4COK
Functional and Structural Characterization of Pyruvate decarboxylase from Gluconoacetobacter diazotrophicus
Summary for 4COK
| Entry DOI | 10.2210/pdb4cok/pdb |
| Descriptor | PYRUVATE DECARBOXYLASE, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | lyase |
| Biological source | GLUCONACETOBACTER DIAZOTROPHICUS PAL 5 |
| Total number of polymer chains | 2 |
| Total formula weight | 119479.00 |
| Authors | vanZyl, L.J.,Schubert, W.-D.,Tuffin, M.,Cowan, D.A. (deposition date: 2014-01-29, release date: 2014-10-01, Last modification date: 2023-12-20) |
| Primary citation | Van Zyl, L.J.,Schubert, W.,Tuffin, M.I.,Cowan, D.A. Structure and Functional Characterization of Pyruvate Decarboxylase from Gluconacetobacter Diazotrophicus. Bmc Struct.Biol., 14:21-, 2014 Cited by PubMed Abstract: Bacterial pyruvate decarboxylases (PDC) are rare. Their role in ethanol production and in bacterially mediated ethanologenic processes has, however, ensured a continued and growing interest. PDCs from Zymomonas mobilis (ZmPDC), Zymobacter palmae (ZpPDC) and Sarcina ventriculi (SvPDC) have been characterized and ZmPDC has been produced successfully in a range of heterologous hosts. PDCs from the Acetobacteraceae and their role in metabolism have not been characterized to the same extent. Examples include Gluconobacter oxydans (GoPDC), G. diazotrophicus (GdPDC) and Acetobacter pasteutrianus (ApPDC). All of these organisms are of commercial importance. PubMed: 25369873DOI: 10.1186/S12900-014-0021-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
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