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Information on EC 3.5.4.3 - guanine deaminase and Organism(s) Homo sapiens
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3.5.4.3 guanine deaminaseSpecify your search results
Word Map
- 3.5.4.3
- xanthine
- purine
-
deamination
-
uric
-
agdas
- hypoxanthine
-
anogenital
- 8-azaguanine
-
anus
-
penis
-
scrotum
- medicine
-
cephalad
- deaminases
- drug development
- analysis
- food industry
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
guanase, guanine deaminase, cypin, agdap, guanine aminohydrolase, ne0047, cytosolic psd-95 interactor, gdease, human guanine deaminase, e. coli guanine deaminase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GDEase
-
-
-
-
guanase
guanine aminase
-
-
-
-
Guanine aminohydrolase
-
-
-
-
p51-nedasin
-
-
-
-
guanase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
guanine aminohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9033-16-3
-
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
ammelide + H2O
cyanuric acid + NH3
the absolute activity toward ammelide is 7 orders of magnitude lower than the activity of wild type GDA for guanine
-
-
?
8-azaguanine + H2O
8-azaxanthine + NH3
-
high substrate specificity, only 60% of the reaction rate with the natural substrate guanine
-
-
?
guanine + H2O
xanthine + NH3
-
-
-
-
?
additional information
?
-
-
nedasin, an enzyme involved in synaptic connections between neurons binding to neuronal and endocrine lethal discs large, might be an isozyme of guanase, overview
-
-
?
additional information
?
-
the enzyme does not metabolize ammelide or melamine
-
-
?
NATURAL SUBSTRATE
NATURAL 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
guanine + H2O
xanthine + NH3
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetic acid
-
0.1 mM 7% loss in the activity, 1 mM 29% loss in the activity after 30 min incubation
F-
-
inhibition decreases as pH increases, 50% activity was inhibited at pH 7.5, most of activity lost at pH 6.5
p-hydroxymercuribenzoate
-
noncompetitive inhibitor, 0.1 mM, 37°C, rapid inactivation
p-hydroxymercuribenzoate
-
0.0001 M 91% loss of activity after 30 min incubation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
LITERATURE
7
recombinant protein, expressed in mice DH5-alpha cells, Km remains constant between pH 6.5 and pH 7.5
7.5 - 9.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
human
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
immunohistochemic expression analysis of guanase, and comparison with the expression profile of nedasin, which might be an isozyme of guanase, nedasin and guanase expression is identical in all tissues but the liver, overview
additional information
-
immunohistochemic expression analysis of guanase, and comparison with the expression profile of nedasin, which might be an isozyme of guanase, overview, no expression of guanase in skeletal muscle
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GUAD_HUMAN
454
0
51003
Swiss-Prot
other Location (Reliability: 5)
A0A024R231_HUMAN
454
0
51003
TrEMBL
other Location (Reliability: 5)
B4DIP8_HUMAN
178
0
19279
TrEMBL
other Location (Reliability: 1)
Q5SZC3_HUMAN
179
0
19310
TrEMBL
other Location (Reliability: 2)
H0YDZ7_HUMAN
176
0
19051
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
120000
200000
50000
55000
59000
55000
2 * 55000, can be converted into monomeric form by addition of sulfhydryl groups
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 55000, can be converted into monomeric form by addition of sulfhydryl groups
dimer
2 * 55000, can be converted into monomeric form by addition of sulfhydryl groups
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
relatively stable, incubation for 5 min, 3% loss in activity, 17% after 30 min
55
-
becomes labile at, loses 21% of activity after 5 min incubation, 49% after 30 min
60
-
50% activity lost during 30 min incubation, after 60 min 40% activity remains
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
medicine
medicine
-
enzyme has been implicated in cancer, liver disease, saturine gout, psoriasis and autoimmune disease, histochemical method for demonstration of guanase should be useful clinically, guanase activity increases significantly in lung and gastric cancer tissues or in patients with liver diseases like hepatitis, guanase is a biochemical indicator of rejection in liver transplant recipients, serum enzyme activity is the most sensitive indicator of liver disease, inhibition of guanase has beneficial implications in cancer chemotherapy, an inhibitor as chemotherapeutic agent selectively inhibit the growth of rapidly proliferating cancerous cells via depletion of the purine nucleotide pool
medicine
enzyme has been implicated in cancer, liver disease, saturine gout, psoriasis and autoimmune disease, histochemical method for demonstration of guanase should be useful clinically, guanase activity increases significantly in lung and gastric cancer tissues or in patients with liver diseases like hepatitis, guanase is a biochemical indicator of rejection in liver transplant recipients, serum enzyme activity is the most sensitive indicator of liver disease, inhibition of guanase has beneficial implications in cancer chemotherapy, an inhibitor as chemotherapeutic agent selectively inhibit the growth of rapidly proliferating cancerous cells via depletion of the purine nucleotide pool
medicine
-
test for cancerous tissues, lower guanase activities compared with non-cancerous ones
medicine
-
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
medicine
GDA is an attractive and potential drug target for treatment of both liver diseases and cognitive disorders
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kimm, S.W.; Park, J.B.; Kim, H.L.
The physicochemical properties of guanine aminohydrolase purified from human liver
Korean J. Biochem.
19
39-46
1987
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus sp.
-
Kimm, S.W.; Park, J.B.; Lee, I.S.
Purification and characterization of guanine aminohydrolase from human liver
Korean J. Biochem.
17
139-148
1985
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
-
Gupta, N.K.; Glantz, M.D.
Isolation and characterization of human liver guanine deaminase
Arch. Biochem. Biophys.
236
266-276
1985
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus sp.
Pugh, M.E.; Bieber, A.L.
Studies of rabbit brain, intestine and liver guanine aminohydrolase
Comp. Biochem. Physiol. B
77
619-627
1984
Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Ovis ammon, Sus sp.
Kim, C.J.; Kimm, S.W.
Enzymatic evidence for a mitochondrial inhibitor of guanine aminohydrolase in rat liver
Korean J. Biochem.
14
77-93
1982
Clostridium sp., Homo sapiens, Mus musculus, Ophiodon elongatus, Rattus norvegicus, Rattus norvegicus Sprague Dawley
-
Kuzmits, R.; Stemberger, H.; Muller, M.M.
Guanase from human liver - purification and characterization
Adv. Exp. Med. Biol.
122B
183-188
1980
Homo sapiens, Mus musculus, Rattus norvegicus
Fogle, P.J.; Bieber, A.L.
Purification of rabbit liver guanine aminohydrolase
Prep. Biochem.
5
59-77
1975
Oryctolagus cuniculus, Homo sapiens, Ophiodon elongatus, Rattus norvegicus
Ito, S.; Maeda, T.; Iwasaki, A.; Fujikawa, H.; Okahisa, T.; Saijyou, T.; II, K.; Sano, N.; Matsuda, Y.; Endo, H.
Histochemical and biochemical studies on guanase in the human and rat kidney
Acta Histochem.
24
591-596
1991
Homo sapiens, Mus musculus, Rattus norvegicus
-
Canbolat, O.; Durak, I.; Cetin, R.; Kavutcu, M.; Demirci, S.; Oeztuerk, S.
Activities of adenosine deaminase, 5'-nucleotidase, guanase, and cytidine deaminase enzymes in cancerous and non-cancerous human breast tissues
Breast Cancer Res. Treat.
37
189-193
1996
Homo sapiens
Rajappan, V.P.; Hosmane, R.
Analogues of azepinomycin as inhibitors of guanase
Nucleosides Nucleotides
17
1141-1151
1998
Oryctolagus cuniculus, Homo sapiens
Yuan, G.; Bin, J.C.; McKay, D.J.; Snyder, F.F.
Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein
J. Biol. Chem.
274
8175-8180
1999
Mus musculus, Sus sp., Homo sapiens (Q9Y2T3), Homo sapiens
Maynes, J.T.; Yuan, R.G.; Snyder, F.F.
Identification, expression and characterization of Escherichia coli guanine deaminase
J. Bacteriol.
8
4658-4660
2000
Escherichia coli, Homo sapiens (Q9Y2T3), Homo sapiens
Roberts, E.L.; Newton, R.P.
Estimation of guanine deaminase using guanosine as a "prosubstrate"
Anal. Biochem.
324
250-257
2004
Homo sapiens
Sannomiya, K.; Honda, H.; Kubo, K.; Ii, K.; Yuan, Y.; Aoyagi, E.; Muguruma, N.; Shimizu, I.; Ito, S.
A histochemical and immunohistochemical investigation of guanase and nedasin in rat and human tissues
J. Med. Invest.
53
246-254
2006
Homo sapiens, Rattus norvegicus
Kubo, K.; Honda, H.; Honda, H.; Sannomiya, K.; Aying, Y.; Mei, W.; Mi, S.; Aoyagi, E.; Simizu, I.; Ii, K.; Ito, S.
Histochemical and immunohistochemical investigation of guanase and nedasin in human tissues
J. Med. Invest.
53
264-270
2006
Homo sapiens
Fernandez, J.R.; Sweet, E.S.; Welsh, W.J.; Firestein, B.L.
Identification of small molecule compounds with higher binding affinity to guanine deaminase (cypin) than guanine
Bioorg. Med. Chem.
18
6748-6755
2010
Oryctolagus cuniculus, Rattus norvegicus, Homo sapiens (Q9Y2T3), Homo sapiens
Seffernick, J.L.; Dodge, A.G.; Sadowsky, M.J.; Bumpus, J.A.; Wackett, L.P.
Bacterial ammeline metabolism via guanine deaminase
J. Bacteriol.
192
1106-1112
2010
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110, Escherichia coli, Homo sapiens (Q9Y2T3), Pseudomonas putida, Pseudomonas putida KT 2240
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