Degradation of long-chain n-alkanes by the yeast Candida maltosa

Blasig, Rosel; Mauersberger, Stephan; Riege, P.; Schunck, Wolf‐Hagen; Jockisch, W.; Franke, P.; Mller, Hans-Martin

doi:10.1007/bf00250418

Cited by 40 publications

(10 citation statements)

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“…The main result is that a single P450 enzyme can efficiently catalyze not only the terminal hydroxylation of longchain n-alkanes and the -hydroxylation of fatty acids as previously suggested (12)(13)(14) but also the complete sequence of mono-and diterminal oxidation steps finally yielding ␣,-dioic acids. This conclusion is based on the product pattern arising from the time course of P450 52A3-catalyzed hexadecane oxidation and the observation that each of the intermediates of the reaction cascade can serve as a separate P450 substrate.…”

Section: Discussionmentioning

confidence: 55%

“…C]hexadecanoic acid with specific activities of 57, 54, and 56.6 mCi/mmol, respectively, were purchased from either Sigma (Deisenhofen, Germany) or Amersham-Buchler (Braunschweig, Germany). [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C]Hexadecanal was produced by enzymatic oxidation of labeled 1-hexadecanol using the peroxisomal fatty alcohol oxidase from the yeast C. maltosa as described previously (14 C]hydroxyhexadecanoic acid were prepared by the P450 52A3-catalyzed hydroxylation of labeled 1-hexadecanol in a reconstituted system composed as described below.…”

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confidence: 99%

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Oxygenation Cascade in Conversion of n-Alkanes to α,ω-Dioic Acids Catalyzed by Cytochrome P450 52A3

Scheller¹,

Zimmer²,

Becher³

et al. 1998

Journal of Biological Chemistry

155

119

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Purified recombinant cytochrome P450 52A3 and the corresponding NADPH-cytochrome P450 reductase from the alkane-assimilating yeast Candida maltosa were reconstituted into an active alkane monooxygenase system. Besides the primary product, 1-hexadecanol, the conversion of hexadecane yielded up to five additional metabolites, which were identified by gas chromatography-electron impact mass spectrometry as hexadecanal, hexadecanoic acid, 1,16-hexadecanediol, 16-hydroxyhexadecanoic acid, and 1,16-hexadecanedioic acid. As shown by substrate binding studies, the final product 1,16-hexadecanedioic acid acts as a competitive inhibitor of n-alkane binding and may be important for the metabolic regulation of the P450 activity. Kinetic studies of the individual sequential reactions revealed high V max values for the conversion of hexadecane, 1-hexadecanol, and hexadecanal (27, 23, and 69 min ؊1 , respectively), whereas the oxidation of hexadecanoic acid, 1,16-hexadecanediol, and 16-hydroxyhexadecanoic acid occurred at significantly lower rates (9, 9, and 5 min ؊1 , respectively). 1-Hexadecanol was found to be the main branch point between mono-and diterminal oxidation. Taken together with data on the incorporation of 18 O 2 -derived oxygen into the hexadecane oxidation products, the present study demonstrates that a single P450 form is able to efficiently catalyze a cascade of sequential mono-and diterminal monooxygenation reactions from n-alkanes to ␣,-dioic acids with high regioselectivity.The capability of several yeast species to use n-alkanes and other aliphatic hydrocarbons as a sole source of carbon and energy is mediated by the existence of multiple microsomal cytochrome P450 forms. Corresponding P450 genes or cDNAs have been isolated from the alkane-assimilating yeasts Candida maltosa (1-6), C. tropicalis (7-9), and C. apicola (10). The presently available 21 sequences belong to the family CYP52, according to the nomenclature of the P450 superfamily (11).The metabolic functions of P450 in these yeasts have been established thus far in the terminal oxidation of long-chain n-alkanes to fatty alcohols as the first and rate-determining step of the n-alkane degradation pathway and in the -hydroxylation of fatty acids, initiating the diterminal degradation pathway (Refs. 12-14; for a review, see Ref. 15). Sequential gene disruption revealed that in C. maltosa, four of its eight CYP52 genes, namely CYP52A3, CYP52A4, CYP52A5, and CYP52A9, are directly involved in alkane assimilation (16). After heterologous expression in Saccharomyces cerevisiae, each of the corresponding P450 isoenzymes was found to exhibit an individual substrate specificity in terms of the preferred class (n-alkanes or fatty acids) and the chain length of the hydroxylated aliphatic compounds (17,18).In the present study, we addressed the question of whether P450 monooxygenases may be involved not only in the primary hydroxylation reactions mentioned above but also in the subsequent oxidation steps leading to the formation of fatty acids and long-chain ...

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Section: Discussionmentioning

confidence: 55%

mentioning

confidence: 99%

Oxygenation Cascade in Conversion of n-Alkanes to α,ω-Dioic Acids Catalyzed by Cytochrome P450 52A3

Scheller¹,

Zimmer²,

Becher³

et al. 1998

Journal of Biological Chemistry

155

119

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“…산소가 이용 가능하다면, 효모와 같은 진핵 미생물은 n-알칸을 알코 올로의 산화와 지방산의 ω-히드록시화(hydroxylation)를 시킨다 (Scheller et al, 1998). 효모에 의한 지방족 탄화수소의 산화 과정에서 mono-또는 di-말단 분해가 가능하다 (Blasig et al, 1988;Mauersberger et al, 1996;Schunck et al, 1987 and Markovetz 1970;Kirschner et al, 2007) 에스테르 가수분 해효소(esterase)에 의해 알코올 및 지방산으로 가수분해된다.…”

Section: 휘발성 향기성분 분석unclassified

Characteristics of the Fruit Quality and Volatile Compounds of ‘Cheongsoo’ Grape by Treatment with Different Plant Growth Regulators

Chang,

Jung,

Hur

et al. 2018

HST

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“…Product feed-back inhibition is involved in the bioconversion of alkane inside cells [18]. Because enzyme system which catalyses aY x-oxidation is an inducible enzyme [10], it is very possible that the inhibition is on the level of enzyme molecule.…”

Section: Chemical Structured Modelmentioning

confidence: 99%

Secretion in long-chain dicarboxylic acid fermentation

Lin

Cao

Zhu

et al. 2000

Bioprocess Engineering

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A new experimental method was established to investigate 1,11-dicarboxylic acid (DCA 13 ) secretion in alkane-assimulating yeast, Candida tropicalis. By this method, phenomenon of acid production in resting cells was observed. The whole process can be divided into two phases: the acid secretion phase and the coupling phase of both acid secretion and alkane bioconversion. Extracellular pH and DCA 2À 13 played important roles in this process. High extracellular pH and low DCA 2À 13 can facilitate acid secretion. A chemical structured model was proposed to analyze these two factors detailedly. Model parameters were simulated by the random search method. Simulated data ®tted the experimental results so well that the maximum error between them was less than 5%. This kind of experimental method and kinetic analysis could also be used in other organic acid fermentation.

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Degradation of long-chain n-alkanes by the yeast Candida maltosa

Cited by 40 publications

References 1 publication

Oxygenation Cascade in Conversion of n-Alkanes to α,ω-Dioic Acids Catalyzed by Cytochrome P450 52A3

Oxygenation Cascade in Conversion of n-Alkanes to α,ω-Dioic Acids Catalyzed by Cytochrome P450 52A3

Characteristics of the Fruit Quality and Volatile Compounds of ‘Cheongsoo’ Grape by Treatment with Different Plant Growth Regulators

Secretion in long-chain dicarboxylic acid fermentation

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