| | Authors : | Brandsch,R.;Hinkkanen,A.E.;Mauch,L.;Nagursky,H.;Decker,K. | |
| | Keywords : | Amino Acid Sequence
Arthrobacter/*enzymology
Base Sequence
DNA, Bacterial/analysis
Flavin-Adenine Dinucleotide/metabolism
Oxidoreductases/*genetics
Peptide Mapping
Ribonucleases/metabolism
Transcription, Genetic
| |
| | Abstracts : | The nucleotide sequence of the 6-hydroxy-D-nicotine oxidase (6-HDNO) gene of Arthrobacter oxidans is presented. This covalently flavinylated enzyme specifically oxidizes 6-hydroxy-D-nicotine to 6-hydroxy-N-methylmyosmine. Coinduced in the presence of nicotine is a 6-hydroxy-L-nicotine-specific enzyme, 6-hydroxy-L-nicotine oxidase (6-HLNO), with FAD noncovalently bound to the apoprotein. A comparison of the nucleotide-derived amino acid sequence of the 6-HDNO with the amino acid sequence data obtained from the purified 6-HLNO polypeptide suggests that the two enantiozymes expressed within the same cell are genetically unrelated. This conclusion is supported by the finding that the FAD-binding sites of the two enzymes are different. 6-HLNO exhibits at the amino-terminus of the polypeptide chain a dinucleotide-binding site characteristic for many other FAD- and NAD(P)-dependent enzymes. No such sequence was found in the nucleotide-derived amino acid sequence of 6-HDNO. | |