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Information on EC 3.2.2.1 - purine nucleosidase
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3.2.2.1 purine nucleosidaseIUBMB Comments
The enzyme from the bacterium Ochrobactrum anthropi specifically catalyses the irreversible N-riboside hydrolysis of purine nucleosides. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not substrates .
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Word Map
- 3.2.2.1
-
salvage
- trypanosoma
- vivax
-
crithidia
- fasciculata
-
pyrimidine-specific
-
n-glycosidic
- iminoribitols
- parkin
-
schramm
- formycin
-
horenstein
-
trypanocidal
- pharmacology
- drug development
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
purine nucleosidase, iag-nh, iu-nucleoside hydrolase, iagnh, ribonucleoside hydrolase, ssiag-nh, iag-nucleoside hydrolase, purine nucleoside hydrolase, purine-specific inosine-adenosine-guanosine nucleoside hydrolase, purine-specific nh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
inosine-adenosine-guanosine-preferring nucleoside hydrolase
-
IAG nucleoside hydrolase
-
-
-
-
IU-nucleoside hydrolase
-
-
-
-
N-ribosyl purine ribohydrolase
-
-
-
-
N-ribosyl-purine ribohydrolase
-
-
-
-
nucleosidase
-
-
-
-
nucleosidase g
-
-
-
-
nucleoside hydrolase
-
-
-
-
purine beta-ribosidase
-
-
-
-
Purine nucleosidase
-
-
-
-
purine nucleoside hydrolase
-
-
-
-
purine ribonucleosidase
-
-
-
-
purine-specific hydrolase
-
-
-
-
ribonucleoside hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
purine-nucleoside ribohydrolase
The enzyme from the bacterium Ochrobactrum anthropi specifically catalyses the irreversible N-riboside hydrolysis of purine nucleosides. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not substrates [6].
CAS REGISTRY NUMBER
COMMENTARY
9025-44-9
-
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
4-nitrophenyl beta-D-ribofuranoside + H2O
4-nitrophenol + D-ribose
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R,4S)-1-[(4-amino-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
-
(2R,3R,4S)-1-[(4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidin-3,4-diol
nanomolar inhibitor
(2R,3R,4S)-2-(hydroxymethyl)-1-(4-nitrobenzyl)pyrrolidine-3,4-diol
-
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidin-3,4-diol
nanomolar inhibitor
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidine-3,4-diol
-
(2S,3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
nanomolar inhibitor
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-1,2,3-benzotriazol-5-yl)methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-benzimidazol-2-yl)methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(2-amino-4-benzothiazoyl)-methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(4-amino-2-methylquinolin-8-yl)methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(4-aminothieno[3,2-d]pyrimidin-7-yl)-methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(4-chloro-2-methylquinolin-8-yl)methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(4-methyl-2-phenylpyrimidin-5-yl)methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(7-thieno[3,2-d]pyrimidonyl)-methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-(thieno[3,2-d]pyrimidin-7-yl)methyl-D-ribitol
-
1,4-dideoxy-1,4-imino-N-[4-(1H-1,2,4-triazol-1-yl)benzyl]-D-ribitol
-
1-[2-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]ethyl]guanidine
-
1-[3-[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]propyl]guanidine
-
7-[[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
-
immucillin H
immucilin H is (1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
immucillin H
immucillin H is (1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
2-aminopurine riboside
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.0005
7-methyl guanosine
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.0018
guanosine
mutant enzyme D253P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.0023
guanosine
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.003
guanosine
mutant enzyme E249P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.004
guanosine
mutant enzyme C248P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.008
guanosine
mutant enzyme H247P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.016
guanosine
mutant enzyme L250P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.021
guanosine
mutant enzyme L251P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
0.024
guanosine
mutant enzyme R252P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.57
2-aminopurine riboside
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.07
7-methyl guanosine
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.09
guanosine
mutant enzyme C248P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.4
guanosine
mutant enzyme L250P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
1.7
guanosine
mutant enzyme E249P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
2.3
guanosine
wild type enzyme, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
2.5
guanosine
mutant enzyme L251P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
3.9
guanosine
mutant enzyme D253P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
4.1
guanosine
mutant enzyme H247P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
13
guanosine
mutant enzyme R252P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000041
(2R,3R,4S)-1-[(4-amino-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0000044
(2R,3R,4S)-1-[(4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidin-3,4-diol
-
0.0043
(2R,3R,4S)-2-(hydroxymethyl)-1-(4-iodobenzyl)pyrrolidine-3,4-diol
-
0.0075
(2R,3R,4S)-2-(hydroxymethyl)-1-(4-nitrobenzyl)pyrrolidine-3,4-diol
-
0.0000108
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidin-3,4-diol
-
0.0000108
(2R,3R,4S)-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidine-3,4-diol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.253
(2R,3R,4S,5S)-2-(hydroxymethyl)-5-phenylpyrrolidine-3,4-diol
-
0.0000041
(2S,3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidine-3,4-diol
-
0.00075
1,4-dideoxy-1,4-imino-N-(1-isoquinolinyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00072
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-1,2,3-benzotriazol-5-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0021
1,4-dideoxy-1,4-imino-N-(1-methyl-1H-benzimidazol-2-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.187
1,4-dideoxy-1,4-imino-N-(2(1H)-quinolon-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00004
1,4-dideoxy-1,4-imino-N-(2-amino-4-benzothiazoyl)-methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.12
1,4-dideoxy-1,4-imino-N-(2-aminopyridin-3-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00836
1,4-dideoxy-1,4-imino-N-(2-aminoquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000314
1,4-dideoxy-1,4-imino-N-(2-chloroquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.001258
1,4-dideoxy-1,4-imino-N-(2-methoxyquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.002
1,4-dideoxy-1,4-imino-N-(2-naphthyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00018
1,4-dideoxy-1,4-imino-N-(2-quinolinyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0038
1,4-dideoxy-1,4-imino-N-(3-cyanobenzyl)-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.012
1,4-dideoxy-1,4-imino-N-(3-indolyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0023
1,4-dideoxy-1,4-imino-N-(3-nitrobenzyl)-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.02
1,4-dideoxy-1,4-imino-N-(3-quinolinyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0131
1,4-dideoxy-1,4-imino-N-(4(1H)-quinolon-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0713
1,4-dideoxy-1,4-imino-N-(4-amino-2-methylquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000015
1,4-dideoxy-1,4-imino-N-(4-aminoquinazolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00005
1,4-dideoxy-1,4-imino-N-(4-aminoquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000019
1,4-dideoxy-1,4-imino-N-(4-aminothieno[3,2-d]pyrimidin-7-yl)-methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000369
1,4-dideoxy-1,4-imino-N-(4-chloro-2-methylquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000014
1,4-dideoxy-1,4-imino-N-(4-chloroquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.026
1,4-dideoxy-1,4-imino-N-(4-cyanobenzyl)-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000029
1,4-dideoxy-1,4-imino-N-(4-methoxyquinolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.043
1,4-dideoxy-1,4-imino-N-(4-methyl-2-phenylpyrimidin-5-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.02
1,4-dideoxy-1,4-imino-N-(4-pyridinyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.029
1,4-dideoxy-1,4-imino-N-(4-quinolinyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.032
1,4-dideoxy-1,4-imino-N-(6-methoxypyridin-3-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0023
1,4-dideoxy-1,4-imino-N-(7-methoxy-indol-3-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00072
1,4-dideoxy-1,4-imino-N-(7-quinolinyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.00002
1,4-dideoxy-1,4-imino-N-(7-thieno[3,2-d]pyrimidonyl)-methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.001
1,4-dideoxy-1,4-imino-N-(8-hydroxyquinolin-2-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0000108
1,4-dideoxy-1,4-imino-N-(8-quinolinyl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000058
1,4-dideoxy-1,4-imino-N-(quinazolin-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000109
1,4-dideoxy-1,4-imino-N-(quinazolon-8-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000139
1,4-dideoxy-1,4-imino-N-(quinoxalin-5-yl)-methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000042
1,4-dideoxy-1,4-imino-N-(thieno[3,2-d]pyrimidin-7-yl)methyl-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0034
1,4-dideoxy-1,4-imino-N-[3-(1H-pyrrol-1-yl)benzyl]-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0012
1,4-dideoxy-1,4-imino-N-[4-(1H-pyrazol-1-yl)benzyl]-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.001
1,4-dideoxy-1,4-imino-N-[4-(1H-pyrrol-1-yl)benzyl]-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.018
1-[2-[(2S,3S,4R,5R)-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-2-yl]ethyl]guanidine
-
0.04
1-[3-[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]propyl]guanidine
-
0.0000044
7-[[(2R,3R,4S)-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-yl]methyl]-3,5-dihydro-4H-pyrrolo[3,2-d]pyrimidin-4-one
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0000041
N-(9-deaza-adenin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0000044
N-(9-deazahypoxanthin-9-yl)methyl-1,4-dideoxy-1,4-imino-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.000063
1,4-dideoxy-1,4-imino-N-[4-(1H-1,2,4-triazol-1-yl)benzyl]-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
0.0012
1,4-dideoxy-1,4-imino-N-[4-(1H-1,2,4-triazol-1-yl)benzyl]-D-ribitol
in 50 mM phosphate buffer, pH 7.0, at 35°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, unliganded structure and 3-deaza-adenosine complex
in complex with immucillin H, hanging drop vapour diffusion method, with 20% polyethylene glycol 4000 and 0.25 M ammonium sulfate in 10 mM potassium acetate, pH 5.0
in complex with inhibitors, hanging drop vapour diffusion method, using 25% (w/v) PEG 3350 in 100 mM Bis-Tris buffer pH 6.5 and 0.2 M MgCl2
molecular mechanics and dynamics simulations. The ribose release process can be divided into ribose dissociation and ribose release steps The ribose dissociation includes cleavage and exchange stages, in which a metastable 6fold intermediate will recover to an 8fold coordination shell of Ca2+ . The estimated barrier for the rate-determining step of the entire reaction is 13.0 kcal/mol, which is comparable to the experimental value of 16.7 kcal/mol. The gating mechanism arising from loop1 and loop2, as well as key residues around the active pocket, plays an important role in manipulating the ribose release
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C248P
mutant shows decreased kcat value compared to the wild type enzyme using guanosine as substrate
D253P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
E249P
mutant shows decreased kcat value compared to the wild type enzyme using guanosine as substrate
H247P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
L250P
mutant shows decreased kcat value compared to the wild type enzyme using guanosine as substrate
L251P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
R252P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
additional information
the loop deletion mutant 3G hydrolyzes guanosine and 2-aminopurine riboside with a turnover comparable to that of the wild type, but an increase in Km is observed for both substrates, 7-methyl guanosine is hydrolyzed even faster by 3G compared with the wild type and hardly any difference is observed in the Km
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
once thawed, enzyme stocks are kept at 4°C and used over a period of several days but never refrozen to avoid activity loss
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex-200 gel filtration
Ni-NTA column chromatography and Superdex-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli WK6 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Versees, W.; Decanniere, K.; Pelle, R.; Depoorter, J.; Brosens, E.; Parkin, D.W.; Steyaert, J.
Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax
J. Mol. Biol.
307
1363-1379
2001
Trypanosoma vivax (Q9GPQ4), Trypanosoma vivax
Versees, W.; Goeminne, A.; Berg, M.; Vandemeulebroucke, A.; Haemers, A.; Augustyns, K.; Steyaert, J.
Crystal structures of T. vivax nucleoside hydrolase in complex with new potent and specific inhibitors
Biochim. Biophys. Acta
1794
953-960
2009
Trypanosoma vivax (Q9GPQ4)
Goeminne, A.; Berg, M.; McNaughton, M.; Bal, G.; Surpateanu, G.; Van der Veken, P.; De Prol, S.; Versees, W.; Steyaert, J.; Haemers, A.; Augustyns, K.
N-Arylmethyl substituted iminoribitol derivatives as inhibitors of a purine specific nucleoside hydrolase
Bioorg. Med. Chem.
16
6752-6763
2008
Trypanosoma vivax (Q9GPQ4), Trypanosoma vivax
Berg, M.; Bal, G.; Goeminne, A.; Van der Veken, P.; Versees, W.; Steyaert, J.; Haemers, A.; Augustyns, K.
Synthesis of bicyclic N-arylmethyl-substituted iminoribitol derivatives as selective nucleoside hydrolase inhibitors
ChemMedChem
4
249-260
2009
Trypanosoma vivax (Q9GPQ4)
Vandemeulebroucke, A.; De Vos, S.; Van Holsbeke, E.; Steyaert, J.; Versees, W.
A flexible loop as a functional element in the catalytic mechanism of nucleoside hydrolase from Trypanosoma vivax
J. Biol. Chem.
283
22272-22282
2008
Trypanosoma vivax (Q9GPQ4)
EXTERNAL LINKS (specific for EC-Number 3.2.2.1)
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