Information on EC 3.5.4.3 - guanine deaminase

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

EC NUMBER
COMMENTARY hide
3.5.4.3
-
RECOMMENDED NAME
GeneOntology No.
guanine deaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
guanine + H2O = xanthine + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
drosopterin and aurodrosopterin biosynthesis
-
-
guanosine nucleotides degradation II
-
-
guanosine nucleotides degradation III
-
-
Metabolic pathways
-
-
Purine metabolism
-
-
purine nucleobases degradation I (anaerobic)
-
-
purine nucleobases degradation II (anaerobic)
-
-
purine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
guanine aminohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9033-16-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cow
-
-
Manually annotated by BRENDA team
tea, L. O.Kuntze cv. Yabukita
-
-
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
lingcod
-
-
Manually annotated by BRENDA team
sheep
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Wistar strain
-
-
Manually annotated by BRENDA team
enzyme activity increases during post-diauxic growth, decrease of guanine may be required when cells shift from proliferation to quiescence
-
-
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 + H2O
?
show the reaction diagram
-
the native enzyme shows 107% activity and the recombinant enzyme 98% activity compared to guanine
-
-
?
2,6-diaminopurine + H2O
xanthine + NH3
show the reaction diagram
-
-
-
-
?
2-amino-6-chloropurine + H2O
6-chloro-3,9-dihydro-2H-purin-2-one + NH3
show the reaction diagram
-
-
-
-
?
2-amino-6-chloropurine + H2O
6-chloro-9H-purin-2-ol + NH3
show the reaction diagram
-
the native enzyme shows 93% activity and the recombinant enzyme 88% activity compared to guanine
-
-
?
2-amino-6-methoxypurine + H2O
6-methoxy-3,9-dihydro-2H-purin-2-one + NH3
show the reaction diagram
-
-
-
-
?
6-thioguanine + H2O
6-thioxanthine + NH3
show the reaction diagram
7,8-dihydropterin + H2O
7,8-dihydrolumazine + NH3
show the reaction diagram
8-azaguanine + H2O
8-azaxanthine + NH3
show the reaction diagram
8-azaguanine + H2O
?
show the reaction diagram
8-azaxanthine + H2O
?
show the reaction diagram
-
the native enzyme shows 95% activity and the recombinant enzyme 88% activity compared to guanine
-
-
?
adenine + H2O
allopurinol + NH3
show the reaction diagram
adenosine + H2O
inosine + NH3
show the reaction diagram
ammelide + H2O
cyanuric acid + NH3
show the reaction diagram
-
the absolute activity toward ammelide is 7 orders of magnitude lower than the activity of wild type GDA for guanine
-
-
?
ammeline + H2O
?
show the reaction diagram
-
-
-
?
ammeline + H2O
ammelide + NH3
show the reaction diagram
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
cytidine + H2O
uridine + NH3
show the reaction diagram
-
-
-
-
?
cytosine + H2O
6-hydroxy-1H-pyrimidin-2-one + NH3
show the reaction diagram
-
-
-
-
?
GMP + H2O
XMP + NH3
show the reaction diagram
-
-
-
-
?
guanine + H2O
xanthine + NH3
show the reaction diagram
guanosine + H2O
?
show the reaction diagram
guanosine + H2O
xanthosine + NH3
show the reaction diagram
-
-
-
-
?
hypoxanthine + H2O
?
show the reaction diagram
-
the native enzyme shows 100% activity and the recombinant enzyme 87% activity compared to guanine
-
-
?
uric acid + H2O
?
show the reaction diagram
xanthine + H2O
?
show the reaction diagram
-
the native enzyme shows 01% activity and the recombinant enzyme 87% activity compared to guanine
-
-
?
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
ammeline + H2O
?
show the reaction diagram
Q82Y41
-
-
-
?
guanine + H2O
xanthine + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
-
1 mM AlCl3, relative activity 102%
Hg2+
-
complete inhibition at 1 mM
Mn2+
-
addition results in 2fold increase of activity
additional information
-
not influenced by Ca2+, Fe3+, K+, Mg2+, Ni2+, and Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(6R)-6-hydroxy-3-beta-D-ribofuranosyl-3a,4,5,6,7,8a-hexahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
competitive inhibition
(6S)-6-hydroxy-3-beta-D-ribofuranosyl-3a,4,5,6,7,8a-hexahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
competitive inhibition
1-(4-methoxybenzyl)-4-benzyl-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8-(1H)-one
-
-
-
1-(4-methoxybenzyl)-4-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(1H)-one
-
-
-
2,6-diaminopurine
3-(4-fluorobenzyl)-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
3-(4-methoxybenzyl)-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
3-(4-methoxybenzyl)-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
3-benzyl-5-butoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
3-benzyl-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
3-benzyl-5-hydroxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
3-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
3-benzyl-6-(hydroxymethyl)-3,4,6,7-tetrahydroimidazo[4,5-e][1,4]diazepine-5,8-dione
-
competitive; competitive, the presence of a benzyl group at position-3 enhances the inhibitory activity by greater than twofold as compared to that without the benzyl group
3-Deazaguanine
-
competitive inhibitor
4-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
-
-
4-chloromercuribenzoate
-
the deaminase activities for both 7,8-dihydropterin and guanine are completely inhibited in the presence of 1 mM 4-chloromercuribenzoate
5-amino-4-imidazole carboxamide
5-aminoimidazole-4-carboxamide
5-aminoimidazole-4-carboxamide ribonucleoside
5-methoxy-1-(4-methoxybenzyl)-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(1H)-one
-
-
-
6-(hydroxymethyl)-3,4,6,7-tetrahydroimidazo[4,5-e][1,4]diazepine-5,8-dione
-
competitive; competitive, the presence of a benzyl group at position-3 enhances the inhibitory activity by greater than twofold as compared to that without the benzyl group
6-hydroxy-3,4,6,7-tetrahydroimidazo[4,5-e][1,4]diazepine-5,8-dione
-
i.e. azepinomycin
7-methylguanine
9-(p-aminoethoxyphenyl)guanine
-
strong inhibitor
adenine
adenosine
Ag+
-
6.5% inhibition at 2 mM
allopurinol
-
at concentrations of 1 and 10 mM, potassium fluoride shows weak inhibitory effect on both, guanine deaminase activity (5.2 and 11% inhibition) and dihydropterin deaminase activity (6.2 and 10.1% inhibition)
azepinomycin
Caffeine
Cd(CH3COO)2
-
relative activity 7.4%
CuSO4
-
relative activity 25.8%
Fe2+
-
0.1 mM FeSO4, 82% inhibition
guanidine hydrochloride
-
-
guanosine
-
at concentrations of 1 and 10 mM, guanosine shows weak inhibitory effect on both, guanine deaminase activity (1.8 and 12.5% inhibition) and dihydropterin deaminase activity (3.8 and 5.1% inhibition)
HClO4
Hg2+
-
98.6% inhibition at 2 mM
HgCl2
-
69% inhibition in 5 min
hypoxanthine
Inosine
iodoacetamide
iodoacetic acid
iso-azepinomycin
-
-
-
KCN
-
KCN inhibits dihydropterin deaminase activity strongly 98.6% inhibition at 10 mM whereas it has almost no inhibitory effect on guanine deaminase activity at the same concentration
lumazine
-
at concentrations of 1 and 10 mM, allopurinol shows weak inhibitory effect on both, guanine deaminase activity (4.5 and 17.8% inhibition) and dihydropterin deaminase activity (3.2 and 10% inhibition)
N-2-acetylguanine
natural inhibitor protein
-
p-hydroxymercuribenzoate
Pb2+
-
55.5% inhibition at 2 mM
PCMB
-
relative activity 34.7%
potassium fluoride
-
at concentrations of 1 and 10 mM, potassium fluoride shows weak inhibitory effect on both, guanine deaminase activity (3.6 and 8.1% inhibition) and dihydropterin deaminase activity (0 and 1.2% inhibition)
pterin
-
pterin strongly inhibits guanine deaminase activity (57.8% inhibition at 1 mM), whereas it has a weak effect on dihydropterin deaminase activity
Rose bengal
tetrahydrofolic acid
Urea
-
8 M, both isoenzymes
uric acid
xanthine
Xanthosine
-
-
additional information
-
not inhibited by EDTA, 1,10-phenanthroline, dithiothreitol, L-cysteine, and phenylmethylsulfonyl fluoride
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-dimethylamino-6-hydroxypurine
AMP
-
0.4 mM, residual enzyme activity 112%
ATP
-
0.4 mM, residual enzyme activity 104%
EDTA
-
1 mM, relative activity 104%
GTP
-
positive effector of isoenzyme A, no influence on isoenzyme B
ICH2COOH
-
1mM, relative activity 103%
NaF
-
1 mM, relative activity 102%
uric acid
-
0.4 mM, residual enzyme activity 105%
xanthine
-
0.4 mM, residual enzyme activity 110%
XMP
-
0.4 mM, residual enzyme activity 113%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
6-Thioguanine
-
-
1.621
7,8-dihydropterin
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40C
0.0083 - 0.67
8-Azaguanine
0.0026 - 0.17
guanine
additional information
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.3
7,8-dihydropterin
Drosophila melanogaster
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40C
1.5 - 649
guanine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
7,8-dihydropterin
Drosophila melanogaster
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40C
13265
120 - 8600
guanine
199
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.129
(6R)-6-hydroxy-3-beta-D-ribofuranosyl-3a,4,5,6,7,8a-hexahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
0.119
(6S)-6-hydroxy-3-beta-D-ribofuranosyl-3a,4,5,6,7,8a-hexahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
0.0438
1-(4-methoxybenzyl)-4-benzyl-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8-(1H)-one
-
at 25C and pH 7.4
-
0.0265
1-(4-methoxybenzyl)-4-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(1H)-one
-
at 25C and pH 7.4
-
0.00188
2,6-diaminopurine
-
in 25 mM Tris-HCl, 137 mM NaCl, 2.7 mM KCl, at pH 7.4 and 25C
0.0397
3-(4-fluorobenzyl)-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
-
0.0334
3-(4-methoxybenzyl)-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
-
0.021
3-benzyl-5-butoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
-
0.054
3-benzyl-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
-
0.04
3-benzyl-5-hydroxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
-
0.047
3-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
-
0.00201 - 0.02
3-benzyl-6-(hydroxymethyl)-3,4,6,7-tetrahydroimidazo[4,5-e][1,4]diazepine-5,8-dione
0.0088
4-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
-
at 25C and pH 7.4
-
0.00444
5-amino-4-imidazole carboxamide
-
in 25 mM Tris-HCl, 137 mM NaCl, 2.7 mM KCl, at pH 7.4 and 25C
0.0475
5-methoxy-1-(4-methoxybenzyl)-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(1H)-one
-
at 25C and pH 7.4
-
0.00536 - 0.054
6-(hydroxymethyl)-3,4,6,7-tetrahydroimidazo[4,5-e][1,4]diazepine-5,8-dione
0.0005
6-hydroxy-3,4,6,7-tetrahydroimidazo[4,5-e][1,4]diazepine-5,8-dione
-
pH 7.4, 25C
0.00555
7-methylguanine
-
in 25 mM Tris-HCl, 137 mM NaCl, 2.7 mM KCl, at pH 7.4 and 25C
0.0025 - 2.5
azepinomycin
0.0102
Caffeine
-
in 25 mM Tris-HCl, 137 mM NaCl, 2.7 mM KCl, at pH 7.4 and 25C
0.00344
N-2-acetylguanine
-
in 25 mM Tris-HCl, 137 mM NaCl, 2.7 mM KCl, at pH 7.4 and 25C
0.00434
uric acid
-
in 25 mM Tris-HCl, 137 mM NaCl, 2.7 mM KCl, at pH 7.4 and 25C
0.00196
xanthine
-
in 25 mM Tris-HCl, 137 mM NaCl, 2.7 mM KCl, at pH 7.4 and 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00011
-
crude extract, at 50C, using 7,8-dihydropterin as substrate, pH not specified in the publication
0.1
-
crude extract, at pH 6.0 and 37C
0.6435
-
after 5850fold purification, at 50C, using 7,8-dihydropterin as substrate, pH not specified in the publication
1.14
-
purified liver enzyme
1.36
-
kidney enzyme
2.42
-
brain enzyme
4.7
-
after 51.5fold purification, at pH 6.0 and 37C
5.1
-
liver enzyme
8.61
-
-
9.53
-
recombinant enzyme
9.9
-
liver enzyme, isoenzyme A
11.2
-
intestine enzyme, purification at 0-4C
13.2
-
brain enzyme
13.7
-
purified brain enzyme
16.8
-
brain enzyme, purification at room temperature
17.2
-
liver enzyme, purification at room temperature
19.3
-
liver enzyme, purification at 0-4C
21.5
-
-
21.7
-
-
22.1
-
-
22.4
-
brain enzyme, purification at 0-4C
23.5
-
lung enzyme
25.2
-
liver enzyme
25.4
-
intestine enzyme, purification at room temperature
33.6
-
isoenzyme B
530
-
crude cell extract, pH 7.5, temperature not specified in the publication
1140
-
crude cell extract, pH 7.5, temperature not specified in the publication
additional information
-
colorimetric and HPLC assay method using guanosine as a prosubstrate. Method is suitable for routine assays for measuring plasma enzyme over a wide range of activites
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
8-azaguanine as substrate
5.9
-
liver enzyme
6.5
-
the native enzyme shows optimal pH values of 6.5 and 8.0 while the recombinant enzyme has a single pH optimum at pH 6.5
7 - 7.5
-
double peaks of optimum activity, second optimum at pH 8.5
7
-
recombinant protein, expressed in mice DH5-alpha cells, Km remains constant between pH 6.5 and pH 7.5
7 - 8
-
-
7 - 7.5
-
double peaks of optimum activity, second optimum at pH 8.5
7.4 - 9.4
-
-
7.4
-
assay at
7.5 - 9.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10.5
-
-
5 - 8.5
-
activity relatively low at pH 5.1-5.5, increase in activity above pH 6.0 until pH 8.5, above pH 8.5 activity starts to drop off
5.5 - 9
-
-
5.5 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
activation energy linear
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cancerous and non-cancerous
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
of a patient with resected gastric cancer
Manually annotated by BRENDA team
-
metastatic
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
-
1 * 26000 + 1 * 49000 + 1 * 77000, SDS-PAGE
49000
-
1 * 26000 + 1 * 49000 + 1 * 77000, SDS-PAGE
49500
-
2 * 49500, SDS-PAGE
50200
-
recombinant protein
51040
-
calculated from cDNA corresponding to an open reading frame
53000
-
2 * 53000, calculated from amino acid sequence
53020
-
calculated from amino acid analysis
56000
-
liver enzyme, gel filtration
77000
-
1 * 26000 + 1 * 49000 + 1 * 77000, SDS-PAGE
92200
-
gel filtration, non denaturing PAGE
95800
-
liver enzyme, gel filtration
100000 - 110000
-
recombinant and native enzyme, gel filtration
105000
107800
-
crosslinking
108000
-
gel filtration
117000
-
gel filtration, lower pH and lower ionic strength, 2 different polymers
120000
170000
200000
207000
220000
-
gel filtration without mercaptoethanol
240000
265000
-
gel filtration, lower pH and lower ionic strength, 2 different polymers
525000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
oligomer
-
1 * 26000 + 1 * 49000 + 1 * 77000, SDS-PAGE
tetramer
-
4 * 50000, erythrocytic enzyme, 5% of the protein present, SDS-PAGE
additional information
-
computational homology modeling techniques to construct a three dimensional structural model of cypin, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in absence and presence of inhibitor hypoxanthine, growth of crystals in 30% polyethylene glycol
-
in complex with 8-azaguanine, hanging drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
-
209539
6.5 - 8
-
native and recombinant enzymes are stable during incubation for 1 h at 37C with pH in the range of 6.5-8.0
734510
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
the native enzyme remains stable for 1 h at up to 30C
45
-
relatively stable, incubation for 5 min, 3% loss in activity, 17% after 30 min
65
-
activity completely lost after 30 min incubation
70
-
activity remains unaffected from 0-50C, 19.3% inactivation at 60C, 33% inactivation at 70C, complete lost of activity at 80C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of bovine serum albumin stabilizes the 2 isoenzymes in the cold and isoenzyme A in the frozen state
-
stabilized by 2-mercaptoethanol, labile to heat
-
stable to heat
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, isoenzyme A loses about 60% of activity on thawing after 7 days, isoenzyme B is unaltered in activity
-
-20C stable for 2 weeks with only a few percent loss
-
-20C, 28 days, 123% activity
-
-20C, with 20% (v/v) glycine, 28 days, 65% residual activity
-
0-4C, activity of isoenzyme A completely lost in 16 days, isoenzyme B loses 30% activity
-
0C, 10 mM phosphate buffer, pH 7.0, 0.1 mM dithiothreitol, can be stored for more than 2 weeks without appreciable loss of activity
-
0C, retains its activity unaltered during storage for a month
-
22C, 28 days, 34% residual activity
-
4C stable for 2 weeks with only a few percent loss
-
4C, 0.1 M phosphate buffer, 2 mM 2-mercaptoethanol, pH 7.5, stable for at least 3 months
-
4C, 28 days, 44% residual activity
-
purified enzyme stabilized by storage in 30-40% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes, A and B
-
ammonium sulfate precipitation, phenyl-Sepharose column chromatography, Sephacryl HR S 300 gel filtration
-
heat precipitation, DEAE Sepharose column chromatography, and Superdex 200 gel filtration
-
HiTrap IMAC column chromatography
liver and brain, 2 isoenzymes, A and B
-
Ni-NTAcolumn chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned from kidney and brain cDNA libraries, PCR, subcloned into bacterial expression vector pMAL-c2, expressed in mice DH5-alpha cells and purified
-
expressed in Arxula adeninivorans strain G1212
-
expressed in Escherichia BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21 cells
-
expression of wild-type and mutant enzymes in COS-7 cells, subcloning in Escherichia coli strain DH5alpha
-
gene identified with human cDNA, amplified, subcloned into pMAL-c2 vector, expressed and purified
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of guaD is mainly regulated by nitrogen availability through the action of NtrC
-
immediately after the shift of cells into media with purine as nitrogen source, the enzyme transcript level increases and reached maximum level at 2 h with adenine and 4 h with hypoxanthine, after which transcription fell to the basal level
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E143X
the mutation results in a complete loss of activity
E79X
the mutation results in a complete loss of activity
D330A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H240A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H279A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H71A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
H82A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H84A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I83A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
colorimetric and HPLC assay method using guanosine as a prosubstrate. Method is suitable for routine assays for measuring plasma enzyme over a wide range of activites
drug development
-
because these enzymes play an important role in nucleotide metabolism, they are relevant targets in anticancer and antibacterial therapies
medicine
Show AA Sequence (1693 entries)
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