Induktion der NADP<sup>+</sup>‐abhängigen Aldehyddehydrogenase durch Kohlenwasserstoffe bei <i>Acinetobacter calcoaceticus</i>

Aurich, H; Eitner, G.

doi:10.1002/jobm.19770170402

Cited by 12 publications

(5 citation statements)

References 10 publications

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“…Firm conclusions about the importance of inducible alcohol dehydrogenases for the degradation of n-alkanes by Acinetobacter therefore cannot yet be drawn. Induction of a membrane-bound, NADP+dependent aldehyde dehydrogenase is well established (Aurich and Eitner, 1977;Aurich et aI., 1983;. This enzyme has been purified (Sorger and Aurich, 1978), reconstituted into liposomes (Aurich et aI., 1985) and kinetically characterised (Aurich et aI., 1987).…”

Section: Alcohol and Aldehyde Dehydrogenasesmentioning

confidence: 99%

“…(1) Aurich and Eitner, 1977; (2) Aurich et a1., 1983; (3) Klossek et a1.,198.5;(4) Singer and Finnerty,198.5a. dehydrogenase, key enzymes for the metabolism of excess C 2 -substrates, are repressed in the presence of carbohydrates, phosphoenolpyruvate, or during growth on C 4 -dicarboxylic acids. However, they are induced by n-alkanes, fatty acids, and acetate, whereas malic enzyme' is repressed under these conditions (Kleber, 1973(Kleber, , 1978, avoiding the loss of C 4 -units of the citric acid cycle.…”

Section: Referencesmentioning

confidence: 99%

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The Biology of Acinetobacter

Towner¹,

Bergogne-Bérézin²,

Fewson³

1991

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All rights reservedNo part of this book may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise, without written permission from the Publisher PREFACEThe 1st International Workshop on Acinetobacter was held on 6th September, 1986, in Manchester, England, in association with the 14th International Congress of Microbiology. That occasion was so well attended and productive that there were soon discussions about how, when and where the next meeting should be held. This time, however, there was sufficient confidence to think of a more substantial meeting and to plan for the proceedings to be published. It emerged that there was wide agreement that the time was ripe to take stock of the entire biology of Acinetobacter: its occurrence and taxonomy; its molecular biology, biochemistry and physiology; its clinical importance and its industrial and commercial applications. The 2nd International Workshop on Acinetobacter took place from 6th to 7th September, 1990, at the Institut Pasteur, Paris, and was sponsored by the Federation of European Microbiological Societies. There were about 100 participants from 19 countries. The backbone of the meeting consisted of 23 plenary lectures. There were 28 posters and the meeting closed with a general discussion which went on long after the official finishing time despite all the counter-attractions of a sunny Parisian Friday afternoon. Indeed discussions continued while cruising along the Seine and while dining at the top of the Tour Montparnasse. However, the vitality and usefulness of even the most successful meeting is difficult to transmit by the printed word. The editors decided, therefore, not simply to publish the proceedings of the Workshop, but rather to commission a set of review articles with the aim of giving an up-to-date and rounded picture of our current knowledge of the genus Acinetobacter. These reviews, together with a

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Section: Alcohol and Aldehyde Dehydrogenasesmentioning

confidence: 99%

Section: Referencesmentioning

confidence: 99%

The Biology of Acinetobacter

Towner¹,

Bergogne-Bérézin²,

Fewson³

1991

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“…Aldehydes are considered metabolic intermediates in microbial alkane dissimilation, with aldehydes oxidized to fatty acid via aldehyde dehydrogenase (13). Aldehyde dehydrogenases have been described in a number of hydrocarbon-utilizing microorganisms, including Candida tropicalis (5,6,9,10,17), Candida intermedia (11), Pseudomonas aeruginosa (3,8), Pseudomonas putida (oleovorans) (2), and Acinetobacter calcoaceticus 69V (1,15,16). Sorger and Aurich (16) have reviewed the kinetic properties and cofactor requirements of several microbial aldehyde dehydrogenases.…”

mentioning

confidence: 99%

“…A. calcoaceticus 69V contains a membrane-bound, NADP-dependent aldehyde dehydrogenase which is induced during growth on hexadecane or hexadecanol (1,15,16). Acinetobacter sp.…”

mentioning

confidence: 99%

Fatty aldehyde dehydrogenases in Acinetobacter sp. strain HO1-N: role in hexadecanol metabolism

Singer¹,

Finnerty²

1985

J Bacteriol

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The role of fatty aldehyde dehydrogenases (FALDHs) in hexadecane and hexadecanol metabolism was studied in Acinetobacter sp. strain HO1-N. Two distinct FALDHs were demonstrated in Acinetobacter sp. strain HO1-N: (i) a membrane-bound, NADP-dependent FALDH activity induced 5-, 15-, and 9-fold by growth on hexadecanol, dodecyl aldehyde, and hexadecane, respectively, and (ii) a constitutive, NAD-dependent, membrane-localized FALDH. The NADP-dependent FALDH exhibited apparent Km and Vmax values for decyl aldehyde of 5.0, 13.0, 18.0, and 18.3 ,LM and 537.0, 500.0, 25.0, and 38.0 nmol/min in hexadecane-, hexadecanol-, ethanol-, palmitate-grown ceUs, respectively. FALDH isozymes ald-a, ald-b, and ald-c were demonstrated by gel electrophoresis in extracts of hexadecane-and hexadecanol-grown cells. aid-a, ald-b, and ald-d were present in dodecyl aldehyde-grown cells, while palmitate-grown control cells contained ald-b and ald-d. Dodecyl aldehyde-negative mutants were isolated and grouped into two phenotypic classes based on growth: class 1 mutants were hexadecane and hexadecanol negative and class 2 mutants were hexadecane and hexadecanol positive. Specific activity of NADP-dependent FALDH in Ald2l (class 1 mutant) was 85% lower than that of wild-type FALDH, while the specific activity of Ald24 (class 2 mutant) was 55% greater than that of wild-type FALDH. Ald21R, a dodecyl aldehyde-positive revertant able to grow on hexadecane, hexadecanol, and dodecyl aldehyde, exhibited a 100% increase in the specific activity of the NADP-dependent FALDH. The

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“…calcoaceticus ein Enzyin des Oxidations-Pathways der Alkane (AURICH u. EITNER 1977, SORGER u. AURICH 1978 und in den intracytoplasmatischen Umhiillungsmenibranen der Alkan-Inklusionen lokalisiert (VOAISEK et al 1982). Sie liiljt sich durch Detergentien, wie Desoxycholat, Cholat, Laurylsarkosin und Triton X-100 solubilisieren (AURICH et al 1985) und als Detergens-Phospholipid-Mischmizelle isolieren und reinigen .…”

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Wechselwirkungen der Aldehyddehdyrogenase aus Acinetobacter calcoaceticus mit Membranlipiden II. Rekonstitution in künstlichen Membranvesikeln

Aurich

Bergmann

Lasch

et al. 1985

J. Basic Microbiol.

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Purified aldehyde dehydrogenase (NADP+-dependent) of intracytoplasmic membranes of Acinetobacter cakcoaceticus could he incorporated from micelles formed during the purification procedure into liposomal membranes. Both the cholate dilution method and the ultrasonication method were suitable to produce enzyme liposomes. In unilamellar liposomes produced by phosphntidyl choline, the enzyme activity decreased to 1% (or less) of the original activity. In contrast, about 10% of the original activity could be preserved in unilamellar liposomes prepared from bacterinl phospholipids.The destruction of the enzyme liposomes induced by detergents (lauroyl sarcosinate) was followed by measuring the wavelength dependence of turbidity, which allowed us to draw conclusions on size and stability of the particles in the suspension. I n addition these measurements demonstrated that decanal and NADP+ did not destroy the liposomal structure a t concentrations necessary for the determination of enzyme activity.The liposomal enzyme was inactivated to a lesser degree by proteinase K than the micellar enzyme. Both phospholipase A, and D inactivated the enzyme incorporated into the liposomal membranes to about 50%. After t,reatment with phospholipase A,, the enzyme could be reactivated by bacterial phospholipids. After treatment with phospholipase D, no reactivation was possible by bacterial phospholipids.Die NADP-abhangige Aldehyddehydrogenase ist bei A . calcoaceticus ein Enzyin des Oxidations-Pathways der Alkane (AURICH u. EITNER 1977, SORGER u. AURICH 1978 und in den intracytoplasmatischen Umhiillungsmenibranen der Alkan-Inklusionen lokalisiert (VOAISEK et al. 1982). Sie liiljt sich durch Detergentien, wie Desoxycholat, Cholat, Laurylsarkosin und Triton X-100 solubilisieren (AURICH et al. 1985) und als Detergens-Phospholipid-Mischmizelle isolieren und reinigen . Wahrscheinlich ist Cardiolipin fur die Aktivitat des Enzynis essentiell (BERGMANN 1982

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Induktion der NADP⁺‐abhängigen Aldehyddehydrogenase durch Kohlenwasserstoffe bei Acinetobacter calcoaceticus

Cited by 12 publications

References 10 publications

The Biology of Acinetobacter

The Biology of Acinetobacter

Fatty aldehyde dehydrogenases in Acinetobacter sp. strain HO1-N: role in hexadecanol metabolism

Wechselwirkungen der Aldehyddehdyrogenase aus Acinetobacter calcoaceticus mit Membranlipiden II. Rekonstitution in künstlichen Membranvesikeln

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Induktion der NADP+‐abhängigen Aldehyddehydrogenase durch Kohlenwasserstoffe bei Acinetobacter calcoaceticus

Cited by 12 publications

References 10 publications

The Biology of Acinetobacter

The Biology of Acinetobacter

Fatty aldehyde dehydrogenases in Acinetobacter sp. strain HO1-N: role in hexadecanol metabolism

Wechselwirkungen der Aldehyddehdyrogenase aus Acinetobacter calcoaceticus mit Membranlipiden II. Rekonstitution in künstlichen Membranvesikeln

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Induktion der NADP⁺‐abhängigen Aldehyddehydrogenase durch Kohlenwasserstoffe bei Acinetobacter calcoaceticus