Reaction participants Show >> << Hide
- Name help_outline 2'-deoxyadenosine Identifier CHEBI:17256 (CAS: 958-09-8) help_outline Charge 0 Formula C10H13N5O3 InChIKeyhelp_outline OLXZPDWKRNYJJZ-RRKCRQDMSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@H]1C[C@H](O)[C@@H](CO)O1 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,020 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-deoxy-α-D-ribose 1-phosphate Identifier CHEBI:57259 Charge -2 Formula C5H9O7P InChIKeyhelp_outline KBDKAJNTYKVSEK-VPENINKCSA-L SMILEShelp_outline OC[C@H]1O[C@@H](C[C@@H]1O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline adenine Identifier CHEBI:16708 (CAS: 73-24-5) help_outline Charge 0 Formula C5H5N5 InChIKeyhelp_outline GFFGJBXGBJISGV-UHFFFAOYSA-N SMILEShelp_outline Nc1ncnc2[nH]cnc12 2D coordinates Mol file for the small molecule Search links Involved in 22 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:27742 | RHEA:27743 | RHEA:27744 | RHEA:27745 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.
Mikleusevic G., Stefanic Z., Narczyk M., Wielgus-Kutrowska B., Bzowska A., Luic M.
The catalytic mechanism of Escherichia coli purine nucleoside phosphorylase (PNP) is revised using site-directed mutagenesis, kinetic studies and structure determinations. The experimental evidence on the role of the particular catalytic amino acid during catalysis has not been available. Therefor ... >> More
The catalytic mechanism of Escherichia coli purine nucleoside phosphorylase (PNP) is revised using site-directed mutagenesis, kinetic studies and structure determinations. The experimental evidence on the role of the particular catalytic amino acid during catalysis has not been available. Therefore, the active site mutants Arg24Ala, Asp204Ala, Asp204Asn, Arg217Ala and Asp204Ala/Arg217Ala were prepared and their kinetics and thermodynamic studies were carried out. The activity tests with natural substrates and 7-methylguanosine confirmed the earlier hypothesis, that catalysis involves protonation of the purine base at position N7 by Asp204, which is triggered by Arg217. The crystal structures of the wild type in complexes with phosphate and sulphate, respectively, and of the Arg24Ala mutant in complex with phosphate/sulphate were determined. The structural data show that previously observed conformational change is a result of the phosphate binding and its interaction with Arg24. As E. coli PNP is a promising candidate for the tumour-directed gene therapy, our results may also help to design efficient mutants useful in gene therapy. << Less