Information on EC 3.5.4.2 - adenine deaminase

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

EC NUMBER
COMMENTARY
3.5.4.2
-
RECOMMENDED NAME
GeneOntology No.
adenine deaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
adenine + H2O = hypoxanthine + NH3
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of amidines
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
adenine and adenosine salvage IV
-
Metabolic pathways
-
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
adenine aminohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Aah1p
Saccharomyces cerevisiae BY4742
-
-
-
ADase
-
-
-
-
adenase
-
-
-
-
adenine aminase
-
-
-
-
adenine deaminase
P53909
-
adenine deaminase
Saccharomyces cerevisiae 23344c
P53909
-
-
adenine deaminase
Q9P6I7
-
NadA
Q8X1T6
-
Sgx9403g
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-68-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
no activity in other than some bacteria and some lower eukaryotes
-
-
-
Manually annotated by BRENDA team
Pseudomonas synxantha A3
strain A3
-
-
Manually annotated by BRENDA team
strain BY4742, gene AAH1
-
-
Manually annotated by BRENDA team
this enzyme catalyses the reaction of EC 3.5.4.2. and EC 3.5.4.4; strain 23344c
SwissProt
Manually annotated by BRENDA team
Saccharomyces cerevisiae 23344c
this enzyme catalyses the reaction of EC 3.5.4.2. and EC 3.5.4.4; strain 23344c
SwissProt
Manually annotated by BRENDA team
Saccharomyces cerevisiae BY4742
strain BY4742, gene AAH1
-
-
Manually annotated by BRENDA team
this enzyme catalyses the reaction of EC 3.5.4.2 and EC 3.5.4.4; wild-type 972 h
SwissProt
Manually annotated by BRENDA team
strain J-350P
-
-
Manually annotated by BRENDA team
Streptomyces sp. J-350P
strain J-350P
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
deletion of the AAH locus in intact parasites establishes that AAH is not an essential gene and that -/-aah cells are capable of salvaging the same range of purine nucleobases and nucleosides as wild type Leishmania donovani. The aah null mutant is able to infect murine macrophages in vitro and in mice, although the parasite loads in both model systems are modestly reduced compared with wild type infections
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,6-diaminopurine + H2O
guanine + NH3
show the reaction diagram
-
-
-
?
2,6-diaminopurine + H2O
guanine + NH3
show the reaction diagram
-
-
-
?
2,6-diaminopurine + H2O
guanine + NH3
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
2,6-diaminopurine + H2O
guanine + NH3
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
2-amino-6-chloropurine + H2O
guanine + HCl
show the reaction diagram
-
-
-
?
2-amino-6-chloropurine + H2O
guanine + HCl
show the reaction diagram
-
-
-
?
6-amino-2-hydroxypurine + H2O
xanthine + NH3
show the reaction diagram
-
-
-
-
6-amino-2-hydroxypurine + H2O
xanthine + NH3
show the reaction diagram
-
-
-
?
6-bromopurine + H2O
hypoxanthine + HBr
show the reaction diagram
-
-
-
?
6-bromopurine + H2O
hypoxanthine + HBr
show the reaction diagram
-
-
-
?
6-bromopurine + H2O
hypoxanthine + HBr
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
6-bromopurine + H2O
hypoxanthine + HBr
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
-
-
-
-
?
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
-
-
-
-
-
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
-
-
-
-
?
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
-
-
-
?
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
-
-
-
?
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
-
-
-
-
?
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
6-chloropurine + H2O
hypoxanthine + HCl
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
6-chloropurine + H2O
?
show the reaction diagram
-
-
-
-
-
6-iodopurine + H2O
hypoxanthine + HI
show the reaction diagram
-
-
-
?
6-iodopurine + H2O
hypoxanthine + HI
show the reaction diagram
-
-
-
?
6-iodopurine + H2O
hypoxanthine + HI
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
6-iodopurine + H2O
hypoxanthine + HI
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
6-[(E)-4-hydroxy-3-methylbut-2-enylamino]purine + H2O
?
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae 23344c
P53909
1.8% of the activity of adenine
-
-
?
6-[(Z)-4-hydroxy-3-methylbut-2-enylamino]purine + H2O
?
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae 23344c
P53909
1.7% of the activity of adenine
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
ir
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
ir
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Q8X1T6
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Q9P6I7, -
-
-
-
ir
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
P53909
-
-
-
ir
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
-
specific substrate
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
P53909
irreversible deamination, metabolic salvage pathway of purines
-
-
i
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Q9P6I7, -
irreversible deamination, metabolic salvage pathway of purines
-
-
i
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Pseudomonas synxantha A3
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Streptomyces sp. J-350P
-
-
-
?
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Saccharomyces cerevisiae 23344c
P53909
-
-
-
ir
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
anaerobic conversion
-
-
-
adenine + H2O
?
show the reaction diagram
-
purine salvage pathway and nitrogen metabolism
-
-
-
adenine + H2O
?
show the reaction diagram
-
purine salvage pathway and nitrogen metabolism
-
-
-
adenine + H2O
?
show the reaction diagram
Streptomyces sp. J-350P
-
-
-
-
-
benzyladenine + H2O
hypoxanthine + 1-phenylmethaneamine
show the reaction diagram
P53909
0.7% of the activity of adenine
-
-
ir
benzyladenine + H2O
hypoxanthine + 1-phenylmethaneamine
show the reaction diagram
Q9P6I7, -
3.8% of the activity of adenine
-
-
ir
benzyladenine + H2O
hypoxanthine + 1-phenylmethaneamine
show the reaction diagram
Saccharomyces cerevisiae 23344c
P53909
0.7% of the activity of adenine
-
-
ir
kinetin + H2O
?
show the reaction diagram
P53909
release of hypoxanthine and inosine, release of amine from from the cytokinine side chain
-
-
?
kinetin + H2O
?
show the reaction diagram
Q9P6I7, -
release of hypoxanthine and inosine, release of amine from from the cytokinine side chain
-
-
?
kinetin + H2O
?
show the reaction diagram
P53909
hydrolysis of adenine compounds, cleavage of cytokinins into inosine and the corresponding side chain amine
-
-
?
kinetin + H2O
?
show the reaction diagram
Q9P6I7, -
hydrolysis of adenine compounds, cleavage of cytokinins into inosine and the corresponding side chain amine
-
-
?
kinetin + H2O
hypoxanthine + 1-furan-2-ylmethaneamine
show the reaction diagram
P53909
2.6% of the activity of adenine
-
-
ir
kinetin + H2O
hypoxanthine + 1-furan-2-ylmethaneamine
show the reaction diagram
Q9P6I7, -
2.8% of the activity of adenine
-
-
ie
kinetin + H2O
hypoxanthine + 1-furan-2-ylmethaneamine
show the reaction diagram
Saccharomyces cerevisiae 23344c
P53909
2.6% of the activity of adenine
-
-
ir
m-topolin + H2O
hypoxanthine + 2-(aminomethyl)phenol
show the reaction diagram
P53909
2.5% of the activity of adenine
-
-
ir
N6-(2-isopentenyl)adenine + H2O
?
show the reaction diagram
Q9P6I7, -
partial conversion, at endo-side of N6 amino groups, release of N6-side chain amines
-
-
?
N6-(2-isopentenyl)adenine + H2O
?
show the reaction diagram
Q9P6I7, -
hydrolysis of adenine compounds, low activity towards N6-substituted adenines, partial conversion, release of N6-side chain amines
-
-
?
N6-(2-isopentenyl)adenine + H2O
hypoxanthine + 3-methylbut-2-en-1-amine
show the reaction diagram
P53909
partial conversion, at endo-side of N6 amino groups, release of N6-side chain amines, hydrolysis of adenine compounds, low activity towards N6-substituted adenines, partial conversion, release of N6-side chain amines
-
-
?
N6-isopentenyladenine + H2O
hypoxanthine + 3-methylbut-3-en-1-amine
show the reaction diagram
P53909
2.1% of the activity of adenine
-
-
ir
N6-isopentenyladenine + H2O
hypoxanthine + 3-methylbut-3-en-1-amine
show the reaction diagram
Q9P6I7, -
2.9% of the activity of adenine
-
-
ir
m-topolin + H2O
hypoxanthine + 2-(aminomethyl)phenol
show the reaction diagram
Q9P6I7, -
4.0% of the activity of adenine
-
-
ir
additional information
?
-
Q8X1T6
no substrate: adenosine
-
-
-
additional information
?
-
-
gene AAH1 is tightly downregulated upon cell entry into the non-proliferating state/quiescence, which is induced by nutrient limitations, the Srb10p cyclin-dependent kinase and its cyclin, Srb11p, regulate AAH1 expression at the transcriptional level, while Saf1p, a previously uncharacterized F-box protein, acts at a post-transcriptional level by promoting degradation of Aah1p, Aah1p expression is controlled by the RAS cAMP pathway, overview
-
-
-
additional information
?
-
Q9P6I7, -
the protein exhibits partial amino acid sequence similarity to the CHASE domain of the cytokinin receptor, which may account for its ability to bind and hydrolyse not only kinetin, but also other cytokinins and other cytokinin derivatives, albeit at lower rates than its natural substrate adenine
-
-
-
additional information
?
-
Saccharomyces cerevisiae BY4742
-
gene AAH1 is tightly downregulated upon cell entry into the non-proliferating state/quiescence, which is induced by nutrient limitations, the Srb10p cyclin-dependent kinase and its cyclin, Srb11p, regulate AAH1 expression at the transcriptional level, while Saf1p, a previously uncharacterized F-box protein, acts at a post-transcriptional level by promoting degradation of Aah1p, Aah1p expression is controlled by the RAS cAMP pathway, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-chloropurine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Q9P6I7, -
-
-
-
ir
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
P53909
-
-
-
ir
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
P53909
irreversible deamination, metabolic salvage pathway of purines
-
-
i
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Q9P6I7, -
irreversible deamination, metabolic salvage pathway of purines
-
-
i
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
-
-
-
-
adenine + H2O
?
show the reaction diagram
-
anaerobic conversion
-
-
-
adenine + H2O
?
show the reaction diagram
-
purine salvage pathway and nitrogen metabolism
-
-
-
adenine + H2O
?
show the reaction diagram
-
purine salvage pathway and nitrogen metabolism
-
-
-
adenine + H2O
?
show the reaction diagram
Streptomyces sp. J-350P
-
-
-
-
-
adenine + H2O
hypoxanthine + NH3
show the reaction diagram
Saccharomyces cerevisiae 23344c
P53909
-
-
-
ir
kinetin + H2O
?
show the reaction diagram
P53909
release of hypoxanthine and inosine, release of amine from from the cytokinine side chain
-
-
?
N6-(2-isopentenyl)adenine + H2O
?
show the reaction diagram
Q9P6I7, -
partial conversion, at endo-side of N6 amino groups, release of N6-side chain amines
-
-
?
N6-(2-isopentenyl)adenine + H2O
hypoxanthine + 3-methylbut-2-en-1-amine
show the reaction diagram
P53909
partial conversion, at endo-side of N6 amino groups, release of N6-side chain amines
-
-
?
kinetin + H2O
?
show the reaction diagram
Q9P6I7, -
release of hypoxanthine and inosine, release of amine from from the cytokinine side chain
-
-
?
additional information
?
-
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
-
gene AAH1 is tightly downregulated upon cell entry into the non-proliferating state/quiescence, which is induced by nutrient limitations, the Srb10p cyclin-dependent kinase and its cyclin, Srb11p, regulate AAH1 expression at the transcriptional level, while Saf1p, a previously uncharacterized F-box protein, acts at a post-transcriptional level by promoting degradation of Aah1p, Aah1p expression is controlled by the RAS cAMP pathway, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no dialyzable cofactors required
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
11% of the activity with Mn2+
Fe2+
-
48% of the activity with Mn2+
Fe2+
-
reducing [FeIII/FeIII]-ADE with dithionite restores the deaminase activity
Fe3+
-
[FeII/FeII]-ADE is oxidized to [FeIII/FeIII]-ADE with ferricyanide with inactivation of the deaminase activity
Mn2+
-
required for activity
Zn2+
-
required for activity
Mn2+
-
required, optimal at 1-5 mM, inhibitory above
additional information
-
the apo-enzyme is prepared and reconstituted with Fe2+, Zn2+, or Mn2+. In each case, two enzyme-equivalents of metal are necessary for reconstitution of the deaminase activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2'-Deoxycoformycin
-
-
3-methyl-1-phenyl-2-(phenylseleno)oct-2-en-1-one
-
an inhibition of ADA activity using 100 nM is observed, an increase in cellular viability is shown when 0.03 mM is used
-
4-Aminopyrazolo[3,4-d]pyrimidine
-
-
6-Chloropurine
-
-
6-Dimethylaminopurine
-
-
6-Methylaminopurine
-
-
hypoxanthine
-
competitive, Ki 4 mM
Mercuric acetate
-
-
Mercuric chloride
-
-
Mn2+
-
required, activation at 1-5 mM, inhibitory above
Monoiodoacetic acid
-
-
p-chloromercuribenzoate
-
-
purine
-
61% at 0.5 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
0.14
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
0.29
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
1.1
-
2,6-Diaminopurine
-
-
1
-
2-amino-6-chloropurine
-
-
1.5
-
2-hydroxy-6-aminopurine
-
-
0.5
-
6-bromopurine
-
-
0.026
-
6-Chloropurine
-
pH and temperature not specified in the publication
0.056
-
6-Chloropurine
-
pH and temperature not specified in the publication
0.26
-
6-Chloropurine
-
pH and temperature not specified in the publication
1
-
6-Chloropurine
-
-
0.13
-
6-methoxypurine
-
pH and temperature not specified in the publication
0.14
-
6-methoxypurine
-
pH and temperature not specified in the publication
0.16
-
6-methoxypurine
-
pH and temperature not specified in the publication
0.27
-
6-methoxypurine
-
pH and temperature not specified in the publication
0.0154
-
adenine
-
pH 7.0, 25C
0.025
-
adenine
-
pH and temperature not specified in the publication
0.032
-
adenine
Q9P6I7, -
; 0.2 M phosphate buffer, 33C
0.05
-
adenine
-
whole cells and cell extracts
0.055
-
adenine
P53909
; 0.2 M phosphate buffer, 33C
0.17
-
adenine
-
pH and temperature not specified in the publication
0.2
-
adenine
-
pH and temperature not specified in the publication
0.23
-
adenine
-
pH 7.5, 30C, wild-type Zn/Zn-ADE
0.29
-
adenine
Q8X1T6
pH 7.4, 35C
0.3
-
adenine
-
pH 7.5, 30C, wild-type Mn/Mn-ADE
0.31
-
adenine
-
mutant D474N, pH 7.5, 30C
0.32
-
adenine
-
mutant D285A, pH 7.5, 30C; mutant H214Q, pH 7.5, 30C; mutant H473N, pH 7.5, 30C
0.33
-
adenine
-
pH 7.5, 30C, wild-type Fe/Fe-ADE
0.35
-
adenine
-
mutant D118N, pH 7.5, 30C; mutant H90N, pH 7.5, 30C
0.37
-
adenine
-
mutant H214N, pH 7.5, 30C
0.38
-
adenine
-
mutant H92D, pH 7.5, 30C
0.4
-
adenine
-
mutant H90Q, pH 7.5, 30C
0.41
-
adenine
-
mutant E236Q, pH 7.5, 30C
0.42
-
adenine
-
mutant H92N, pH 7.5, 30C
0.44
-
adenine
-
mutant E121Q, pH 7.5, 30C; mutant H90D, pH 7.5, 30C
0.45
-
adenine
-
mutant H92C, pH 7.5, 30C
0.47
-
adenine
-
mutant H120N, pH 7.5, 30C; mutant S95A, pH 7.5, 30C
0.48
-
adenine
-
mutant H235D, pH 7.5, 30C; mutant H92Q, pH 7.5, 30C
0.51
-
adenine
-
mutant H90C, pH 7.5, 30C
0.8
-
adenine
-
pH 7.5, 37C
0.8
-
adenine
-
mutant H235Q, pH 7.5, 30C
0.82
-
adenine
-
mutant H235N, pH 7.5, 30C
0.86
-
adenine
-
mutant D284A, pH 7.5, 30C
1.1
1.4
adenine
-
-
1.2
-
adenine
-
mutant H235C, pH 7.5, 30C
1.6
-
adenine
-
mutant E185Q, pH 7.5, 30C
1.7
2
adenine
-
-
2
2.2
adenine
-
-
0.088
-
N-6-methyladenine
-
pH and temperature not specified in the publication
0.09
-
N-6-methyladenine
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.8
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
6.9
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
17
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
0.42
-
6-Chloropurine
-
pH and temperature not specified in the publication
0.84
-
6-Chloropurine
-
pH and temperature not specified in the publication
1.9
-
6-Chloropurine
-
pH and temperature not specified in the publication
0.52
-
6-methoxypurine
-
pH and temperature not specified in the publication
1.9
-
6-methoxypurine
-
pH and temperature not specified in the publication
2.2
-
6-methoxypurine
-
pH and temperature not specified in the publication
7.1
-
6-methoxypurine
-
pH and temperature not specified in the publication
0.022
-
adenine
-
mutant D284A, pH 7.5, 30C
0.036
-
adenine
-
mutant H90D, pH 7.5, 30C
0.05
-
adenine
-
mutant H92N, pH 7.5, 30C
0.053
-
adenine
-
mutant H90C, pH 7.5, 30C
0.06
-
adenine
-
mutant E185Q, pH 7.5, 30C
0.072
-
adenine
-
mutant E236Q, pH 7.5, 30C
0.08
-
adenine
-
mutant H92Q, pH 7.5, 30C
0.13
-
adenine
-
mutant H120N, pH 7.5, 30C
0.5
-
adenine
-
mutant H214N, pH 7.5, 30C; mutant H235N, pH 7.5, 30C
0.69
-
adenine
-
mutant H92C, pH 7.5, 30C
0.8
-
adenine
-
mutant H90Q, pH 7.5, 30C; mutant H92D, pH 7.5, 30C
1.2
-
adenine
-
mutant H235D, pH 7.5, 30C
1.3
-
adenine
-
mutant H214Q, pH 7.5, 30C; mutant H235Q, pH 7.5, 30C
1.5
-
adenine
-
mutant H235C, pH 7.5, 30C
2
-
adenine
-
wild-type, pH 7.5, 30C
3
6
adenine
-
pH and temperature not specified in the publication
5.5
-
adenine
P53909
; 0.067 mM adenine in 0.2 M phosphate buffer, 33C, pH 7.0
8
-
adenine
-
mutant H90N, pH 7.5, 30C
13.4
-
adenine
Q9P6I7, -
;
16.75
-
adenine
-
pH 7.0, 25C
37
-
adenine
-
mutant D285A, pH 7.5, 30C
56
-
adenine
-
pH and temperature not specified in the publication
57
-
adenine
-
mutant E121Q, pH 7.5, 30C
61
-
adenine
-
pH and temperature not specified in the publication
62
-
adenine
-
pH and temperature not specified in the publication
78
-
adenine
-
mutant S95A, pH 7.5, 30C
123
-
adenine
-
pH 7.5, 30C, wild-type Zn/Zn-ADE
171
-
adenine
-
mutant D474N, pH 7.5, 30C
173
-
adenine
-
mutant D118N, pH 7.5, 30C
178
-
adenine
-
mutant H473N, pH 7.5, 30C
185
-
adenine
-
pH 7.5, 30C, wild-type Mn/Mn-ADE
196
-
adenine
-
pH 7.5, 30C, wild-type Fe/Fe-ADE
200
-
adenine
-
wild-type, pH 7.5, 30C, + Fe sequestered with a metal chelator, growth medium supplemented with Mn2+ prior to induction
0.48
-
N-6-methyladenine
-
pH and temperature not specified in the publication
1.28
-
N-6-methyladenine
-
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
19
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
1972
24
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
1972
28
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
1972
120
-
2,6-Diaminopurine
-
pH and temperature not specified in the publication
1972
7.3
-
6-Chloropurine
-
pH and temperature not specified in the publication
5626
9.6
-
6-Chloropurine
-
pH and temperature not specified in the publication
5626
15
-
6-Chloropurine
-
pH and temperature not specified in the publication
5626
16
-
6-Chloropurine
-
pH and temperature not specified in the publication
5626
4
-
6-methoxypurine
-
pH and temperature not specified in the publication
144008
12
-
6-methoxypurine
-
pH and temperature not specified in the publication
144008
17
-
6-methoxypurine
-
pH and temperature not specified in the publication
144008
26
-
6-methoxypurine
-
pH and temperature not specified in the publication
144008
0.026
-
adenine
-
mutant D284A, pH 7.5, 30C
6389
0.038
-
adenine
-
mutant E185Q, pH 7.5, 30C
6389
0.082
-
adenine
-
mutant H90D, pH 7.5, 30C
6389
0.103
-
adenine
-
mutant H90C, pH 7.5, 30C
6389
0.119
-
adenine
-
mutant H92N, pH 7.5, 30C
6389
0.166
-
adenine
-
mutant H92Q, pH 7.5, 30C
6389
0.17
-
adenine
-
mutant E236Q, pH 7.5, 30C
6389
0.361
-
adenine
-
mutant H120N, pH 7.5, 30C
6389
0.609
-
adenine
-
mutant H235N, pH 7.5, 30C
6389
1.3
-
adenine
-
mutant H214N, pH 7.5, 30C; mutant H235C, pH 7.5, 30C
6389
1.4
-
adenine
-
mutant H92C, pH 7.5, 30C
6389
1.6
-
adenine
-
mutant H235Q, pH 7.5, 30C
6389
2
-
adenine
-
mutant H90Q, pH 7.5, 30C
6389
2.1
-
adenine
-
mutant H92D, pH 7.5, 30C
6389
2.5
-
adenine
-
mutant H235D, pH 7.5, 30C; wild-type, pH 7.5, 30C
6389
4
-
adenine
-
mutant H214Q, pH 7.5, 30C
6389
22
-
adenine
-
mutant H90N, pH 7.5, 30C
6389
130
-
adenine
-
mutant D285A, pH 7.5, 30C; mutant E121Q, pH 7.5, 30C
6389
160
-
adenine
-
mutant S95A, pH 7.5, 30C
6389
310
-
adenine
-
pH and temperature not specified in the publication
6389
330
-
adenine
-
pH and temperature not specified in the publication
6389
500
-
adenine
-
wild-type, pH 7.5, 30C, + Fe sequestered with a metal chelator, growth medium supplemented with Mn2+ prior to induction
6389
540
-
adenine
-
pH 7.5, 30C, wild-type Zn/Zn-ADE
6389
550
-
adenine
-
mutant D474N, pH 7.5, 30C
6389
560
-
adenine
-
mutant D118N, pH 7.5, 30C; mutant H473N, pH 7.5, 30C
6389
590
-
adenine
-
pH 7.5, 30C, wild-type Fe/Fe-ADE
6389
610
-
adenine
-
pH 7.5, 30C, wild-type Mn/Mn-ADE
6389
1400
-
adenine
-
pH and temperature not specified in the publication
6389
3100
-
adenine
-
pH and temperature not specified in the publication
6389
1.3
-
N-6-methyladenine
-
pH and temperature not specified in the publication
324858
1.6
-
N-6-methyladenine
-
pH and temperature not specified in the publication
324858
5.3
-
N-6-methyladenine
-
pH and temperature not specified in the publication
324858
15
-
N-6-methyladenine
-
pH and temperature not specified in the publication
324858
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0231
-
2'-Deoxycoformycin
-
pH 7.0, 25C
0.00013
-
6-Chloropurine
-
pH 7.5, 30C
4
-
hypoxanthine
-
competitive
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.071
-
-
in crude extracts
5.97
-
-
pH 7.5, 37C
8.34
-
P53909
recombinant protein, adenine as substrate, 0.067 mM in 0.2 M phosphate buffer, 33C, pH 7.0, adenine most favoured substrate, also hydrolyzes N6-substituted adenines from the cytokinin group of plant hormones, reaction products identified by mass spectroscopy, relative reaction rates given
additional information
-
P53909
139 nkat/mg with substrate adenine
additional information
-
Q9P6I7, -
326 nkat/mg with substrate adenine; comparable molecular properties with mammalian enzymes, adenine most favoured substrate, also hydrolyzes N6-substituted adenines from the cytokinin group of plant hormones, reaction products identified by mass spectroscopy, relative reaction rates given
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
substrate: 2-amino-6-chloropurine
6.7
-
Q9P6I7, -
0.2 M phosphate buffer, 33C; assay at
7
7.5
-
medium at
7
-
-
enzyme not purified
7
-
-
substrate: adenine and 6-bromopurine
7
-
P53909
0.2 M phosphate buffer, 30-37C; assay at
7.5
-
-
substrate: 6-chloropurine, 6-iodopurine, 2,6-diaminopurine
7.6
-
-
assay at
9
-
-
Tris-HCl buffer at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8.5
-
pH 5: about 30% of maximal activity, pH 8.5: about 20% of maximal activity
6
8
-
potassium phosphate buffer, maximal activity pH 7
7
9
-
Tris-HCl buffer, maximal activity pH 9
7.5
9
-
glycine-NaOH buffer, maximal activity pH 7
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
37
P53909
0.2 M phosphate buffer, pH 7.0
33
-
Q9P6I7, -
0.2 M phosphate buffer, pH 6.7; assay at
35
-
P53909
ranges from 30-37C
37
-
-
assay at
40
-
-
enzyme not purified
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
37
P53909
determined at pH 7.0
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Streptomyces sp. J-350P
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Agrobacterium tumefaciens (strain C58 / ATCC 33970)
Agrobacterium tumefaciens (strain C58 / ATCC 33970)
Agrobacterium tumefaciens (strain C58 / ATCC 33970)
Arthrobacter aurescens (strain TC1)
Enterococcus faecalis (strain ATCC 700802 / V583)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37000
-
-
gel filtration
39630
-
P53909
calculated; deduced from sequence
40800
-
-
SDS-PAGE
41200
-
Q9P6I7, -
calculated; deduced from sequence
46000
-
P53909
SDS-PAGE
48000
-
Q9P6I7, -
SDS-PAGE
120000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
P53909
x * 46000, SDS-PAGE
?
Q9P6I7, -
x * 48000, SDS-PAGE
homodimer
-
2 * 60000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
X-ray structures of Pa0148 (Pseudomonas aeruginos) and AAur1117 (Arthrobacter aurescens) are determined and reveal nearly identical distorted (beta/alpha)8 barrels with a single zinc ion that is characteristic of members of the amidohydrolase superfamily
-
modeling of structure reveals (beta/alpha)8 barrel and amino acids H15, H17, H214, D295, E217 and H238 involved in catalytic mechanism
Q8X1T6
the three-dimensional structure of adenine deaminase from Agrobacterium tumefaciens (Atu4426) is determined by X-ray crystallography at 2.2 A resolution
-
X-ray structures of Pa0148 (Pseudomonas aeruginos) and AAur1117 (Arthrobacter aurescens) are determined and reveal nearly identical distorted (beta/alpha)8 barrels with a single zinc ion that is characteristic of members of the amidohydrolase superfamily
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
P53909
activity highest in potassium phosphate buffer, decreasing activity to 75% in Tris/HCl buffer and to 30% in MOPS buffer
additional information
-
Q9P6I7, -
activity highest in potassium phosphate buffer, decreasing activity to 75% in Tris/HCl buffer and to 30% in MOPS buffer
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
pH 7.0, potassium phosphate buffer, unstable
55
-
-
less than 10% loss of activity after 60 min
55
-
-
pH 6.5, 80% loss of activity after 60 min
65
-
-
20% loss of activity after 5 min
additional information
-
P53909
prolonged storage in solution, at -20C in presence of 50% glycerol, at -80C in presence of 10-20% glycerol
additional information
-
Q9P6I7, -
prolonged storage in solution, at -20C in presence of 50% glycerol, at -80C in presence of 10-20% glycerol
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dialysis, 24 h against 0.9% KCl, stable
-
bovine serum albumin protects against heat inactivation in dilute solutions
-
after dissolving the freeze-dried enzyme a significant decrease od activity is observed within 3-4 h
P53909
after dissolving the freeze-dried enzyme a significant decrease od activity is observed within 3-4 h
Q9P6I7, -
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, ammonium sulfate, for at least 2 months
-
4C, 10 mM phoshate buffer, pH7.5, 20 mM 2-mercaptoethanol, 1-2 weeks, minimal losses
-
activity of purified protein is stable for 1-2 weeks when stored at 4C at concentrations above 10 mg/ml with the addition of 20% (v/v) glycerol. Prolonged storage in solution is possible at -20C with 50% (v/v) glycerol and at -80C with 10-20% (v/v) glycerol or as freeze-dried powder
P53909
at 4C in potassium buffer above a concentration of 10 mg/ml and in presence of 20% glycerol stable for 1-2 weeks, prolonged storage in solution at -20C in presence of 50% glycerol and at -80C in presence of 10-20% glycerol, or as freeze-dried powder
P53909
activity of purified protein is stable for 1-2 weeks when stored at 4C at concentrations above 10 mg/ml with the addition of 20% (v/v) glycerol. Prolonged storage in solution is possible at -20C with 50% (v/v) glycerol and at -80C with 10-20% (v/v) glycerol or as freeze-dried powder
Q9P6I7, -
at 4C in potassium buffer above a concentration of 10 mg/ml and in presence of 20% glycerol stable for 1-2 weeks, prolonged storage in solution at -20C in presence of 50% glycerol and at -80C in presence of 10-20% glycerol, or as freeze-dried powder
Q9P6I7, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
His-tagged, recombinant protein
Q8X1T6
recombonant protein
-
gel filtration, SDS-PAGE; using Ni2+-nitrilotriacetate (Ni2+-NTA) column chromatography
P53909
gel filtration, SDS-PAGE; using Ni2+-nitrilotriacetate (Ni2+-NTA) column chromatography
Q9P6I7, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpression in Escherichia coli
-
expressed in Escherichia coli, pDrive, pet100/D-TOPO, pet151/D-TOPO vectors; overexpression in Escherichia coli BL21 (DE3)
P53909
expression in Escherichia coli
-
expressed in Escherichia coli, pDrive, pet100/D-TOPO, pet151/D-TOPO vectors; overexpression in Escherichia coli BL21 (DE3)
Q9P6I7, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Western blot analysis establishes that AAH is expressed in both life cycle stages of Leishmania donovani
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D118N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 173/sec
D284A
-
mutants is able to bind two equivalents of Mn2+ or Fe2+ in the active site but mutant is unable to catalyze the deaminase reaction
D285A
-
mutant is able to bind 2 metals per active site, kcat (adenine): 37/sec
D474N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 171/sec
E121Q
-
mutant is able to bind 2 metals per active site, kcat (adenine): 57/sec
E185Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
E236Q
-
mutants is able to bind two equivalents of Mn2+ or Fe2+ in the active site but mutant is unable to catalyze the deaminase reaction
H120N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 0.13/sec
H214N
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H214Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235C
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235D
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235N
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H473N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 178/sec
H90C
-
mutant is unable to bind either iron or manganese
H90D
-
mutant is unable to bind either iron or manganese
H90N
-
mutant is able to bind two equivalents of Mn2+ or Fe2+ per monomer and shows a kcat of about 5% of the wild-type enzyme
H90Q
-
mutant is unable to bind either iron or manganese
H92C
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H92D
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H92N
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H92Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
S95A
-
mutant is able to bind 2 metals per active site, kcat (adenine): 78/sec
additional information
-
isolation and analysis of three deletion mutants srb10, srb11 and saf1 (ybr280c) affecting AAH1 expression during post-diauxic growth and in early stationary phase, overview
additional information
Saccharomyces cerevisiae BY4742
-
isolation and analysis of three deletion mutants srb10, srb11 and saf1 (ybr280c) affecting AAH1 expression during post-diauxic growth and in early stationary phase, overview
-