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Enzyme Name | UniProtKB | KEGG |
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| P55859 | P00491 | P81989 |
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Protein name | Purine nucleoside phosphorylase | Purine nucleoside phosphorylase | Purine nucleoside phosphorylase | purine-nucleoside phosphorylaseinosine phosphorylasePNPasePUNPIPUNPIIinosine-guanosine phosphorylasenucleotide phosphatasepurine deoxynucleoside phosphorylasepurine deoxyribonucleoside phosphorylasepurine nucleoside phosphorylasepurine ribonucleoside phosphorylase |
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Synonyms | PNPEC 2.4.2.1Inosine phosphorylase | PNPEC 2.4.2.1Inosine phosphorylase | PNPEC 2.4.2.1Inosine phosphorylase |
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RefSeq |
| NP_000261.2 (Protein) NM_000270.3 (DNA/RNA sequence)
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Pfam | PF01048 (PNP_UDP_1) [Graphical view]
| PF01048 (PNP_UDP_1) [Graphical view]
| PF01048 (PNP_UDP_1) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00230 | Purine metabolism | MAP00240 | Pyrimidine metabolism | MAP00760 | Nicotinate and nicotinamide metabolism |
UniProtKB:Accession Number | P55859 | P00491 | P81989 |
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Entry name | PNPH_BOVIN | PNPH_HUMAN | PUNA_CELSP |
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Activity | Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. | Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. | Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. |
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Subunit | Homotrimer. | Homotrimer. | Homotrimer. |
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Subcellular location |
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Cofactor |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[6] | Fig.7, Fig.9, p.11746-11747 | 3 | [7] | Fig.8, p.7144-7145 | 2 | [9] | Fig.5, p.1248-1250 | 3 | [11] | Fig.1 | 2 | [14] | Fig.5, Fig.7, p.14 | 2 | [15] | Fig.1 | 2 |
references | [1] |
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PubMed ID | 2104852 |
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Journal | J Biol Chem |
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Year | 1990 |
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Volume | 265 |
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Pages | 1812-20 |
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Authors | Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al |
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Title | Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. |
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Related UniProtKB | P00491 |
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[2] |
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PubMed ID | 1763067 |
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Journal | Proc Natl Acad Sci U S A |
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Year | 1991 |
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Volume | 88 |
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Pages | 11540-4 |
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Authors | Ealick SE, Babu YS, Bugg CE, Erion MD, Guida WC, Montgomery JA, Secrist JA 3rd |
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Title | Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors. |
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Related PDB | 1ula,1ulb |
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[3] |
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PubMed ID | 7607309 |
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Journal | FEBS Lett |
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Year | 1995 |
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Volume | 367 |
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Pages | 214-8 |
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Authors | Bzowska A, Luic M, Schroder W, Shugar D, Saenger W, Koellner G |
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Title | Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor. |
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[4] |
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PubMed ID | 9020983 |
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Journal | J Mol Biol |
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Year | 1997 |
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Volume | 265 |
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Pages | 202-16 |
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Authors | Koellner G, Luic M, Shugar D, Saenger W, Bzowska A |
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Title | Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution. |
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Related PDB | 1vfn |
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Related UniProtKB | P55859 |
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[5] |
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PubMed ID | 9305962 |
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Journal | Biochemistry |
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Year | 1997 |
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Volume | 36 |
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Pages | 11725-34 |
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Authors | Erion MD, Takabayashi K, Smith HB, Kessi J, Wagner S, Honger S, Shames SL, Ealick SE |
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Title | Purine nucleoside phosphorylase. 1. Structure-function studies. |
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[6] |
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PubMed ID | 9305963 |
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Journal | Biochemistry |
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Year | 1997 |
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Volume | 36 |
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Pages | 11735-48 |
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Authors | Erion MD, Stoeckler JD, Guida WC, Walter RL, Ealick SE |
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Title | Purine nucleoside phosphorylase. 2. Catalytic mechanism. |
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[7] |
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PubMed ID | 9585525 |
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Journal | Biochemistry |
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Year | 1998 |
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Volume | 37 |
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Pages | 7135-46 |
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Authors | Mao C, Cook WJ, Zhou M, Federov AA, Almo SC, Ealick SE |
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Title | Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues. |
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Related PDB | 1a9o,1a9p,1a9q,1a9r,1a9s,1a9t,1pbn |
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[8] |
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PubMed ID | 10404592 |
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Journal | Structure Fold Des |
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Year | 1999 |
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Volume | 7 |
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Pages | 629-41 |
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Authors | Appleby TC, Erion MD, Ealick SE |
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Title | The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis. |
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[9] |
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PubMed ID | 10600382 |
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Journal | J Mol Biol |
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Year | 1999 |
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Volume | 294 |
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Pages | 1239-55 |
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Authors | Tebbe J, Bzowska A, Wielgus-Kutrowska B, Schroder W, Kazimierczuk Z, Shugar D, Saenger W, Koellner G |
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Title | Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs. |
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Related PDB | 1qe5,1c3x |
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Related UniProtKB | P81989 |
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[10] |
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PubMed ID | 11134924 |
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Journal | Acta Crystallogr D Biol Crystallogr |
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Year | 2001 |
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Volume | 57 |
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Pages | 30-6 |
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Authors | Luic M, Koellner G, Shugar D, Saenger W, Bzowska A |
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Title | Calf spleen purine nucleoside phosphorylase: structure of its ternary complex with an N(7)-acycloguanosine inhibitor and a phosphate anion. |
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Related PDB | 1fxu |
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[11] |
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PubMed ID | 11170405 |
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Journal | Biochemistry |
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Year | 2001 |
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Volume | 40 |
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Pages | 853-60 |
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Authors | Fedorov A, Shi W, Kicska G, Fedorov E, Tyler PC, Furneaux RH, Hanson JC, Gainsford GJ, Larese JZ, Schramm VL, Almo SC |
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Title | Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis. |
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Related PDB | 1b8o,1b8n |
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[12] |
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PubMed ID | 11444966 |
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Journal | Biochemistry |
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Year | 2001 |
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Volume | 40 |
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Pages | 8204-15 |
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Authors | Shi W, Basso LA, Santos DS, Tyler PC, Furneaux RH, Blanchard JS, Almo SC, Schramm VL |
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Title | Structures of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complexes with immucillin-H and its pieces. |
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[13] |
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PubMed ID | 11591349 |
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Journal | Structure (Camb) |
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Year | 2001 |
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Volume | 9 |
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Pages | 941-53 |
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Authors | Lee JE, Cornell KA, Riscoe MK, Howell PL |
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Title | Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. |
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[14] |
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PubMed ID | 11743878 |
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Journal | Biochem J |
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Year | 2002 |
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Volume | 361 |
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Pages | 1-25 |
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Authors | Pugmire MJ, Ealick SE |
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Title | Structural analyses reveal two distinct families of nucleoside phosphorylases. |
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[15] |
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PubMed ID | 12463747 |
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Journal | Biochemistry |
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Year | 2002 |
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Volume | 41 |
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Pages | 14489-98 |
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Authors | Kicska GA, Tyler PC, Evans GB, Furneaux RH, Shi W, Fedorov A, Lewandowicz A, Cahill SM, Almo SC, Schramm VL |
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Title | Atomic dissection of the hydrogen bond network for transition-state analogue binding to purine nucleoside phosphorylase. |
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comments | The enzymes of this entry corresponds to the Trimeric subunit members of nucleoside phosphorylase family-I [14]. The literature [14] summarized the proposed catalytic mechanism of the enzyme. Beta-nucleoside binds in a high-energy (anticlinal torsion angle of the glycosidic bond, with the ribose moiety in the uncommon C-4'-endo sugar pucker), according to the literature [6]. This high-energy conformation produces steric strain, which induces glycosidic cleavage. The glycosidic bond is weakened further as electrons flow from O-4' of the ribose to the purine ring, resulting in an oxocarbenium ion that is stabilized by the negative charges of the phosphate ion. The phosphate ion binds on the alpha-side of the ribose ring, where it is postioned to participate in an SN1 nucleophilic attack at the C-1' position. The flow of electrons from the glycosidic bond to the purine ring is probably stabilized by active site residue (Asn) interactions at N-7 position of the purine base.
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created | updated |
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2002-07-12 | 2011-09-27 |
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