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Information on EC 3.5.4.4 - adenosine deaminase and Organism(s) Gallus gallus and UniProt Accession Q5ZKP6

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IUBMB Comments
The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
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This record set is specific for:
Gallus gallus
UNIPROT: Q5ZKP6
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The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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adenosine
+
H2O
=
inosine
+
NH3
+
=
+
Synonyms
adenosine deaminase, adenosine deaminase 2, adenosine aminohydrolase, adenosine deaminase 1, adaii, pvada, mj1541, ciada, sco4901, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine deaminase
-
Adenosine aminohydrolase
-
-
-
-
adenosine deaminase 1
-
-
adenosine deaminase 2
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
adenosine aminohydrolase
The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-93-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
show the reaction diagram
-
-
-
ir
adenosine + H2O
inosine + NH3
show the reaction diagram
-
-
-
ir
2',3'-deoxyadenosine + H2O
2',3'-deoxyinosine + NH3
show the reaction diagram
-
1.7% of the activity with adenosine
-
-
?
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
show the reaction diagram
3'-deoxyadenosine + H2O
3'-deoxyinosine + NH3
show the reaction diagram
-
2.4% of the activity with adenosine
-
-
?
5'-AMP + H2O
5'-IMP + NH3
show the reaction diagram
-
1.4% of the activity with adenosine
-
-
?
adenosine + H2O
inosine + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
show the reaction diagram
-
-
-
ir
adenosine + H2O
inosine + NH3
show the reaction diagram
-
-
-
ir
additional information
?
-
-
the enzyme is involved in purine metabolism and plays an important role in the mechanism of the immune system
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
corticosterone
inhibits the adenosine deaminase activity in an age- and region-specific manner
2'-deoxycoformycin
erythro-9-(2-hydroxy-3-nonyl)-adenine hydrochloride
-
0.4 nM, 50% inhibition
additional information
-
no inhibition by erythro-9-(2-hydroxy-3-nonyl)-adenine hydrochloride
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dibutyryl-cAMP
causes a significant increase in the activity level of adenosine deaminase depending on the regions of the gastrointestinal tract
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.333
2'-deoxyadenosine
-
-
0.000023 - 0.144
adenosine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Babcock Venkateswara 380, BV 380 breed
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADA_CHICK
357
0
40679
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
gel filtration
42000
-
1 * 42000, enzyme exists as monomer, not in complex with dipeptidyl peptidase IV, SDS-PAGE
61000
-
2 * 61000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 61000, SDS-PAGE
monomer
-
1 * 42000, enzyme exists as monomer, not in complex with dipeptidyl peptidase IV, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
following treatment with N-glycosidase, the molecular weight changes from 61000 Da to 55000 Da
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iwaki-Egawa, S.; Watanabe, Y.
Characterization and purification of adenosine deaminase 1 from human and chicken liver
Comp. Biochem. Physiol. B
133
173-182
2002
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Iwaki-Egawa, S.; Namiki, C.; Watanabe, Y.
Adenosine deaminase 2 from chicken liver: purification, characterization, and N-terminal amino acid sequence
Comp. Biochem. Physiol. B
137
247-254
2004
Gallus gallus
Manually annotated by BRENDA team
Bhattacharjee, P.; Sharma, R.
Antithetical effects of corticosterone and dibutyryl cAMP on adenosine deaminase in the gastrointestinal tract of chicken during postnatal development
Mol. Cell. Biochem.
327
79-86
2009
Gallus gallus (Q5ZKP6), Gallus gallus
Manually annotated by BRENDA team