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Information on EC 3.5.4.3 - guanine deaminase and Organism(s) Drosophila melanogaster

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.3 guanine deaminase
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Drosophila melanogaster
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The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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guanine
+
H2O
=
xanthine
+
NH3
+
=
+
Synonyms
guanase, guanine deaminase, cypin, agdap, guanine aminohydrolase, ne0047, cytosolic psd-95 interactor, gdease, human guanine deaminase, e. coli guanine deaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDEase
-
-
-
-
guanase
-
-
-
-
guanine aminase
-
-
-
-
Guanine aminohydrolase
-
-
-
-
p51-nedasin
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
guanine aminohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9033-16-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydropterin + H2O
7,8-dihydrolumazine + NH3
show the reaction diagram
-
the enzyme exhibits 40fold higher activity for guanine than for 7,8-dihydropterin. Guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin
-
-
?
8-azaguanine + H2O
?
show the reaction diagram
-
the enzyme shows 60% activity for 8-azaguanine relative to 7,8-dihydropterin
-
-
?
guanine + H2O
xanthine + NH3
show the reaction diagram
-
-
-
-
?
guanosine + H2O
?
show the reaction diagram
-
the enzyme shows 5% activity for guanosine relative to 7,8-dihydropterin
-
-
?
additional information
?
-
-
the enzyme has no deaminase activities for other dihydropteridines such as 7,8-dihydrobiopterin, 7,8-dihydroneopterin, and sepiapterin, it also does not show deaminase activity with fully oxidized pteridines such as pterin, biopterin, neopterin, monapterin, xanthopterin, isoxanthopterin, aminopterin, 6-formylpterin, 6-carboxypterin, and 6-hydroxymethylpterin. Moreover the enzyme does not use folic acid, pyrimidodiazepine, drosopterin, or isodrosopterin as a substrate. No activity is found for adenine and adenosine
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
the deaminase activities for both 7,8-dihydropterin and guanine are completely inhibited in the presence of 1 mM 4-chloromercuribenzoate
adenine
-
at concentrations of 1 and 10 mM, adenine shows weak inhibitory effect on both, guanine deaminase activity (7.1 and 24% inhibition) and dihydropterin deaminase activity (10.3 and 14.1% inhibition)
adenosine
-
at concentrations of 1 and 10 mM, adenosine shows weak inhibitory effec on both, guanine deaminase activity (5.6 and 22.7% inhibition) and dihydropterin deaminase activity (11.5 and 16.7% inhibition)
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)
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)
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)
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
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pterin strongly inhibits guanine deaminase activity (57.8% inhibition at 1 mM), whereas it has a weak effect on dihydropterin deaminase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.621
7,8-dihydropterin
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40°C
0.0757
guanine
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in 100 mM potassium phosphate buffer (pH 7.5), at 40°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.3
7,8-dihydropterin
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40°C
649
guanine
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
7,8-dihydropterin
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40°C
8600
guanine
-
in 100 mM potassium phosphate buffer (pH 7.5), at 40°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00011
-
crude extract, at 50°C, using 7,8-dihydropterin as substrate, pH not specified in the publication
0.6435
-
after 5850fold purification, at 50°C, using 7,8-dihydropterin as substrate, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GUAD_DROME
448
0
48885
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 48000, native enzyme, SDS-PAGE and gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl-Sepharose column chromatography, Sephacryl HR S 300 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, J.; Park, S.I.; Ahn, C.; Kim, H.; Yim, J.
Guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin, a minor red eye pigment of Drosophila
J. Biol. Chem.
284
23426-23435
2009
Drosophila melanogaster, Drosophila melanogaster Oregon-R
Manually annotated by BRENDA team