with 5-phospho-alpha-D-ribose 1-diphosphate binding first, active site helix comprising D137-D153 with key active site residues K68, D137, and K165, substrate binding sites and structures, overview
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
reaction mechanism
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
ordered reaction mechanism. The substrates bind in a functionally ordered fashion, with 5-phospho-alpha-D-ribose 1-diphosphate binding first in the forward direction and IMP or GMP first in the reverse reaction, transition state structure and 5'-phosphate binding structure on HGPRT, overview
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
ordered reaction mechanism, 5-phospho-alpha-D-ribose 1-diphosphate-Mg2+ binds first followed by the purine base. After the covalent reaction, diphosphate then dissociates from the complex and the nucleoside monophosphate is released in the rate-limiting step
-
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
binding structure involving residue K68 at the AB-dimer interface and residues V96 and D97 of the opposing subunit, overview. Residues E133 and D137 block the binding of 5-phospho-alpha-D-ribose 1-diphosphate, mechanism, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
pentosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
IMP:diphosphate phospho-D-ribosyltransferase
Guanine and 6-mercaptopurine can replace hypoxanthine.
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CAS REGISTRY NUMBER
COMMENTARY
9016-12-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes; strain LT-2
-
-
; phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes
-
-
-
638395, 638396, 638399, 638405, 638409, 638414, 638419, 638421, 662654, 662878, 672965, 673370, 675050, 676249, 677077, 703955, 705826, 705998, 706843, 721773, 723304, 735767
-
-
construction of 4 chimeric enzymes with segments of human and Plasmodium falciparum enzymes
-
-
construction of 4 chimeric enzymes with segments of human and Plasmodium falciparum enzymes
-
-
single gene locus, two alternative-splicing-derived isozymes HXGPRT-I and HXGPRT-II
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
a deficiency in HPRT activity leads to overproduction of uric acid, hyperuricemia, with gouty arthritis, nephrolithiasis, and mild neurologic symptoms. According to the degree of enzymatic deficiency, a large spectrum of neurologic features can also be observed, ranging from mild or no neurologic involvement to complete Lesch-Nyhan disease
malfunction
-
HPRT deficiency influences early developmental processes controlling the dopaminergic phenotype, and is involved in Lesch-Nyhan disease pathogenesis
malfunction
-
complete deficiency of hypoxanthine-guanine phosphoribosyltransferase causes the Lesch-Nyhan disease, a genetic disorder associated with motor and psychiatric disturbance and self-injurious behaviour, the role of serotonin receptor 2C, HTR2C, might be involved, overview
malfunction
-
mutations in the gene encoding the purine biosynthetic enzyme HPRT cause the resulting intractable and largely untreatable neurological impairment of Lesch-Nyhan disease. The disorder is associated with a defect in basal ganglia DA pathways, phenotype mechanisms analysis in human embryonic carcinoma neurogenesis model, overview
malfunction
-
enzyme knockdown causes a marked switch from neuronal to glial gene expression and dysregulates expression of Sox2 and its regulator, genes vital for stem cell pluripotency and for the neuronal/glial cell fate decision. In addition, enzyme deficiency dysregulates many cellular functions controlling cell cycle and proliferation mechanisms, RNA metabolism, DNA replication and repair, replication stress, lysosome function, membrane trafficking, signaling pathway for platelet activation multiple neurotransmission systems and sphingolipid, sulfur and glycan metabolism
metabolism
-
comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
metabolism
-
comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
physiological function
-
HPRT is a housekeeping enzyme responsible for recycling purines, it regulates early developmental programming of dopamine neurons
physiological function
-
the purine salvage enzyme HGXPRT is essential for purine nucleotide and hence nucleic acid synthesis in the malaria parasite
physiological function
-
the enzyme is involved in the specification and development of neurons, including dopaminergic neurons, as well as in the regulation of dopaminergic transcription factors, overview
physiological function
-
the enzyme enables the reutilization of purine base adenine converting it to mononucleotide AMP, substrate for the synthesis of high-energy nucleotides
physiological function
-
the enzyme enables the reutilization of purine base adenine converting it to mononucleotide AMP, substrate for the synthesis of high-energy nucleotides
physiological function
-
treatment of cells with guanosine and GMP results in statistically significant decreases in cell growth after 48 h and 72 h in the melanoma cell line C32 and in the U-87 glioma cell line. Presence of hypoxanthine blocks the antiproliferative effects. Hypoxanthine phosphoribosyltransferase-negative cell line C32-TG cells completely has lost the inhibitory response to guanine treatment. Hypoxanthine phosphoribosyltransferase silencing by siRNA is able to partially block the guanine-induced antiproliferative effects in U-87 glioma cell lines
physiological function
-
production of enzyme-deficient human Coxsackievirus-induced pluripotent stem cells and human HUES11 embryonic stem cells using shRNA. Both cells show >99% enzyme knock-down and demonstrate markedly decreased expression of the purinergic P2Y1 receptor mRNA. In Coxsackievirus-induced cells, P2Y1 mRNA and protein down-regulation by hypoxanthine phosphoribosyltransferase knockdown is refractory to activation by the P2Y1 receptor agonist ATP and shows aberrant purinergic signaling, as reflected by marked deficiency of the transcription factor pCREB and constitutive activation of the MAP kinases phospho-ERK1/2. Moreover, hypoxanthine phosphoribosyltransferase-knockdown Coxsackievirus-induced cells also demonstrate marked reduction of phosphorylated beta-catenin
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2-amino-6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
2-hydroxy-6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2-hydroxy-6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
3-oxo-4-(5-O-phosphono-beta-D-ribofuranosyl)-3,4-dihydropyrazine-2-carboxamide + diphosphate
-
T-1105, poor substrate
-
-
?
3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
T-1105, poor substrate
-
-
?
6-fluoro-3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
6-fluoro-3-oxo-4-(5-O-phosphono-beta-D-ribofuranosyl)-3,4-dihydropyrazine-2-carboxamide + diphosphate
-
T-705, poor substrate
-
-
?
6-fluoro-3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
T-705, poor substrate
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-thioinosine monophosphate + diphosphate
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
thioinosinic monophosphate + diphosphate
-
a thiopurine antimetabolite
a therapeutically active metabolite
-
-
6-thioguanine + 5-phospho-alpha-D-ribose 1-diphosphate
6-thio-GMP + diphosphate
-
-
-
-
?
8-azahypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
8-aza-IMP + diphosphate
-
-
-
-
?
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
allopurinol ribonucleoside 5'-monophosphate + diphosphate
XMP + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
allopurinol ribonucleoside 5'-monophosphate + diphosphate
-
low activity
-
?
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
allopurinol ribonucleoside 5'-monophosphate + diphosphate
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
binds hypoxanthine 67-times less effectively than guanine and 4-times less effectively than xanthine
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
absolutely specific for guanine
diphosphate binds at Thr70, diphosphate-binding loop sequence: LTGA
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
guanine is utilized more rapidly than hypoxanthine
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
salvage synthesis
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
wild-type enzyme, no activity with mutant F36L
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
wild-type and chimeric mutant enzyme
modeling of GMP binding to the chimeric enzyme
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
wild-type and chimeric mutant enzyme
modeling of GMP binding to the chimeric enzyme
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
hypoxanthine and guanine preferred substrates
-
-
ir
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
equilibrium lies far in direction of IMP formation
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
2 assay methods
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
binding mechanism and structure of IMP occupying the diphosphate site, overview
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
hypoxanthine is the preferred substrate
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
unlike the hypoxanthine-guanine phosphoribosyltransferase from other sources this enzyme binds hypoxanthine 67-times less effectively than guanine and 4-times less effectively than xanthine
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
binds hypoxanthine 67-times less effectively than guanine and 4-times less effectively than xanthine
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
no activity with hypoxanthine
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
equilibrium lies far in direction of IMP formation
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
salvage synthesis
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
wild-type enzyme, no activity with mutant F36L
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
wild-type and chimeric mutant enzyme
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
the enzyme is involved in the purine salvage pathway
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
wild-type and chimeric mutant enzyme
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
hypoxanthine and guanine preferred substrates, continuous spectrophotometric enzyme assay, pH 7.5, 12 mM MgCl2, 40-70°C, 30 sec
Kd(diphosphate): 4.7 +/-0.1 mM, revealed by quenching of intrinsic fluorescence of the enzyme upon diphosphate-binding
-
ir
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
most effective substrate
diphosphate is bound by Thr47
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
wild-type and chimeric mutant enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
wild-type and chimeric mutant enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
mutant F36L, no activity with the wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
low activity
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
-
-
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
-
-
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
recombinant chimeric mutant DS1
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
wild-type human enzyme does not accept xanthine as substrate, mutant F36L does catalyze the conversion of xanthine to XMP with a kcat much lower than those of hypoxanthine and guanine
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
recombinant chimeric mutant DS1
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
the enzyme also performs the reaction of xanthine phosphoribosyltransferase, EC 2.4.2.22
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
low catalytic efficiency (kcat/KM), xanthine is not preferred but a usable substrate
-
-
ir
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
-
-
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
poor substrate
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
additional information
?
-
-
no substrates: 5-formamido-4-imidazolecarboxamide, uric acid, 8-azaguanine, 2,6-diaminopurine, orotic acid, phosphate
-
-
-
additional information
?
-
-
the conformation of the flexible loop, containing a 3-10 helix and a unique double serine repeat, is important for substrate binding and activation of the enzyme
-
-
-
additional information
?
-
-
no incorporation of xanthine in vivo
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
-
dynamic and conformational properties of purified enzyme alone, in complex with GMP and Mg2+, and in equilibration mixture of enzyme with IMP, Mg2+/diphosphate and hypoxanthine, Mg2+/5-phosphoribosyl 1-diphosphate, and in transition-state analogue complex of enzyme, immucillin-GP and Mg2+/diphosphate
-
-
-
additional information
?
-
-
a mentally retarded child and its asymptomatic uncle have a partial enzyme deficiency, homozygous, while mother and grandmother are heterozygous and not enzyme-deficient
-
-
-
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
-
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
-
additional information
?
-
-
substrate binding induces conformational changes required for catalysis
-
-
-
additional information
?
-
the flexibilty of loop IV can influence the substrate specificity
-
-
-
additional information
?
-
-
enzyme-deficiency is involved in development of gout
-
-
-
additional information
?
-
-
the enzyme is organized in a branched bi-enzyme system with xanthine oxidase, EC 1.17.3.2
-
-
-
additional information
?
-
-
substrate binding structure involving residue K68 at the AB-dimer interface and residues V96 and D97 of the opposing subunit, overview. Residues E133 and D137 block the binding of 5-phospho-alpha-D-ribose 1-diphosphate, mechanism, overview
-
-
-
additional information
?
-
-
the binding site for the 5'-phosphate is located at residues 132-141
-
-
-
additional information
?
-
-
The substrates bind in a functionally ordered fashion, with 5-phospho-alpha-D-ribose 1-diphosphate binding first in the forward direction and IMP or GMP first in the reverse reaction, transition state structure and 5'-phosphate binding structure on HGPRT, overview
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
-
the enzyme activity is regulated by stabilization and destabilization of the enzyme through release or binding of product and substrates, overview
-
-
-
additional information
?
-
-
the purified recombinant enzyme shows very low activity
-
-
-
additional information
?
-
-
the parasite depends on the human host purine salvage pathway enzyme hypoxanthine guanine xanthine phosphoribosyltransferase for survival, because it does not have a de novo pathway for synthesis of nucleotides on its own
-
-
-
additional information
?
-
-
the binding site for the 5'-phosphate is located at residues 132-141
-
-
-
additional information
?
-
-
no formation of PRPP and 6-oxopurine by pyrophosphorylysis due to disability of binding to nucleotides IMP, GMP, XMP at 40-70°C and substrate concentrations of up to 0.5 mM
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
the two isozymes exhibit similar substrate specificity, kinetic characteristics, and temporal expression patterns, overview
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
-
forward reaction: transfer of the phosphoribosyl group to N9 position of 6-oxopurines
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
formation of dead-end complexes with purine substrates and diphosphate
-
-
-
additional information
?
-
-
L67 side chain participates in hydrophobic interactions between dimer subunits important for the proper positioning of main chain atoms that influence enzyme chemistry and the binding of 5-phospho-alpha-D-ribose 1-diphosphate, diphosphate, and hypoxanthine, residue 69 needs to be small like Gly, which is found there, to avoid sterical interference with binding of 5-phospho-alpha-D-ribose 1-diphosphate and diphosphate as well as the positioning of a metal ion
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
XMP + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
P00492
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
Q5ZVC1
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
salvage synthesis
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
Q5ZVC1
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
P9WHQ9
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
P20035
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
Q8R7L0
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
salvage synthesis
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
Q5ZVC1
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
P9WHQ9
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
P20035
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
the enzyme is involved in the purine salvage pathway
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
-
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
P00492
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
Q5ZVC1
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
P20035
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
P00492
mutant F36L, no activity with the wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
low activity
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
additional information
?
-
-
no incorporation of xanthine in vivo
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
-
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
-
additional information
?
-
-
enzyme-deficiency is involved in development of gout
-
-
-
additional information
?
-
-
the enzyme is organized in a branched bi-enzyme system with xanthine oxidase, EC 1.17.3.2
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
Q9NJI5
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
Q9NJI5
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
-
the enzyme activity is regulated by stabilization and destabilization of the enzyme through release or binding of product and substrates, overview
-
-
-
additional information
?
-
-
the parasite depends on the human host purine salvage pathway enzyme hypoxanthine guanine xanthine phosphoribosyltransferase for survival, because it does not have a de novo pathway for synthesis of nucleotides on its own
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
-
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
required for binding of 5-phospho-alpha-D-ribose 1-diphosphate, binding via side chains of Glu101 and Asp102 and water molecules in the apoenzyme, binding site structure
Mg2+
-
absolute requirement for Mg2+ or Mn2+
Mn2+
-
absolute requirement for Mg2+ or Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
(3-[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]propyl)phosphonic acid
-
competitive. 466fold lower affinity for human enzyme. Treatment of cultured parasites with the bis-pavalate of the inhibitor as a prodrug inhbits growth with an IC50 of 45 microM
4-(2-methyl-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
78.12% inhibition at 0.25 mg/ml
4-(2-methyl-6,8-dibromo-4-oxo-(3H)quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.07% inhibition at 0.25 mg/ml
4-(2-methyl-6-bromo-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
77.06% inhibition at 0.25 mg/ml
4-(2-phenyl-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.42% inhibition at 0.25 mg/ml
4-(2-phenyl-6,8-dibromo-4-oxo-(3H)quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.71% inhibition at 0.25 mg/ml
4-(2-phenyl-6-bromo-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.55% inhibition at 0.25 mg/ml
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
diethyl dicarbonate
-
alkylation of Arg155, complete inactivation at pH 9.0, pH dependent
immucillin-G 5'-phosphate
-
active site contacts in the HGPRT/immucillin-G 5'-phosphate/diphosphate complex, overview
immucillin-H
-
transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics
Mg2+
-
inhibitory effects are noncompetitive against 5-phosphoribose 1-diphosphate
Phenylglyoxal
-
irreversible, complete inactivation, alkylation of Arg155, GMP protects, no alkylation of mutant R155K
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
Tetranitromethane
-
complete inactivation at pH 9.0, pH dependent, modifies Tyr96 in the active site
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
[(3S)-4-hydroxy-3-[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]butyl]phosphonic acid
-
competitive. 592fold lower affinity for human enzyme
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
(1S)-1-(9-deazaguanin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
-
-
(1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
-
-
(1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
-
-
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
-
-
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
-
-
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
; is toxic to cells and arrests cell growth
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
; is toxic to cells and arrests cell growth
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
-
-
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
-
-
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive against GMP; product inhibition
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive versus diphosphate and GMP or IMP
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
-
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
-
9-[2-(phosphonomethoxy)ethyl]guanine
-
; is toxic to cells and arrests cell growth
9-[2-(phosphonomethoxy)ethyl]guanine
-
; is toxic to cells and arrests cell growth
acyclic nucleoside phosphonates
-
analogues of the nucleotide reaction product, comprising a purine base joined by a linker to a phosphonate moiety, inhibitor design and potencies, overview. The inhibitors are selectivity for the enzyme of the human parasite Plasmodium falciparum, up to factor 58, compared to the human enzyme, overview
acyclic nucleoside phosphonates
-
analogues of the nucleotide reaction product, comprising a purine base joined by a linker to a phosphonate moiety, inhibitor design and potencies, overview. Selectivity for the parasite enzyme of up to 58 compared to the Homo sapiens enzyme, overview, design of potent and selective acyclic nucleoside phosphonates inhibitors of Plasmodium falciparum HGXPRT as antimalarial drug leads
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
diphosphate
-
competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, uncompetitive versus hypoxanthine or guanine
GMP
-
competitive against 5-phospho-alpha-D-ribose 1-diphosphate; product inhibition
GMP
-
0.3 mM, 50% inhibition of guanine phosphoribosyltransferase activity
GMP
-
competitive inhibitor with respect to guanine, xanthine, and 5-phospho-alpha-D-ribose 1-diphosphate
GMP
-
competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, noncompetitive versus guanine
guanine
-
0.06 mM, 50% inhibition of hypoxanthine phosphoribosyltransferase activity
hypoxanthine
-
0.16 mM, 50% inhibition of guanine phosphoribosyltransferase activity
immucillin-H 5'-phosphate
-
transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics
IMP
-
feedback inhibition, competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, binding mode
IMP
-
competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, noncompetitive versus hypoxanthine
nucleotides
-
all free 5'-nucleotides are inhibitory, 6-OH purine nucleotides are most inhibitory, while 6-NH2 purine only at high concentrations
-
nucleotides
-
all free 5'-nucleotides are inhibitory, 6-OH purine nucleotides are most inhibitory, while 6-NH2 purine only at high concentrations
-
Pb2+
-
inhibits the enzyme in erythrocytes about 20% at 0.0005 mM and about 12% at 0.0001 mM, and participates in hemolysis, the intensity of which negatively correlates with the activity of phosphoribosyltransferases, HPRT inhibition as one of the mechanisms of lead toxicity
Pb2+
-
moderately inhibits both the enzyme in erythrocytes even at very low concentrations, and participates in hemolysis, the intensity of which negatively correlates with the activity of phosphoribosyltransferases, HPRT inhibition as one of the mechanisms of lead toxicity
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
-
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
-
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
-
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
-
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
-
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
-
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
-
-
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
-
-
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
-
-
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
-
-
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
-
-
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
-
-
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
-
-
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
-
-
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
-
-
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
-
-
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
-
-
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
-
-
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
-
-
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
-
-
additional information
-
overview: inhibition constant of purines and purine analogs
-
additional information
-
cytotoxicity studies using human lung carcinoma A549 cells at 37°C. The binding site for the 5'-phosphate is located at residues 132-141. No inhibition by (R)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
additional information
-
no effect of iodoacetate, phenylglyoxal, p-chloromercuribenzoate, acetic anhydride, ethyl dimethylaminopropylcarbodiimide/ammonium acetate, and diisopropyl fluorophosphate
-
additional information
-
guanine phosphoribosyltransferase activity: IMP and AMP are not inhibitory at concentrations up to 0.6 mM, adenine and xanthine are not inhibitory at concentrations up to 0.5 mM. Adenine and xanthine do not inhibit hypoxanthine phosphoribosyltransferase activity
-
additional information
-
mechanism of product inhibition; no inhibition by ADP, ATP, dAMP, UMP, and UTP
-
additional information
the activity of HGXPRTase was unaffected by the triphosphates ATP, GTP, CTP or UTP
-
additional information
-
product inhibition study, the substrates/products protect the enzyme against digestion by trypsin, especially hypoxanthine with diphosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GMP
-
0.05 mM, at least 2fold stimulation, hypoxanthine phosphoribosyltransferase activity
IMP
-
0.2 mM, at least 2fold stimulation, hypoxanthine phosphoribosyltransferase activity
IMP
-
activation with IMP results primarily in an increase in kcat, which is 3-5fold in the case of hypoxanthine and xanthine phosphoribosylation and more than 10fold in the case of guanine phosphoribosylation
additional information
-
hypoxanthine phosphoribosyltransferase activity is unaffected by AMP
-
additional information
-
activation by substrate and product IMP, reversibly destabilizes the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant F36L, with xanthine
0.0044
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant F36K, with hypoxanthine
0.0065
5-phospho-alpha-D-ribose 1-diphosphate
with guanine as cosubstrate, at pH 7.5 and 25°C
0.011
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant F36G, with hypoxanthine
0.0141
5-phospho-alpha-D-ribose 1-diphosphate
with hypoxanthine as cosubstrate, at pH 7.5 and 25°C
0.027
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant F36L, with hypoxanthine
0.029
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant F36K, with guanine
0.03
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with hypoxanthine
0.031
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme, with hypoxanthine
0.032
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.032
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme, with guanine
0.035
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with hypoxanthine
0.041
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant F36L, with guanine
0.05
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant F36G, with guanine
0.053
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated enzyme, at pH 7.4 and 23°C
0.06
5-phospho-alpha-D-ribose 1-diphosphate
with guanine as cosubstrate, wild type enzyme, at pH 7.5 and 25°C
0.076
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with guanine
0.079
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with xanthine
0.083
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant mutant G69S
0.094
5-phospho-alpha-D-ribose 1-diphosphate
-
activated enzyme, with xanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.102
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant L44F, with hypoxanthine
0.104
5-phospho-alpha-D-ribose 1-diphosphate
with guanine as cosubstrate, mutant enzyme R76S, at pH 7.5 and 25°C
0.112
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 50°C, with guanine
0.116
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant L44F, with guanine
0.116
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, with guanine
0.119
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, with hypoxanthine
0.123
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 25°C, with hypoxanthine
0.125
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 25°C, with guanine
0.132
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant mutant L67M
0.133
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 12 mM MgCl2
0.138
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 50°C, with hypoxanthine
0.151
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant L44F, with xanthine
0.183
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated enzyme, with hypoxanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.201
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with guanine
0.256
5-phospho-alpha-D-ribose 1-diphosphate
-
activated enzyme, with hypoxanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.263
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated enzyme, with guanine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.275
5-phospho-alpha-D-ribose 1-diphosphate
-
activated enzyme, with guanine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.277
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated enzyme, with xanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.327
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 12 mM MgCl2, in presence of 0.05 mM IMP
0.36
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 25°C, recombinant enzyme, with guanine
0.546
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine
0.546
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine
0.972
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated enzyme, with hypoxanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
1.075
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 28°C, recombinant chimeric mutant enzyme, with substrate guanine
1.075
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 28°C, recombinant chimeric mutant enzyme, with substrate guanine
1.08
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated enzyme, at pH 7.4 and 23°C
1.084
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated enzyme, with xanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
1.548
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated enzyme, with guanine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
2.039
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 25°C, recombinant enzyme, with hypoxanthine
0.127
5-phosphoribosyl 1-diphosphate
recombinant enzyme, with guanine
0.138
5-phosphoribosyl 1-diphosphate
recombinant enzyme, with hypoxanthine