SEQUENCE-ANALYSIS OF THE GENES ENCODING A MULTICOMPONENT DIOXYGENASE INVOLVED IN OXIDATION OF ANILINE AND O-TOLUIDINE IN ACINETOBACTER SP. STRAIN YAA

Citation
M. Takeo et al., SEQUENCE-ANALYSIS OF THE GENES ENCODING A MULTICOMPONENT DIOXYGENASE INVOLVED IN OXIDATION OF ANILINE AND O-TOLUIDINE IN ACINETOBACTER SP. STRAIN YAA, Journal of fermentation and bioengineering, 85(1), 1998, pp. 17-24
Citations number
52
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Food Science & Tenology","Biothechnology & Applied Migrobiology
ISSN journal
0922-338X
Volume
85
Issue
1
Year of publication
1998
Pages
17 - 24
Database
ISI
SICI code
0922-338X(1998)85:1<17:SOTGEA>2.0.ZU;2-U
Abstract
The nucleotide (nt) sequence of the genes encoding the oxidation of an iline and o-toluidine to the corresponding catechols was determined in the Acinetobacter sp. strain YAA. The 6293-bp DNA region sequenced co ntained five genes (atdA1-A5) in one strand. From the deduced amino ac id (aa) sequences, the atdA1-A5 genes were predicted to encode a gluta mine synthetase-like protein (AtdA1), a glutamine amidotransferase-lik e protein (AtdA2) and three subunits of benzene-ring hydroxylating oxy genase [the large and small subunits of the terminal dioxygenase compo nent (AtdA3 and AtdA4) and the reductase component (AtdA5)] in this or der. A glutamine synthetase ATP-binding motif and a putative glutamine amidotransferase class-I active site were found in AtdA1 and AtdA2, r espectively, whereas Rieske-type-and plant ferredoxin-type-[2Fe-2S] bi nding motifs were found in AtdA3 and AtdA5, respectively. These result s suggest that, in aniline oxidation in this strain, the former two ge ne products (AtdA1 and AtdA2) are involved in the recognition and rele ase of aniline amino-groups, while the latter three (AtdA3, AtdA4 and AtdA5) are involved in dihydroxylation of the benzene-ring. Although t his aniline oxidation system has a significant resemblance (31.1-62.0% homology at the aa sequence level) to that from Pseudomonas putida UC C22 (Fukumori and Saint, J. Bacteriol., 179, 399-408, 1997), the G+C c ontent of these Acinetobacter genes (40.1-47.4%) is quite different fr om that of the Pseudomonas genes, tdnQTA1A2B (63.1-71.2%). Polypeptide analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis confirmed the production of all the above polypeptides with a molecul ar mass calculated from each aa sequence.