Information on EC 1.7.1.7 - GMP reductase

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

EC NUMBER
COMMENTARY hide
1.7.1.7
-
RECOMMENDED NAME
GeneOntology No.
GMP reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
IMP + NH3 + NADP+ = GMP + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
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reductive deamination
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
purine metabolism
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-
Purine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
inosine-5'-phosphate:NADP+ oxidoreductase (aminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9029-32-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mutants containing mutations in the salvage pathway of purine synthesis
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
no activity in Haemophilus influenzae
-
-
-
Manually annotated by BRENDA team
no activity in Methanocaldococcus jannaschii
other name Methanococcus jannaschii
-
-
Manually annotated by BRENDA team
no activity in Mycoplasma genitalium
-
-
-
Manually annotated by BRENDA team
mRNA increases 30fold in brown adipose tissue within 6 h of cold exposure
SwissProt
Manually annotated by BRENDA team
cf. EC 1.1.1.205
UniProt
Manually annotated by BRENDA team
cf. EC 1.1.1.205
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
the enzyme activity establishes a link between guanosine metabolism and RHOGTPase-dependent melanoma cell invasion
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GMP + NADPH + H+
IMP + NH3 + NADP+
show the reaction diagram
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
show the reaction diagram
NADPH + H+ + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
enzyme nucleotide bindng analysis, nucleotide binding alters the quarternary structure of the enzyme, overview
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-
-
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
GMP + NADPH + H+
IMP + NH3 + NADP+
show the reaction diagram
NADPH + guanosine 5'-phosphate
NADP+ + inosine 5'-phosphate + NH3
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
highly activating, best monovalent cation, amino acid sequences of putative K+-binding sites of TbGMPR, overview
NH4Cl
highly activating
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-dXMP
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
0.66 mM, 33% inhibition after 30 min
6-Chloro-9-beta-D-ribofuranosylpurine 5'-phosphate
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0.01 mM, 80% inhibition after 40 min, 1 mM GMP protect
6-Chloropurine ribonucleotide
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6-Thio-GMP
6-thio-IMP
6-Thio-XMP
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8-Aza-7-deaza-XMP
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-
8-Aza-XMP
-
-
adenosine 2'-phosphate
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ADP
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2 mM, 85% inhibition
arabinosyl-XMP
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-
Fe2+
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10 mM, more than 90% inhibition
iodoacetamide
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progressive inhibition, 2 mM GMP protect
iodoacetate
-
progressive inhibition, 2 mM GMP protect
mizoribine 5'-monophosphate
Mn2+
-
-
Mycophenolic acid
NH4Cl
-
;
p-hydroxymercuribenzoate
p-mercuribenzoate
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2 mM, complete inhibition, complete protection by 2 mM GSH
ribavirin 5'-monophosphate
RMP, competitive inhibition
XTP
-
0.05 mM, 50% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
cysteine
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2 mM required for maximal activity
diguanosine 5',5'''-(P1-P4-tetraphosphate)
-
-
dithiothreitol
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activation
GSH
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2 mM required for maximal activity
GTP
-
nonessential activator
thioglycolic acid
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activation
additional information
-
no sulfhydryl donor required for activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014 - 0.096
GMP
0.0055
guanosine 5'-phosphate
-
pH 7.8, 25C
0.0085 - 0.0348
NADPH
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.265 - 0.519
GMP
0.28
guanosine 5'-phosphate
-
pH 7.8, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
51
guanosine 5'-phosphate
-
pH 7.8, 25C
19
NADPH
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pH 7.8, 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
2'-dXMP
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-
0.0003
8-Aza-XMP
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-
0.014 - 0.035
IMP
0.02
Mycophenolic acid
pH 6.9, 25C, recombinant enzyme
0.00446
ribavirin 5'-monophosphate
pH 8.0, 35C
0.00001 - 0.0011
XMP
additional information
additional information
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0237 - 0.1191
mizoribine 5'-monophosphate
0.1018
ribavirin 5'-monophosphate
Trypanosoma brucei brucei
Q57ZS7
pH 8.0, 35C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003 - 0.0076
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activity in extracts of cells grown on different media
0.0051
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activity in wild-type
0.0052
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-
0.35
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-
0.66
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pH 7.8, 25C
0.8
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activity in wild-type
4.6
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activity in guaC mutant harbouring a guaC plasmid
21.7
pH 8.0, 35C, with NaCl
30.6
pH 8.0, 35C, with NH4Cl
43.8
pH 8.0, 35C, with KCl
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
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enzyme shows 2 maxima
7.5
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7.5 - 8.2
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7.5 - 8.2
7.8
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enzyme shows 2 maxima, strong decrease above
8
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assay at; assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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pH 6: about 50% of activity at maximum, pH 9: about 70% of activity at maximum
7 - 9.5
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pH 7: about 25% of activity at maximum, pH 9.5: about 30% of activity at maximum
7 - 8.2
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strong decrease above
8.1 - 8.6
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 37
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assay at; assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 50
activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.7
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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strong expression
Manually annotated by BRENDA team
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expressed at low levels
Manually annotated by BRENDA team
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expressed at low levels
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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expression of guanosine monophosphate reductase (GMPR), an enzyme involved in de novo biosynthesis of purine nucleotides, is downregulated in invasive stages of human melanoma. From 9 arbitrarily chosen human metastatic melanoma cell lines, GMPR is expressed in only one cell line
Manually annotated by BRENDA team
-
peripheral
Manually annotated by BRENDA team
additional information
not expressed in testis, lung, liver or spleen
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
x * 36000, SDS-PAGE
37382
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4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
37383
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4 * 38000, SDS-PAGE, 4 * 37383, calculated
37384
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4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
37440
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determination of nucleotide sequence
37800
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calculated from the deduced amino acid sequence
38000
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4 * 38000, SDS-PAGE, 4 * 37383, calculated; 4 * 38000, SDS-PAGE, 4 * 37384, calculated, 4 * 37382, mass spectrometry
90000
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gel filtration
156000
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gel filtration
170000
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gel filtration
250000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
quaternary structure determination, LmGMPR subunits may adopt conformations with Trp121 differentially exposed to the aqueous environment
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
no glycosylation site found
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67
-
15 min, 40% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol
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-70C, 2 months, less than 20% loss of activity
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-70C, 2-mercaptoethanol, 6 months, less than 15% loss of activity after several rounds of freezing and thawing
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-80C, no loss of activity
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-80C, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity purification on Cibacron blue
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from recombinant COS-7 cells
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recombinant enzyme using His-tag
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recombinant GST-tagged enzyme from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, the tag is cleaved off by a commercial protease, followed by dialysis
recombinant His-tagged enzyme
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recombinant untagged enzyme from Escherichia coli strain H1174 by affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli M15 as His-tag fusion protein
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expression in Escherichia coli
gene LMJF_17_0725, DNA and amino acid sequence determination and analysis, , the gene has a 131 amino acid insertion encoding two tandem CBS domains, sequence comparisons, recombinant expression in Escherichia coli strain H1174
gene Tb927.5.2080, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene TCIL3000_5_1940, recombinant expression in Escherichia coli
in vitro transcription/translation
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overexpression of wild-type and mutant enzymes in SK-Mel-103 melanoma cells
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transfection of HL-60 leukemia cells, expressed in COS-7 cells as His-tag fusion protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of guanosine monophosphate reductase (GMPR), an enzyme involved in de novo biosynthesis of purine nucleotides, is downregulated in invasive stages of human melanoma
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C186A
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site-directed mutagenesis, a catalytically inactive mutant, overexpression of GMPRC186A mutant at levels comparable to overexpression of wild-type GMPR does not affect invasion in of melanoma cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
-
potential target for the treatment of leukemia
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