The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase

The Pseudomonas oleovorans alkBAC operon encodes seven proteins, of which at least three are involved in alkane hydroxylase (alkBA) and alkanol dehydrogenase (alkC) activities. We have determined the nucleotide sequence of the 2.5-kilobase pair alkA region and analyzed the role of its translation pr...

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Bibliographic Details
Published in:The Journal of biological chemistry 1989-04, Vol.264 (10), p.5442-5451
Main Authors: Kok, M, Oldenhuis, R, van der Linden, M P G, Meulenberg, C H C, Kingma, J, Witholt, B
Format: Article
Language:English
Subjects:
aldehyde dehydrogenase
Aldehyde Dehydrogenase - genetics
Amino Acid Sequence
Base Sequence
Biological and medical sciences
Cytochrome P-450 CYP4A
Cytochrome P-450 Enzyme System - genetics
Escherichia coli - genetics
Ferredoxins - genetics
Fundamental and applied biological sciences. Psychology
Genes
Genes, Bacterial
Genotype
Mixed Function Oxygenases - genetics
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
nucleotide sequence
Operon
operons
Phenotype
Plasmids
Pseudomonas - enzymology
Pseudomonas - genetics
Pseudomonas oleovorans
Restriction Mapping
rubredoxin
Rubredoxins - genetics
Sequence Homology, Nucleic Acid
Translation. Translation factors. Protein processing
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Summary:The Pseudomonas oleovorans alkBAC operon encodes seven proteins, of which at least three are involved in alkane hydroxylase (alkBA) and alkanol dehydrogenase (alkC) activities. We have determined the nucleotide sequence of the 2.5-kilobase pair alkA region and analyzed the role of its translation products in alkane oxidation. The alkA region contains three coding sequences, encoding two related rubredoxins (alkF and alkG) of 14- and 18-kDa molecular mass and a 52-kDa aldehyde dehydrogenase (alkH). Deletion analysis indicated that neither the 14-kDa alkF gene product (rubredoxin 1) nor the amino-terminal part of the 18-kDa alkG gene product (rubredoxin 2) is required for alkane hydroxylase activity in vivo. The product of the alkH cistron restores growth of a P. oleovorans aldehyde dehydrogenase mutant on aliphatic alcohols and aldehydes. Its amino acid sequence shows considerable homology to previously characterized aldehyde dehydrogenases from mammalian and fungal origin. The nucleotide composition of the alk genes (47% G+C) differs considerably from the G+C content of the P. oleovorans genome suggesting that the alk regulon may originate from an unrelated organism.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)83565-7