Literature summary for 3.5.4.4 extracted from

Larson, E.T.; Deng, W.; Krumm, B.E.; Napuli, A.; Mueller, N.; Van Voorhis, W.C.; Buckner, F.S.; Fan, E.; Lauricella, A.; DeTitta, G.; Luft, J.; Zucker, F.; Hol, W.G.; Verlinde, C.L.; Merritt, E.A.
Structures of substrate- and inhibitor-bound adenosine deaminase from a human malaria parasite show a dramatic conformational change and shed light on drug selectivity (2008), J. Mol. Biol., 381, 975-988.

Application

Application	Comment	Organism
drug development	Plasmodium parasites lack enzymes critical for de novo purine synthesis and thus rely on purine salvage to supply precursors for nucleic acid synthesis and energy metabolism. Thus, the purine salvage pathway is an attractive drug target	Plasmodium vivax

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli BL21(DE3)	Plasmodium vivax

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of adenosine deaminase from Plasmodium vivax in complex with inhibitor, 2-deoxycoformycin (pentostatin), 33% PEG 20000, 0.1 M TAPS (pH 9.0), 0.1 M Sodium phosphate (monobasic), 16% acetonitrile, 5 mM adenosine, pH 7.0, vapor diffusion, sitting drop, temperature 298K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular modeling, crystal structure of adenosine deaminase from Plasmodium vivax in complex with adenosine, space group C 2 2 21, X-ray diffraction structure determination and analysis at 1.89 A resolution, crystal structure of adenosine deaminase from Plasmodium vivax in complex with guanosine, 27.3% PEG 20000, 0.1 M CHES (pH 9.5), 0.1 M Sodium phosphate monobasic, 5 mM guanosine, vapor diffusion, sitting drop, temperature 293K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.19 A resolution, these structures highlight a drastic conformational change in plasmodial adenosine deaminase upon substrate binding, these complexes illuminate the structural basis for the differential substrate specificity and potential drug selectivity between mammalian and parasite enzymes	Plasmodium vivax

Crystallization (Comment)

Organism

crystal structure of adenosine deaminase from Plasmodium vivax in complex with inhibitor, 2-deoxycoformycin (pentostatin), 33% PEG 20000, 0.1 M TAPS (pH 9.0), 0.1 M Sodium phosphate (monobasic), 16% acetonitrile, 5 mM adenosine, pH 7.0, vapor diffusion, sitting drop, temperature 298K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular modeling, crystal structure of adenosine deaminase from Plasmodium vivax in complex with adenosine, space group C 2 2 21, X-ray diffraction structure determination and analysis at 1.89 A resolution, crystal structure of adenosine deaminase from Plasmodium vivax in complex with guanosine, 27.3% PEG 20000, 0.1 M CHES (pH 9.5), 0.1 M Sodium phosphate monobasic, 5 mM guanosine, vapor diffusion, sitting drop, temperature 293K, space group C 2 2 21, X-ray diffraction structure determination and analysis at 2.19 A resolution, these structures highlight a drastic conformational change in plasmodial adenosine deaminase upon substrate binding, these complexes illuminate the structural basis for the differential substrate specificity and potential drug selectivity between mammalian and parasite enzymes

Plasmodium vivax

Inhibitors

Inhibitors	Comment	Organism	Structure
2'-deoxycoformycin	-	Plasmodium vivax

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	-	Plasmodium vivax

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5'-methylthioadenosine + H2O	Plasmodium vivax	adenosine deaminase has a secondary function in recycling methylthiopurines from the polyamine biosynthetic pathway	5'-methylthioinosine + NH3	-	ir
adenosine + H2O	Plasmodium vivax	-	inosine + NH3	-	ir

Organism

Organism	UniProt	Comment	Textmining
Plasmodium vivax	A5KE01	-	-

Purification (Commentary)

Purification (Comment)	Organism
using immobilized metal-affinity chromatography on a Ni-NTA column followed by size-exclusion chromatography on a HiLoad Superdex 200 column	Plasmodium vivax

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
5'-methylthioadenosine + H2O	-	Plasmodium vivax	5'-methylthioinosine + NH3	-	ir
5'-methylthioadenosine + H2O	adenosine deaminase has a secondary function in recycling methylthiopurines from the polyamine biosynthetic pathway	Plasmodium vivax	5'-methylthioinosine + NH3	-	ir
adenosine + H2O	-	Plasmodium vivax	inosine + NH3	-	ir

Synonyms

Synonyms	Comment	Organism
ADA	-	Plasmodium vivax
adenosine deaminase	-	Plasmodium vivax
PvADA	-	Plasmodium vivax