Genetic Analysis of a Gene Cluster for Cyclohexanol Oxidation in
            <i>Acinetobacter</i>
            sp. Strain SE19 by In Vitro Transposition

Cheng, Qiong; Thomas, Stuart M.; Kostichka, Kristy; Valentine, James R.; Nagarajan, Vasantha

doi:10.1128/jb.182.17.4744-4751.2000

Cited by 77 publications

(58 citation statements)

References 28 publications

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“…These results and those of the phylogenetic analysis suggest that the unknown protein from A. pleuropneumoniae (2) (ORF1Ap), protein ID317 from B. japonicum (21), ChnZ from Acinetobacter sp. strain SE19 (9), and the putative transposase from a Wolbachia endosymbiont of D. simulans (accession number AAK96114) might be encoded by complete or truncated ISs. These sequences, along with ISCce1, might form a new group of ISs, which is probably related to the IS481 and the IS3 families.…”

Section: Discussionmentioning

confidence: 99%

ISCce 1 and ISCce 2 , Two Novel Insertion Sequences in Clostridium cellulolyticum

et al. 2003

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Two new insertion sequences, ISCce1 and ISCce2, were found to be inserted into the cipC gene of spontaneous mutants of Clostridium cellulolyticum. In these insertional mutants, the cipC gene was disrupted either by ISCce1 alone or by both ISCce1 and ISCce2. ISCce1 is 1,292 bp long and has one open reading frame. The open reading frame encodes a putative 348-amino-acid protein with significant levels of identity with putative proteins having unknown functions and with some transposases belonging to the IS481 and IS3 families. Imperfect 23-bp inverted repeats were found near the extremities of ISCce1. ISCce2 is 1,359 bp long, carries one open reading frame, and has imperfect 35-bp inverted repeats at its termini. The open reading frame encodes a putative 398-amino-acid protein. This protein shows significant levels of identity with transposases belonging to the IS256 family. Upon transposition, both ISCce1 and ISCce2 generate 8-bp direct repeats of the target sequence, but no consensus sequences could be identified at either insertion site. ISCce1 is copied at least 20 times in the genome, as assessed by Southern blot analysis. ISCce2 was found to be mostly inserted into ISCce1. In addition, as neither of the elements was detected in seven other Clostridium species, we concluded that they may be specific to the C. cellulolyticum strain used.

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Section: Discussionmentioning

confidence: 99%

ISCce 1 and ISCce 2 , Two Novel Insertion Sequences in Clostridium cellulolyticum

et al. 2003

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“…14,15) It is known that the bacterial metabolism of cyclohexanol to adipic acid proceeds via cyclohexanone, "-caprolactone, 6-hydroxyhexanoic acid, and 6-oxohexanoic acid. 16) Each gene encoding the enzyme involved in this pathway has been identified, 17) so that the identification of the enzyme oxidizing cyclohexane to cyclohexanol and its coding gene is essential for studies of the cycloalkane degradation pathway. It has been thought that AH catalyzes the terminal oxidation of n-alkanes.…”

Section: Discussionmentioning

confidence: 99%

Biotransformation of Various Alkanes Using theEscherichia coliExpressing an Alkane Hydroxylase System fromGordoniasp. TF6

Fujii¹,

Narikawa²,

Takeda³

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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“…The alicyclic hydrocarbons are a major component of petroleum, and microbial metabolism of these compounds has been reported in various microorganisms (5,7,9,11,13,18,26). Most of the microbes isolated to date that metabolize alicyclic hydrocarbons contain degradation pathways for small (C 5 , C 6 , and C 7 ) cyclic compounds (7,12,13,15).…”

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confidence: 99%

Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1

et al. 2001

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Biological oxidation of cyclic ketones normally results in formation of the corresponding dicarboxylic acids, which are further metabolized in the cell. Rhodococcus ruber strain SC1 was isolated from an industrial wastewater bioreactor that was able to utilize cyclododecanone as the sole carbon source. A reverse genetic approach was used to isolate a 10-kb gene cluster containing all genes required for oxidative conversion of cyclododecanone to 1,12-dodecanedioic acid (DDDA). The genes required for cyclododecanone oxidation were only marginally similar to the analogous genes for cyclohexanone oxidation. The biochemical function of the enzymes encoded on the 10-kb gene cluster, the flavin monooxygenase, the lactone hydrolase, the alcohol dehydrogenase, and the aldehyde dehydrogenase, was determined in Escherichia coli based on the ability to convert cyclododecanone. Recombinant E. coli strains grown in the presence of cyclododecanone accumulated lauryl lactone, 12-hydroxylauric acid, and/or DDDA depending on the genes cloned. The cyclododecanone monooxygenase is a type 1 Baeyer-Villiger flavin monooxygenase (FAD as cofactor) and exhibited substrate specificity towards long-chain cyclic ketones (C 11 to C 15 ), which is different from the specificity of cyclohexanone monooxygenase favoring short-chain cyclic compounds (C 5 to C 7 ).

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Genetic Analysis of a Gene Cluster for Cyclohexanol Oxidation in Acinetobacter sp. Strain SE19 by In Vitro Transposition

Cited by 77 publications

References 28 publications

ISCce 1 and ISCce 2 , Two Novel Insertion Sequences in Clostridium cellulolyticum

ISCce 1 and ISCce 2 , Two Novel Insertion Sequences in Clostridium cellulolyticum

Biotransformation of Various Alkanes Using theEscherichia coliExpressing an Alkane Hydroxylase System fromGordoniasp. TF6

Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1

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