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4COK

Functional and Structural Characterization of Pyruvate decarboxylase from Gluconoacetobacter diazotrophicus

Summary for 4COK
Entry DOI10.2210/pdb4cok/pdb
DescriptorPYRUVATE DECARBOXYLASE, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordslyase
Biological sourceGLUCONACETOBACTER DIAZOTROPHICUS PAL 5
Total number of polymer chains2
Total formula weight119479.00
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 citationVan 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: 25369873
DOI: 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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