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Information on EC 3.5.4.3 - guanine deaminase
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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 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Agdap
cypin
GDA
GDEase
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guaD
guanase
guanine aminase
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Guanine aminohydrolase
guanine deaminase
GUD1
KLLAOD9492
p51-nedasin
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additional information
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cypin is a member of the metal-dependent aminohydrolase family
guanase
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Guanine aminohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
guanine + H2O = xanthine + NH3
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guanine + H2O = xanthine + NH3
catalytic mechanism, quantum mechanical calculations using multilayered ONIOM and molecular dynamics study, the active-site residues of the enzyme do not affect the tautomeric state of guanine, Glu55 and Asp114 play important roles in proton shuttling in the reaction, proton transfer from a Zn-bound water to protonate Asp114, which can then transfer its proton to the N3 of the bound guanine, facilitating the nucleophilic attack on C2 of the guanine by the Zn-bound hydroxide to form a tetrahedral intermediate. Glu55 then transfers a proton from the Zn-hydroxide to the amino group of the reaction intermediate, ammonia leaves the active site, and xanthine is freed by the cleavage of the Zn-O2 bond
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
amidine hydrolysis
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
guanine aminohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9033-16-3
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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
2,6-diaminopurine + H2O
?
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the native enzyme shows 107% activity and the recombinant enzyme 98% activity compared to guanine
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?
2-amino-6-chloropurine + H2O
6-chloro-3,9-dihydro-2H-purin-2-one + NH3
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?
2-amino-6-chloropurine + H2O
6-chloro-9H-purin-2-ol + NH3
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the native enzyme shows 93% activity and the recombinant enzyme 88% activity compared to guanine
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?
2-amino-6-methoxypurine + H2O
6-methoxy-3,9-dihydro-2H-purin-2-one + NH3
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?
8-azaxanthine + H2O
?
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the native enzyme shows 95% activity and the recombinant enzyme 88% activity compared to guanine
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?
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
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?
hypoxanthine + H2O
?
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the native enzyme shows 100% activity and the recombinant enzyme 87% activity compared to guanine
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?
xanthine + H2O
?
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the native enzyme shows 01% activity and the recombinant enzyme 87% activity compared to guanine
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?
6-thioguanine + H2O
6-thioxanthine + NH3
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?
7,8-dihydropterin + H2O
7,8-dihydrolumazine + NH3
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the enzyme exhibits 40fold higher activity for guanine than for 7,8-dihydropterin. Guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin
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?
7,8-dihydropterin + H2O
7,8-dihydrolumazine + NH3
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the enzyme exhibits 40fold higher activity for guanine than for 7,8-dihydropterin. Guanine deaminase functions as dihydropterin deaminase in the biosynthesis of aurodrosopterin
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?
8-azaguanine + H2O
8-azaxanthine + NH3
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the native enzyme shows 99% activity and the recombinant enzyme 95% activity compared to guanine
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?
8-azaguanine + H2O
8-azaxanthine + NH3
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the native enzyme shows 99% activity and the recombinant enzyme 95% activity compared to guanine
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?
8-azaguanine + H2O
8-azaxanthine + NH3
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high substrate specificity, only 60% of the reaction rate with the natural substrate guanine
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?
8-azaguanine + H2O
8-azaxanthine + NH3
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?
8-azaguanine + H2O
?
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the enzyme shows 60% activity for 8-azaguanine relative to 7,8-dihydropterin
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?
8-azaguanine + H2O
?
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the enzyme shows 60% activity for 8-azaguanine relative to 7,8-dihydropterin
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?
adenine + H2O
allopurinol + NH3
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the native enzyme shows 102% activity and the recombinant enzyme 85% activity compared to guanine
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?
adenine + H2O
allopurinol + NH3
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the native enzyme shows 102% activity and the recombinant enzyme 85% activity compared to guanine
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?
adenosine + H2O
inosine + NH3
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the native enzyme shows 98% activity and the recombinant enzyme 91% activity compared to guanine
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?
adenosine + H2O
inosine + NH3
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the native enzyme shows 98% activity and the recombinant enzyme 91% activity compared to guanine
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?
guanine + H2O
xanthine + NH3
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substrate binding structure and tautomerization of the bound guanine, reaction steps in a detailed overview
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?
guanine + H2O
xanthine + NH3
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?
guanine + H2O
xanthine + NH3
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enzyme shows activity toward guanine not toward adenine
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?
guanine + H2O
xanthine + NH3
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209584, 209586, 209587, 209591, 209592, 209593, 209594, 209595, 209601, 667985, 711469, 733480, 733496
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?
guanine + H2O
xanthine + NH3
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reaction via tetrahedral intermediate
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?
guanine + H2O
xanthine + NH3
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?
guanine + H2O
xanthine + NH3
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the enzyme plays a central role in neuronal development, and an active role in regulating dendrite branching in hippocampal neurons, cypin-promoted increases in dendrite number are dependent on its zinc-dependent guanine deaminase activity, overview
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?
guanosine + H2O
?
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the native enzyme shows 48% activity and the recombinant enzyme 70% activity compared to guanine
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?
guanosine + H2O
?
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the enzyme shows 5% activity for guanosine relative to 7,8-dihydropterin
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?
guanosine + H2O
?
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the enzyme shows 5% activity for guanosine relative to 7,8-dihydropterin
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?
uric acid + H2O
?
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the native enzyme shows 89% activity and the recombinant enzyme 86% activity compared to guanine
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?
uric acid + H2O
?
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the native enzyme shows 89% activity and the recombinant enzyme 86% activity compared to guanine
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?
additional information
?
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the enzyme does not metabolize ammelide or melamine
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?
additional information
?
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the enzyme does not metabolize ammelide or melamine
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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the enzyme does not metabolize ammelide or melamine
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?
additional information
?
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9-methylguanine, 6-O-methylguanine, 6-thioguanine, and 2,6-diaminopurine, also exhibit measurable activity but turn over very slowly, i.e. below 0.001 per s
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?
additional information
?
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9-methylguanine, 6-O-methylguanine, 6-thioguanine, and 2,6-diaminopurine, also exhibit measurable activity but turn over very slowly, i.e. below 0.001 per s
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?
additional information
?
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nedasin, an enzyme involved in synaptic connections between neurons binding to neuronal and endocrine lethal discs large, might be an isozyme of guanase, overview
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?
additional information
?
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the enzyme does not metabolize ammelide or melamine
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?
additional information
?
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the enzyme does not metabolize ammelide or melamine
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?
additional information
?
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the enzyme does not metabolize ammelide or melamine
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?
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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
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?
guanine + H2O
xanthine + NH3
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?
guanine + H2O
xanthine + NH3
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?
guanine + H2O
xanthine + NH3
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the enzyme plays a central role in neuronal development, and an active role in regulating dendrite branching in hippocampal neurons, cypin-promoted increases in dendrite number are dependent on its zinc-dependent guanine deaminase activity, overview
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
Mg2+
Zinc
Zn2+
additional information
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not influenced by Ca2+, Fe3+, K+, Mg2+, Ni2+, and Zn2+
Cu2+
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at 1 mM Cu2+, the native enzyme shows about 80% inhibition and the recombinant enzyme almost complete (99%) inhibition
Mg2+
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1.0 mM MgSO4, 27% activation of isoenzyme A, 22% of isoenzyme B, 0.5 mM 18% activation of isoenzyme A, 11% activation of isoenzyme B, 1.0 mM MgCl2, 45% activation of isoenzyme A, 33% activation of isoenzyme B, 0.5 mM MgCl2, no effect on isoenzyme A, 11% activation of isoenzyme B
Zinc
GuaD possesses a single zinc cation with trigonal bipyrimidal coordination geometry within its active site
Zinc
Gud1 possesses a single zinc cation with trigonal bipyrimidal coordination geometry within its active site
Zn2+
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essential for activity, binding structure, computational homology modeling shows that several histidines and aspartic acid residues are responsible for zinc binding, e.g. His82, His84, His240, His279, and Asp330, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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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
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competitive inhibition
1-(4-methoxybenzyl)-4-benzyl-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8-(1H)-one
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1-(4-methoxybenzyl)-4-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(1H)-one
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3-(4-fluorobenzyl)-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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3-(4-methoxybenzyl)-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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3-(4-methoxybenzyl)-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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3-benzyl-5-butoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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3-benzyl-5-ethoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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3-benzyl-5-hydroxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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3-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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3-benzyl-6-(hydroxymethyl)-3,4,6,7-tetrahydroimidazo[4,5-e][1,4]diazepine-5,8-dione
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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
4-benzyl-5-methoxy-4,5,6,7-tetrahydroimidazo[4,5-e][1,4]diazepin-8(3H)-one
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4-chloromercuribenzoate
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the deaminase activities for both 7,8-dihydropterin and guanine are completely inhibited in the presence of 1 mM 4-chloromercuribenzoate
5-aminoimidazole-4-carboxamide ribonucleoside