Abstract
n-Alkane oxidation in a long chain n-alkane utilizer, Acinetobacter sp. M- l, was investigated. In Acinetobacter, n-alkanes have been postulated to be converted to the acid via a non-conventional oxidation pathway: n-alkane → n-alkyl hydroperoxide → aldehyde → acid (Finnerty, W.R.: Lipids of Acinetobacter. In Proceedings of the World Conference on Biotechnology for the Fats and Oils Industry, 184-188, 1988). However, there is little biochemical information on the enzymes involved in the postulated pathway, particularly the enzyme catalyzing the first step. In this study, we purified an n-alkane-oxidizing enzyme to apparent homogeneity by SDS-PAGE. The enzyme was a flavoprotein, and required molecular oxygen and Cu2+ for its activity, but did not require a reduced coenzyme such as NAD(P)H. A hydroperoxide was detected as a product of the enzyme reaction. We assume that the n-alkane-oxidizing enzyme is a dioxygenase. In addition, as a fatty alcohol does not appear to be an intermediate, fatty alcohol dehydrogenase is assumed not to participate in the n-alkane oxidation. The validity of the postulated pathway is supported by the following observations: (i) n-alkane monooxygenase activity was not detected, (ii) fatty alcohol dehydrogenase activities were low, and (iii) NAD(P)H-dependent long chain fatty aldehyde dehydrogenase activities were strongly induced in n-alkane-grown cells. NAD(P)H-dependent fatty aldehyde reductase activity was also found in n- alkane-grown cells, which may contribute to the formation of waxes that are cell reserve substances in n-alkane-utilizing Acinetobacter.
| Original language | English |
|---|---|
| Pages (from-to) | 286-291 |
| Number of pages | 6 |
| Journal | Journal of Fermentation and Bioengineering |
| Volume | 81 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1996 |
| Externally published | Yes |
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Keywords
- Acinetobacter
- aldehyde dehydrogenase
- dioxygenase
- long-chain alkane
- pathway
ASJC Scopus subject areas
- Biotechnology
- Applied Microbiology and Biotechnology
Cite this
A non-conventional dissimilation pathway for long chain n-alkanes in Acinetobacter sp. M-1 that starts with a dioxygenase reaction. / Sakai, Yasuyoshi; Maeng, Jun Ho; Kubota, Seigo; Tani, Akiwo; Tani, Yoshiki; Kato, Nobuo.
In: Journal of Fermentation and Bioengineering, Vol. 81, No. 4, 1996, p. 286-291.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A non-conventional dissimilation pathway for long chain n-alkanes in Acinetobacter sp. M-1 that starts with a dioxygenase reaction
AU - Sakai, Yasuyoshi
AU - Maeng, Jun Ho
AU - Kubota, Seigo
AU - Tani, Akiwo
AU - Tani, Yoshiki
AU - Kato, Nobuo
PY - 1996
Y1 - 1996
N2 - n-Alkane oxidation in a long chain n-alkane utilizer, Acinetobacter sp. M- l, was investigated. In Acinetobacter, n-alkanes have been postulated to be converted to the acid via a non-conventional oxidation pathway: n-alkane → n-alkyl hydroperoxide → aldehyde → acid (Finnerty, W.R.: Lipids of Acinetobacter. In Proceedings of the World Conference on Biotechnology for the Fats and Oils Industry, 184-188, 1988). However, there is little biochemical information on the enzymes involved in the postulated pathway, particularly the enzyme catalyzing the first step. In this study, we purified an n-alkane-oxidizing enzyme to apparent homogeneity by SDS-PAGE. The enzyme was a flavoprotein, and required molecular oxygen and Cu2+ for its activity, but did not require a reduced coenzyme such as NAD(P)H. A hydroperoxide was detected as a product of the enzyme reaction. We assume that the n-alkane-oxidizing enzyme is a dioxygenase. In addition, as a fatty alcohol does not appear to be an intermediate, fatty alcohol dehydrogenase is assumed not to participate in the n-alkane oxidation. The validity of the postulated pathway is supported by the following observations: (i) n-alkane monooxygenase activity was not detected, (ii) fatty alcohol dehydrogenase activities were low, and (iii) NAD(P)H-dependent long chain fatty aldehyde dehydrogenase activities were strongly induced in n-alkane-grown cells. NAD(P)H-dependent fatty aldehyde reductase activity was also found in n- alkane-grown cells, which may contribute to the formation of waxes that are cell reserve substances in n-alkane-utilizing Acinetobacter.
AB - n-Alkane oxidation in a long chain n-alkane utilizer, Acinetobacter sp. M- l, was investigated. In Acinetobacter, n-alkanes have been postulated to be converted to the acid via a non-conventional oxidation pathway: n-alkane → n-alkyl hydroperoxide → aldehyde → acid (Finnerty, W.R.: Lipids of Acinetobacter. In Proceedings of the World Conference on Biotechnology for the Fats and Oils Industry, 184-188, 1988). However, there is little biochemical information on the enzymes involved in the postulated pathway, particularly the enzyme catalyzing the first step. In this study, we purified an n-alkane-oxidizing enzyme to apparent homogeneity by SDS-PAGE. The enzyme was a flavoprotein, and required molecular oxygen and Cu2+ for its activity, but did not require a reduced coenzyme such as NAD(P)H. A hydroperoxide was detected as a product of the enzyme reaction. We assume that the n-alkane-oxidizing enzyme is a dioxygenase. In addition, as a fatty alcohol does not appear to be an intermediate, fatty alcohol dehydrogenase is assumed not to participate in the n-alkane oxidation. The validity of the postulated pathway is supported by the following observations: (i) n-alkane monooxygenase activity was not detected, (ii) fatty alcohol dehydrogenase activities were low, and (iii) NAD(P)H-dependent long chain fatty aldehyde dehydrogenase activities were strongly induced in n-alkane-grown cells. NAD(P)H-dependent fatty aldehyde reductase activity was also found in n- alkane-grown cells, which may contribute to the formation of waxes that are cell reserve substances in n-alkane-utilizing Acinetobacter.
KW - Acinetobacter
KW - aldehyde dehydrogenase
KW - dioxygenase
KW - long-chain alkane
KW - pathway
UR - http://www.scopus.com/inward/record.url?scp=9344245667&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=9344245667&partnerID=8YFLogxK
U2 - 10.1016/0922-338X(96)80578-2
DO - 10.1016/0922-338X(96)80578-2
M3 - Article
AN - SCOPUS:9344245667
VL - 81
SP - 286
EP - 291
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 4
ER -