| IED ID | IndEnz0019000003 |
| Enzyme Type ID | polyphenol oxidase000003 |
| Protein Name |
Purine nucleoside phosphorylase YfiH EC 2.4.2.1 Adenosine deaminase YfiH EC 3.5.4.4 Polyphenol oxidase YfiH EC 1.10.3.- S-methyl-5'-thioadenosine phosphorylase YfiH EC 2.4.2.28 |
| Gene Name | yfiH b2593 JW2575 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSKLIVPQWPQPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENRKRLFAAGNLPSKPVWLEQVHGKDVLKLTGEPYASKRADASYSNTPGTVCAVMTADCLPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVSCFADNPENILAWLGPAIGPRAFEVGGEVREAFMAVDAKASAAFIQHGDKYLADIYQLARQRLANVGVEQIFGGDRCTYTENETFFSYRRDKTTGRMASFIWLI |
| Enzyme Length | 243 |
| Uniprot Accession Number | P33644 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:31978345};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27643; Evidence={ECO:0000269|PubMed:31978345}; CATALYTIC ACTIVITY: Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474, ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000269|PubMed:31978345};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853; Evidence={ECO:0000269|PubMed:31978345}; CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:31978345};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647; Evidence={ECO:0000269|PubMed:31978345}; CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:31978345};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000269|PubMed:31978345}; |
| DNA Binding | |
| EC Number | 2.4.2.1; 3.5.4.4; 1.10.3.-; 2.4.2.28 |
| Enzyme Function | FUNCTION: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine (PubMed:31978345). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (PubMed:31978345). Also has adenosine deaminase activity (PubMed:31978345). May also act as a polyphenol oxidase: able to oxidize syringaldazine and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) in vitro (PubMed:16740638). {ECO:0000269|PubMed:16740638, ECO:0000269|PubMed:31978345}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 44 degrees Celsius. Maintains more than 80% activity at 50 degrees Celsius. {ECO:0000269|PubMed:16740638}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-8.4. Maintains 80% activity at pH 5.0-9.0. {ECO:0000269|PubMed:16740638}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (11); Chain (1); Helix (8); Metal binding (3); Sequence conflict (1); Turn (3) |
| Keywords | 3D-structure;Copper;Hydrolase;Metal-binding;Oxidoreductase;Reference proteome;Transferase;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1Z9T; 7F3V; 7W1G; |
| Mapped Pubmed ID | 16606699; 35164571; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,339 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; KM=1.10 uM for syringaldazine (at pH 4.5 and 40 degrees Celsius) {ECO:0000269|PubMed:16740638}; Note=kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid as substrate. kcat is 21720 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius). {ECO:0000269|PubMed:16740638}; |
| Metal Binding | METAL 71; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 107; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138; METAL 124; /note=Zn(2+); catalytic; /evidence=ECO:0000250|UniProtKB:P84138 |
| Rhea ID | RHEA:27642; RHEA:27643; RHEA:11852; RHEA:11853; RHEA:27646; RHEA:27647; RHEA:24408; RHEA:24409 |
| Cross Reference Brenda |