1NRG
Structure and Properties of Recombinant Human Pyridoxine-5'-Phosphate Oxidase
Summary for 1NRG
| Entry DOI | 10.2210/pdb1nrg/pdb |
| Descriptor | pyridoxine 5'-phosphate oxidase, PHOSPHATE ION, FLAVIN MONONUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | plp, fmn, pyridoxine-5'-phosphate, oxidase, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 30905.62 |
| Authors | Musayev, F.N.,di Salvo, M.L.,Ko, T.P.,Schirch, V.,Safo, M.K. (deposition date: 2003-01-24, release date: 2003-02-11, Last modification date: 2023-08-16) |
| Primary citation | Musayev, F.N.,Di Salvo, M.L.,Ko, T.P.,Schirch, V.,Safo, M.K. Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. Protein Sci., 12:1455-1463, 2003 Cited by PubMed Abstract: Pyridoxine 5'-phosphate oxidase catalyzes the terminal step in the synthesis of pyridoxal 5'-phosphate. The cDNA for the human enzyme has been cloned and expressed in Escherichia coli. The purified human enzyme is a homodimer that exhibits a low catalytic rate constant of approximately 0.2 sec(-1) and K(m) values in the low micromolar range for both pyridoxine 5'phosphate and pyridoxamine 5'-phosphate. Pyridoxal 5'-phosphate is an effective product inhibitor. The three-dimensional fold of the human enzyme is very similar to those of the E. coli and yeast enzymes. The human and E. coli enzymes share 39% sequence identity, but the binding sites for the tightly bound FMN and substrate are highly conserved. As observed with the E. coli enzyme, the human enzyme binds one molecule of pyridoxal 5'-phosphate tightly on each subunit. PubMed: 12824491DOI: 10.1110/ps.0356203 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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