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Information on EC 3.5.4.4 - adenosine deaminase and Organism(s) Plasmodium falciparum and UniProt Accession Q8IJA9

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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:
Plasmodium falciparum
UNIPROT: Q8IJA9
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The taxonomic range for the selected organisms is: Plasmodium falciparum
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 aminohydrolase
-
-
-
-
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
5'-methylthioadenosine + H2O
5'-methylthioinosine + NH3
show the reaction diagram
-
-
-
ir
adenosine + H2O
inosine + NH3
show the reaction diagram
-
-
-
ir
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
show the reaction diagram
-
-
-
-
?
5'-methylthioadenosine + H2O
5'-methylthioinosine + NH3
show the reaction diagram
-
-
-
-
?
adenosine + H2O
inosine + NH3
show the reaction diagram
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
adenosine + H2O
inosine + NH3
show the reaction diagram
-
-
-
ir
5'-methylthioadenosine + H2O
5'-methylthioinosine + NH3
show the reaction diagram
-
-
-
-
?
adenosine + H2O
inosine + NH3
show the reaction diagram
-
adenosine deamination is involved in the essential pathway of purine salvage in Plasmodium falciparum, and inhibition of purine salvage results in parasite death
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxycoformycin
-
a natural product transition state analogue inhibitor
2,6-diaminopurine
-
-
5'-methylthio-2'-deoxycoformycin
-
-
5'-methylthiocoformycin
6-methylamino riboside
-
-
6-Methylmercaptopurine riboside
-
-
coformycin
cordycepin
-
-
D-coformycin
-
powerful picomolar inhibitor of ADA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0306 - 0.37605
5'-methylthioadenosine
0.00943 - 0.32206
adenosine
0.057
2'-deoxyadenosine
-
-
0.115
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
0.051 - 0.088
adenosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 14.07
5'-methylthioadenosine
0.31 - 7.45
adenosine
5.8
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
5.6
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 450
5'-methylthioadenosine
2 - 260
adenosine
50
5'-methylthioadenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
64
adenosine
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000079
5'-methylthio-2'-deoxycoformycin
-
-
0.00000043 - 0.0000032
5'-methylthiocoformycin
0.000014
D-coformycin
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
Plasmodium falciparum, a malarial pathogen, can only synthesize purine nucleotides employing a salvage pathway because it lacks de novo biosynthesis. Adenosine deaminase, one of the three purine salvage enzymes
metabolism
-
ADA is a key enzyme in the pathway of hypoxanthine formation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of a surface engineered adenosine deaminase at a resolution of 2.48 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C27Q/L227I
the mutation promotes crystallization via crystal packing and to prevents intermolecular disulfide bond formation. The surface engineered enzyme is kinetically comparable to the wild type enzyme
D176A
mutation reduces adenosine and 5'-methylthioadenosine substrate affnity
D176M
mutation reduces adenosine and 5'-methylthioadenosine substrate affnity
F136L
mutant enzyme shows increased Km (more than 10fold) for adenosine and 5'-methylthioinosine
T174A
mutation affects 5'-methylthioadenosine binding affinity
T174I
mutation affects 5'-methylthioadenosine binding affinity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
expression of His-tagged enzyme in Escherichia coli strain BL21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
-
Plasmodium falciparum-specific inhibitors of adenosine deaminase have potential for development as antimalarials without inhibition of host enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daddona, P.E.; Wiesmann, W.P.; Lambros, C.; Kelley, W.N.; Webster, H.K.
Human malaria parasite adenosine deaminase
J. Biol. Chem.
259
1472-1475
1984
Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
Tyler, P.C.; Taylor, E.A.; Froehlich, R.F.; Schramm, V.L.
Synthesis of 5-methylthio coformycins: specific inhibitors for malarial adenosine deaminase
J. Am. Chem. Soc.
129
6872-6879
2007
Bos taurus, Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
Ho, M.C.; Cassera, M.B.; Madrid, D.C.; Ting, L.M.; Tyler, P.C.; Kim, K.; Almo, S.C.; Schramm, V.L.
Structural and metabolic specificity of methylthiocoformycin for malarial adenosine deaminases
Biochemistry
48
9618-9626
2009
Plasmodium berghei, Plasmodium falciparum, Plasmodium gallinaceum, Plasmodium knowlesi, Plasmodium vivax, Plasmodium cynomolgi
Manually annotated by BRENDA team
Jaruwat, A.; Riangrungroj, P.; Ubonprasert, S.; Sae-Ueng, U.; Kuaprasert, B.; Yuthavong, Y.; Leartsakulpanich, U.; Chitnumsub, P.
Crystal structure of Plasmodium falciparum adenosine deaminase reveals a novel binding pocket for inosine
Arch. Biochem. Biophys.
667
6-13
2019
Homo sapiens (P00813), Homo sapiens, Plasmodium falciparum (Q8IJA9), Plasmodium falciparum
Manually annotated by BRENDA team