EC number:2.4.2.1

Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.2 Pentosyltransferases
ID:2.4.2.1
Description:Purine-nucleoside phosphorylase.
Alternative Name: PNPase.
Inosine phosphorylase.
Prosite: PDOC00954; PDOC00946;
PDB:
PDBScop
1QE5 8032189; 8044567; 8032189; 8044567; 8032189; 8044567;
1C3X 8032189; 8044567; 8032189; 8044567; 8032189; 8044567;
1LVU 8032188; 8044566; 8032188; 8044566; 8032188; 8044566; 8032188; 8044566; 8032188; 8044566; 8032188; 8044566;
1LV8 8032188; 8044566; 8032188; 8044566; 8032188; 8044566; 8032188; 8044566; 8032188; 8044566; 8032188; 8044566;
3FUC 8032188; 8044566; 8032188; 8044566; 8032188; 8044566;
 » show all
Cath: 3.40.50.1580;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.2.1
BRENDA Enzyme Link: BRENDA 2.4.2.1
KEGG Enzyme Link: KEGG2.4.2.1
BioCyc Enzyme Link: BioCyc 2.4.2.1
ExPASy Enzyme Link: ExPASy2.4.2.1
EC2PDB Enzyme Link: EC2PDB 2.4.2.1
ExplorEnz Enzyme Link: ExplorEnz 2.4.2.1
PRIAM enzyme-specific profiles Link: PRIAM 2.4.2.1
IntEnz Enzyme Link: IntEnz 2.4.2.1
MEDLINE Enzyme Link: MEDLINE 2.4.2.1

EC number:2.4.2.1

MSA:

2.4.2.1;
Phylogenetic Tree:

2.4.2.1;
Uniprot:
M-CSA:
RHEA:13233 guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4](:[*:5]):[*:6].[*:7]-[OH;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:8]-[*:7].[*:5]:[nH;+0:4]:[*:6]
Reaction
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References

TitleAuthorsDatePubMed ID
Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.Sévin DC, Fuhrer T, Zamboni N, Sauer U2017 Feb27941785
RHEA:19805 a purine ribonucleoside + phosphate = a purine base + alpha-D-ribose 1-phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]:[n;H0;+0:4](:[*:5])-[CH;+0:6](-[*:7])-[*:8]>>[*:7]-[CH;+0:6](-[*:8])-[O;H0;+0:2]-[*:1].[*:3]:[nH;+0:4]:[*:5]
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References

TitleAuthorsDatePubMed ID
Purine nucleoside phosphorylase from human erythrocytes. IV. Crystallization and some properties.Agarwal RP, Parks RE Jr1969 Feb 255768862
Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.Sévin DC, Fuhrer T, Zamboni N, Sauer U2017 Feb27941785
RHEA:27638 phosphate + xanthosine = alpha-D-ribose 1-phosphate + xanthine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]:[n;H0;+0:4](:[*:5])-[CH;+0:6](-[*:7])-[*:8]>>[*:7]-[CH;+0:6](-[*:8])-[O;H0;+0:2]-[*:1].[*:3]:[nH;+0:4]:[*:5]
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References

TitleAuthorsDatePubMed ID
Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.Sévin DC, Fuhrer T, Zamboni N, Sauer U2017 Feb27941785
RHEA:27642 adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]:[n;H0;+0:4](:[*:5])-[CH;+0:6](-[*:7])-[*:8]>>[*:7]-[CH;+0:6](-[*:8])-[O;H0;+0:2]-[*:1].[*:3]:[nH;+0:4]:[*:5]
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References

TitleAuthorsDatePubMed ID
Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.Sévin DC, Fuhrer T, Zamboni N, Sauer U2017 Feb27941785
RHEA:27646 inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4]1:[*:5]:[*:6](:[c;H0;+0:7](-[OH;+0:8]):[n;H0;+0:9]:[*:10]):[n;H0;+0:11]:[*:12]:1.[*:13]-[OH;+0:14]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:14]-[*:13].[*:10]:[nH;+0:9]:[c;H0;+0:7](=[O;H0;+0:8]):[*:6]1:[*:5]:[n;H0;+0:4]:[*:12]:[nH;+0:11]:1
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References

TitleAuthorsDatePubMed ID
Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.Sévin DC, Fuhrer T, Zamboni N, Sauer U2017 Feb27941785
RHEA:27738 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4](:[*:5]):[*:6].[*:7]-[OH;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:8]-[*:7].[*:5]:[nH;+0:4]:[*:6]
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RHEA:27742 2'-deoxyadenosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + adenine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]:[n;H0;+0:4](:[*:5])-[CH;+0:6](-[*:7])-[*:8]>>[*:7]-[CH;+0:6](-[*:8])-[O;H0;+0:2]-[*:1].[*:3]:[nH;+0:4]:[*:5]
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RHEA:27750 2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + hypoxanthine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4]1:[*:5]:[*:6]:[n;H0;+0:7]:[*:8]:1.[*:9]-[OH;+0:10]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:10]-[*:9].[*:5]1:[*:6]:[nH;+0:7]:[*:8]:[n;H0;+0:4]:1
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RHEA:36431 2-deoxy-N-D-ribosylpurine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + purine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4]1:[*:5]:[*:6]:[n;H0;+0:7]:[*:8]:1.[*:9]-[OH;+0:10]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:10]-[*:9].[*:5]1:[*:6]:[nH;+0:7]:[*:8]:[n;H0;+0:4]:1
Reaction
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References

TitleAuthorsDatePubMed ID
Purification and characterization of purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-2.Hamamoto T, Noguchi T, Midorikawa Y1996 Jul8782414
Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus.Saunders PP, Wilson BA, Saunders GF1969 Jul 104978445
[Phosphorolysis and hydrolysis of purine ribosides by enzymes from yeast].HEPPEL LA, HILMOE RJ1952 Oct12999785
A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus.Cacciapuoti G, Forte S, Moretti MA, Brio A, Zappia V, Porcelli M2005 Apr15819883
Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism.Koellner G, Bzowska A, Wielgus-Kutrowska B, Luić M, Steiner T, Saenger W, Stepiński J2002 Jan 1811786017