PMID:240388
| Citation |
Applebaum, D, Sabo, DL, Fischer, EH and Morris, DR (1975) Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5'-phosphate binding site. Biochemistry 14:3675-81 |
|---|---|
| Abstract |
The biodegradative ornithine decarboxylase of Escherichia coli has been purified to apparent homogeneity. At its pH optimum (pH 7.0), the enzyme exists as a dimer of 160,000 molecular weight. Aggregation of the dimer was promoted by lower pH values. The enzyme requires pyridoxal 5'-phosphate for activity. The coenzyme appears to be bound in Schiff base linkage as suggested by spectral studies and inhibition by NaBH4. The following sequence was determined for the coenzyme binding site: Val-His-(epsilon-Pxy)Lys-Gln-Gln-Ala-Gly-Gln. The properties of this enzyme are compared with the other biodegradative amino acid decarboxylases that have been isolated from E. coli. |
| Links | |
| Keywords |
Amino Acid Sequence; Apoenzymes/isolation & purification; Binding Sites; Carboxy-Lyases/metabolism; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; Ornithine Decarboxylase/isolation & purification; Ornithine Decarboxylase/metabolism; Peptide Fragments/analysis; Protein Binding; Pyridoxal Phosphate/pharmacology; Spectrophotometry |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.