Biosynthesis of the C18 family of cutin acids. ι-Hydroxyoleic acid, ι-hydroxy-9,10-epoxystearic acid, 9,10,18-trihydroxystearic acid, and their Δ<sup>12</sup>-unsaturated analogs

Kolattukudy, Pappachan E.; Walton, Terence J.; Kushwaha, R. P. S.

doi:10.1021/bi00746a029

Cited by 56 publications

(20 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…They are also associated with acute respiratory distress syndrome and severe burns (16). In addition, they are found in many polymeric plant cuticles as constitutive monomers (17) and hence can be derived from vegetable food intake. The biological roles of these products and derivatives are still poorly understood.…”

mentioning

confidence: 99%

Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides

Quéré

Plée-Gautier

Potin

et al. 2004

Journal of Lipid Research

View full text Add to dashboard Cite

CYP4F isoforms are involved in the oxidation of important cellular mediators such as leukotriene B 4 (LTB4) and prostaglandins. The proinflammatory agent LTB4 and cytotoxic leukotoxins have been associated with several inflammatory diseases. We present evidence that the hydroxylation of Z 9(10)-epoxyoctadecanoic, Z 9(10)-epoxyoctadec-Z 12-enoic, and Z 12(13)-epoxyoctadec-Z 9-enoic acids and that of monoepoxides from arachidonic acid [epoxyeicosatrienoic acid (EET)] is important in the regulation of leukotoxin and EET activity. These three epoxidized derivatives from the C18 family (C18-epoxides) were converted to 18-hydroxy-C18-epoxides by human hepatic microsomes with apparent K m values of between 27.6 and 175 M. Among recombinant P450 enzymes, CYP4F2 and CYP4F3B catalyzed mainly the -hydroxylation of C18-epoxides with an apparent V max of between 0.84 and 15.0 min ؊ 1 , whereas the apparent V max displayed by CYP4F3A, the isoform found in leukocytes, ranged from 3.0 to 21.2 min ؊ 1 . The rate of -hydroxylation by CYP4A11 was experimentally found to be between 0.3 and 2.7 min ؊ 1 . CYP4F2 and CYP4F3 exhibited preferences for -hydroxylation of Z 8(9)-EET, whereas human liver microsomes preferred Z 11(12)-EET and, to a lesser extent, Z 8(9)-EET. Moreover, vicinal diol from both C18-epoxides and EETs were -hydroxylated by liver microsomes and by CYP4F2 and CYP4F3. These data support the hypothesis that the human CYP4F subfamily is involved in the -hydroxylation of fatty acid epoxides. These findings demonstrate that another pathway besides conversion to vicinal diol or chain shortening by ␤ -oxidation exists for fatty acid epoxide inactivation. -Le Quéré, V., E. Plée-Gautier, P. Potin, S. Madec, and J-P. Salaün. Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides.

show abstract

mentioning

confidence: 99%

Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides

Quéré

Plée-Gautier

Potin

et al. 2004

Journal of Lipid Research

View full text Add to dashboard Cite

show abstract

“…To determine whether the bacterial cutinase releases all types of cutin monomers or a selected class of monomers, the enzyme preparation was incubated with 14C-labeled apple cutin in which all classes of monomers were known to be labeled (6). Thin-layer chromatographic analysis of the products showed that all classes of apple cutin monomers were released (Fig.…”

Section: Resultsmentioning

confidence: 99%

Discovery of a cutinase-producing Pseudomonas sp. cohabiting with an apparently nitrogen-fixing Corynebacterium sp. in the phyllosphere

Strzalka¹,

Chandra²,

Kolattukudy³

1987

J Bacteriol

View full text Add to dashboard Cite

A phyllospheric bacterial culture, previously reported to partially replace nitrogen fertilizer (B. R. Patti and A. K. Chandra, Plant Soil 61:419-427, 1981) was found to contain a fluorescent pseudomonas which was identified as Pseudomonas putida and a Corynebacterium sp. The P. putida isolate was found to produce an extraceliular cutinase when grown in a medium containing cutin, the polyester structural component of plant cuticle. The Corynebacterium sp. grew on nitrogen-free medium but could not produce cutinase under any induction conditions tested, whereas P. putida could not grow on nitrogen-free medium. When cocultured with the nitrogen-fixing Corynebacterium sp., the P. putida isolate grew in a nitrogen-free medium, suggesting that the former provided fixed N2 for the latter. These results suggest that the two species coexist on the plant surface, with one providing carbon and the other providing reduced nitrogen for their growth. The presence of cutin in the medium induced cutinase production by P. putida. However, unlike the previously studied fungal systems, cutin hydrolysate did not induce cutinase. Thin-layer chromatographic analysis of the products released from labeled apple fruit cutin showed that the extracellular enzyme released all classes of cutin monomers. This enzyme also catalyzed hydrolysis of the model ester substrates, p-nitrophenyl esters of fatty acids, and optimal conditions were determined for a spectrophotometric assay with p-nitrophenyl butyrate as the substrate. It did not hydrolyze triacyl glycerols, indicating that the cutinase activity was not due to a nonspecific lipase. It showed a broad pH optimum between 8.0 and 10.5 with 3H-labeled apple cutin as the substrate. Diisopropylfluorophosphate severely inhibited the enzyme, whereas thiol-directed reagents did not inhibit it, suggesting that catalysis by this bacterial cutinase involves active serine.It has been suggested that a well-established and mixed population of microorganisms in the phyllosphere could make a substantial contribution to the nitrogen requirements of field vegetation (16). Some nitrogen-fixing organisms have been isolated from the leaf surface (8, 13, 18). These nitrogen fixers, when sprayed on the crop plants, increased crop yield when compared with crops which received no nitrogen fertilizers (8). The carbon source for these organisms on the leaf surface is not known. Proposed sources of nutrients include leaf exudates or organic deposits on the leaf surface. Whether these nitrogen fixers are capable of utilizing any of the leaf surface components has not been determined. If the microorganisms are to utilize the insoluble polymer cutin on the leaf surface, these organisms would have to produce an extracellular cutinase. Although cutinases have been purified and characterized from fungi and pollen (2, 3), little is known about bacterial cutinase. In this paper we report that a phyllospheric fluorescent Pseudomonas putida strain, coisolated with a nitrogen-fixing bacterium, may be induced to produce cutina...

show abstract

“…From such results we concluded that palmitic acid was hydroxylated first at the co-carbon followed by another hydroxylation at C-10. Incorporation of specifically labeled precursors into cutin and suberin in tissues slices showed that w-hydroxylation of linoleic acid and/or oleic acid was also involved in the biosynthesis of the major monomers of cutin and suberin (5,13 (soluble PVP, Mr 400,000) was provided by GAF Corp. Carbon monoxide (research grade, 99.99%) was purchased from Matheson Gas Products, while the other gases were obtained from Liquid Air, Inc. Hexadecane-1,16-dioic acid was purchased from K & K Lab., 16-hydroxyhexadecanoic acid from Aldrich Chemical Co., and 2-hydroxyhexadecanoic acid from Analabs, Inc. Hexadecane-1,16-diol and hexadecane-1,2-diol were prepared by LiAlH4 reduction of hexadecane-1,16-dioic acid and 2-hydroxyhexadecanoic acid, respectively.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

Biosynthesis of Cutin ω-Hydroxylation of Fatty Acids by a Microsomal Preparation from Germinating Vicia faba

Soliday¹,

Kolattukudy²

1977

Plant Physiol.

View full text Add to dashboard Cite

ci-Hydroxylation of fatty acids, which is a key reaction in the biosynthesis of cutin and suberin, has been demonstrated for the first time in a cell-free preparation from a higher plant. A crude microsomal fraction (105,000g pellet) from germinating embryonic shoots of Vicia faba catalyzed the conversion of palmitic acid to ci-hydroxypaimitic acid. As the crude cell-free preparation also catalyzes the formation of other hydroxy acids such as a-and l8-hydroxy acids, the o-hydroxylation product was identified by gas chromatography on a polyester column and reverse phase, high performance liquid chromatography, two techniques which were shown to resolve the positional isomers. Gas chromatographic analysis of the dicarboxylic acid obtained by CrO3 oxidation of the enzymic product also confirmed the identity of the enzymic whydroxylation product. This enzymic hydroxylation required 02 and NADPH, but substitution of NADH resulted in nearly half the reaction rate obtained with NADPH. Maximal rates of w-hydroxylation occurred at pH 8 and the rate increased in a sigmoidal manner with increasing concentrations of palmitic acid. This w-hydroxylation was inhibited by the cassicad mixed function oxidase inhibitors such as metal chelators (ophenanthroline, 8-hydroxyquinoline, and a,a-dipyridyl), NaN3 and thiol reagents (N-ethylmaleimide andp-chloromercuribenzoate). As expected of a hydroxylase, involving cytochrome P450, the present c-hydroxylase was inhibited by CO and this enzyme system showed unusually high sensitivity to this inhibition; 10% CO caused inhibition and 30% CO completely inhibited the reaction. Another unusual feature was that the inhibition caused by any level of CO could not be reversed by light (420-460 nm).Palmitic acid, 16-hydroxypalmitic acid, and 10,16-dihydroxypalmitic acid constitute the most common components of cutin (10,15). Exogenous labeled palmitic acid was incorporated into both hydroxy acids, whereas labeled 16-hydroxypalmitic acid was incorporated specifically into the dihydroxy acid in Vicia faba leaf discs (12). From such results we concluded that palmitic acid was hydroxylated first at the co-carbon followed by another hydroxylation at C-10. Incorporation of specifically labeled precursors into cutin and suberin in tissues slices showed that w-hydroxylation of linoleic acid and/or oleic acid was also involved in the biosynthesis of the major monomers of cutin and suberin (5,13 (soluble PVP, Mr 400,000) was provided by GAF Corp. Carbon monoxide (research grade, 99.99%) was purchased from Matheson Gas Products, while the other gases were obtained from Liquid Air, Inc. Hexadecane-1,16-dioic acid was purchased from K & K Lab., 16-hydroxyhexadecanoic acid from Aldrich Chemical Co., and 2-hydroxyhexadecanoic acid from Analabs, Inc. Hexadecane-1,16-diol and hexadecane-1,2-diol were prepared by LiAlH4 reduction of hexadecane-1,16-dioic acid and 2-hydroxyhexadecanoic acid, respectively. Both of these diol standards were purified by TLC on Silica Gel G with diethyl ether-hexane-methanol (...

show abstract

Biosynthesis of the C18 family of cutin acids. ι-Hydroxyoleic acid, ι-hydroxy-9,10-epoxystearic acid, 9,10,18-trihydroxystearic acid, and their Δ¹²-unsaturated analogs

Cited by 56 publications

References 46 publications

Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides

Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides

Discovery of a cutinase-producing Pseudomonas sp. cohabiting with an apparently nitrogen-fixing Corynebacterium sp. in the phyllosphere

Biosynthesis of Cutin ω-Hydroxylation of Fatty Acids by a Microsomal Preparation from Germinating Vicia faba

Contact Info

Product

Resources

About

Biosynthesis of the C18 family of cutin acids. ι-Hydroxyoleic acid, ι-hydroxy-9,10-epoxystearic acid, 9,10,18-trihydroxystearic acid, and their Δ12-unsaturated analogs

Cited by 56 publications

References 46 publications

Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides

Human CYP4F3s are the main catalysts in the oxidation of fatty acid epoxides

Discovery of a cutinase-producing Pseudomonas sp. cohabiting with an apparently nitrogen-fixing Corynebacterium sp. in the phyllosphere

Biosynthesis of Cutin ω-Hydroxylation of Fatty Acids by a Microsomal Preparation from Germinating Vicia faba

Contact Info

Product

Resources

About

Biosynthesis of the C18 family of cutin acids. ι-Hydroxyoleic acid, ι-hydroxy-9,10-epoxystearic acid, 9,10,18-trihydroxystearic acid, and their Δ¹²-unsaturated analogs