Oleate Hydratase Catalyzes the Hydration of a Nonactivated Carbon-Carbon Bond

Bevers, Loes E.; Pinkse, Martijn W. H.; Verhaert, Peter; Hagen, Wilfred R.

doi:10.1128/jb.00306-09

Cited by 87 publications

(71 citation statements)

References 13 publications

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“…The MCRA protein family is highly conserved among different bacterial species, including gram-positive and gram-negative bacteria, and some of them have FA hydratase activity ( 12,13,(16)(17)(18)(19)28 ).…”

Section: Discussionmentioning

confidence: 99%

“…However, the hydratase responsible for the conversion of LA to 13-hydroxycis -9-octadecenoic acid has not yet been identifi ed, and the physiological activities of 13-hydroxy-cis -9-octadecenoic acid are unclear. As for the known bacterial hydratases, the length of the carbon chain in the substrate FA is limited to C16 and C18 ( 1,12,13,(16)(17)(18)(19).…”

Section: Lipid Analysesmentioning

confidence: 99%

See 1 more Smart Citation

A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

Hirata

Kishino

Park

et al. 2015

Journal of Lipid Research

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This article is available online at http://www.jlr.org revealed that the metabolites of LA, 10-hydroxy-cis -12-octadecenoic acid and 13-hydroxy-cis -9-octadecenoic acid, were detected at higher levels in the intestines of specifi c pathogen-free (SPF) mice than in those of germ-free mice, indicating that gastrointestinal microbes play a role in modifying the FA profi le of their host mice.The physiological functions of 10-hydroxy FAs and their derivatives begin to become clear. 10-Hydroxy-cis -12-octadecenoic acid ameliorates intestinal epithelial barrier impairment via the G protein-coupled receptor 40 (GPR40)-MAPK/ERK kinase (MEK)-ERK pathway and may be useful in the treatment of tight junction-related disorders such as infl ammatory bowel disease ( 3 ). 10-Oxo-cis -12-octadecenoic acid potently activates PPAR ␥ , a master regulator of adipocyte differentiation, and may be involved in the regulation of host energy metabolism ( 5 ).The production of 10-hydroxy-cis -12-octadecenoic acid from LA has been reported in many bacteria, including Lactobacillus acidophilus ( 7 ), L. plantarum ( 8, 9 ), Streptococcus bovis ( 10 ), and Stenotrophomonas nitritireducens ( 11 ). In our previous study, we reported that the enzyme linoleic acid hydratase (CLA-HY) from L. plantarum AKU 1009a catalyzes the hydration of the cis -9 double bond in C16 and C18 FAs, forming the corresponding 10-hydroxy FAs ( 12 ). Volkov et al. ( 13 ) reported that SPH, a hydratase from Streptococcus pyogenes M49, is a myosin-cross-reactive antigen (MCRA) family protein that catalyzes the hydration of the cis-9 and cis -12 double bonds in C16 and C18 FAs, forming the corresponding 10-hydroxy and 10,13-dihydroxy FAs.The production of 13-hydroxy-cis -9-octadecenoic acid from LA has also been reported in some anaerobic bacteria. Hudson et al. ( 10 ) reported that a ruminant bacterium, S. bovis JB1, converts LA into 13-hydroxy-cis -9-octadecenoic acid, and Kishimoto et al. ( 14 ) reported that L. acidophilus Abstract Hydroxy FAs, one of the gut microbial metabolites of PUFAs, have attracted much attention because of their various bioactivities. The purpose of this study was to identify lactic acid bacteria with the ability to convert linoleic acid (LA) to hydroxy FAs. A screening process revealed that a gut bacterium, Lactobacillus acidophilus NTV001, converts LA mainly into 13-hydroxy-cis -9-octadecenoic acid and resulted in the identifi cation of the hydratase responsible, fatty acid hydratase 1 (FA-HY1) . Recombinant FA-HY1 was purifi ed, and its enzymatic characteristics were investigated. FA-HY1 could convert not only C18 PUFAs but also C20 and C22 PUFAs. C18 PUFAs with a cis carbon-carbon double bond at the ⌬ 12 position were converted into the corresponding 13-hydroxy FAs. Arachidonic acid and DHA were converted into the corresponding 15-hydroxy FA and 14-hydroxy FA, respectively. To the best of our knowledge, this is the fi rst report of a bacterial FA hydratase that can convert C20 and C22 PUFAs into the corresponding hydroxy FAs. These novel ...

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Section: Discussionmentioning

confidence: 99%

Section: Lipid Analysesmentioning

confidence: 99%

A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

Hirata

Kishino

Park

et al. 2015

Journal of Lipid Research

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“…The enzyme involved in the conversion of oleic acid to 10-HSA was first identified in E. meningoseptica and was named OhyA because of its highest activity being toward oleic acid among unsaturated fatty acids (6). The biochemical properties of OhyAs from other bacteria, including S. pyogenes, M. caseolyticus (12), L. fusiformis (11), S. maltophilia (13), and B. breve (8,9), were subsequently characterized.…”

Section: Discussionmentioning

confidence: 99%

“…The biochemical properties of OhyAs from Elizabethkingia meningoseptica (6,7), Bifidobacterium breve (8,9), Streptococcus pyogenes (10), Lysinibacillus fusiformis (11), Macrococcus caseolyticus (12), Stenotrophomonas maltophilia (13), and Stenotrophomonas nitritireducens (14) have been characterized to date. All OhyAs contain flavin adenine dinucleotide (FAD)-binding motifs.…”

mentioning

confidence: 99%

Comparison of Biochemical Properties of the Original and Newly Identified Oleate Hydratases from Stenotrophomonas maltophilia

Kang

Seo

Shin

et al. 2017

Appl Environ Microbiol

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Oleate hydratases (OhyAs) catalyze the conversion of unsaturated fatty acids to 10-hydroxy fatty acids, which are used as precursors of important industrial compounds, including lactones and -hydroxycarboxylic and ␣, -dicarboxylic acids. The genes encoding OhyA and a putative fatty acid hydratase in Stenotrophomonas maltophilia were identified by genomic analysis. The putative fatty acid hydratase was purified and identified as an oleate hydratase (OhyA2) based on its substrate specificity. The activity of OhyA2 as a holoenzyme was not affected by adding cofactors, whereas the activity of the original oleate hydratase (OhyA1) showed an increase. Thus, all characterized OhyAs were categorized as either OhyA1 or OhyA2 based on the activities of holoenzymes upon adding cofactors, which were determined by the type of the fourth conserved amino acid of flavin adenine dinucleotide (FAD)-binding motif. The hydration activities of S. maltophilia OhyA2 toward unsaturated fatty acids, including oleic acid, palmitoleic acid, linoleic acid, ␣-linolenic acid, and ␥-linolenic acid, were greater than those of OhyA1. Moreover, the specific activity of S. maltophilia OhyA2 toward unsaturated fatty acids, with the exception of ␥-linolenic acid, was the highest among all reported OhyAs. IMPORTANCE All characterized OhyAs were categorized as OhyA1s or OhyA2s based on the different properties of the reported and newly identified holo-OhyAs in S. maltophilia upon the addition of cofactors. OhyA2s showed higher activities toward polyunsaturated fatty acids (PUFAs), including linoleic acid, ␣-linolenic acid, and ␥-linolenic acid, than those of OhyA1s. This suggests that OhyA2s can be used more effectively to convert plant oils to 10-hydroxy fatty acids because plant oils contain not only oleic acid but also PUFAs. The hydration activity of the newly identified OhyA2 from S. maltophilia toward oleic acid was the highest among the activity levels reported so far. Therefore, this enzyme is an efficient biocatalyst for the conversion of plant oils to 10-hydroxy fatty acids, which can be further converted to important industrial materials. KEYWORDS Stenotrophomonas maltophilia, enzyme characterization, oleate hydrataseO leate hydratase (OhyA) converts unsaturated fatty acids to 10-hydroxy fatty acids, which are then converted to ␥-lactones by the yeasts Candida boidinii and Waltomyces lipofer (1, 2). ␥-Lactones are flavor compounds used in food and cosmetics (3). Multistep enzymatic reactions involving OhyA, alcohol dehydrogenase, Baeyer-Villiger monooxygenases, and esterase convert unsaturated fatty acids to -hydroxycarboxylic and ␣, -dicarboxylic acids (4), which are used in the preparation of resins, nylons, plastics, and lubricants (5). An effective OhyA is necessary for the efficient production of ␥-lactones, -hydroxycarboxylic acids, and ␣, -dicarboxylic acids.

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“…Recently, MCRAs from S. pyogenes and Pseudomonas sp. were demonstrated to have hydratase activity (Bevers et al, 2009;Volkov et al, 2010). In addition, the MCRA from S. pyogenes was shown to contribute to blood survival and adherence to keratinocytes (Volkov et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Functional and phenotypic characterization of a protein from Lactobacillus acidophilus involved in cell morphology, stress tolerance and adherence to intestinal cells

O’Flaherty

Klaenhammer

2010

Microbiology

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Structural components of the cell surface have an impact on some of the beneficial attributes of probiotic bacteria. In silico analysis of the L. acidophilus NCFM genome sequence revealed the presence of a putative cell surface protein that was predicted to be a myosin cross-reactive antigen (MCRA). As MCRAs are conserved among many probiotic bacteria, we used the uppbased counterselective gene replacement system, designed recently for use in L. acidophilus, to determine the functional role of this gene (LBA649) in L. acidophilus NCFM. Phenotypic assays were undertaken with the parent strain (NCK1909) and deletion mutant (NCK2015) to assign a function for this gene. The growth of NCK2015 (DLBA649) was reduced in the presence of lactate, acetate, porcine bile and salt. Adhesion of NCK2015 to Caco-2 cells was substantially reduced for both stationary-phase (~45 % reduction) and exponential-phase cells (~50 % reduction). Analysis of NCK2015 by scanning electron microscopy revealed a longer cell morphology after growth in MRS broth compared to NCK1909. These results indicate a role for LBA649 in stress tolerance, cell wall division and adherence to Caco-2 cells. INTRODUCTIONSpecies of the genus Lactobacillus, such as Lactobacillus delbrueckii subsp. bulgaricus and Lactobacillus helveticus, have long been used in fermented foods as starter cultures in yogurt and in cheese manufacture, respectively. Others are classified as probiotic bacteria and fall into the definition of a probiotic as defined by the World Health Organization: 'live microorganisms which when administered in adequate amounts confer a health benefit on the host' (www.who.int/ foodsafety/publications/fs_management/probiotics2/en/). Lactobacillus acidophilus is one of the most widely used probiotic species in the US and has demonstrated health benefits, such as lowering levels of cold and influenza-like symptoms during antibiotic administration in children (Leyer et al., 2009) and decreasing the duration of diarrhoea (Liévin-Le Moal et al., 2007). Additional studies with L. acidophilus have demonstrated modulation of intestinal pain and induction of pain receptors in intestinal cells which exert analgesic effects in colitis models (Rousseaux et al., 2007), and activation of toll-like receptors and dendritic cells (Konstantinov et al., 2008;Mohamadzadeh & Klaenhammer, 2008).Understanding probiotic bacteria and their effector molecules that contribute to health-promoting properties has been facilitated by advances in molecular tools and 'omic' technologies. Since the genome sequence of L. acidophilus was published in there have been numerous studies on the transcriptome of this bacterium under conditions such as acid and bile stress, and carbohydrate metabolism Barrangou et al., 2006;Pfeiler & Klaenhammer, 2009;Pfeiler et al., 2007). In addition, gene inactivation or deletion has confirmed the role of genes contributing to probiotic traits, such as bile tolerance (Pfeiler & Klaenhammer, 2009;Pfeiler et al., 2007) METHODSBacterial strains and growth con...

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Oleate Hydratase Catalyzes the Hydration of a Nonactivated Carbon-Carbon Bond

Cited by 87 publications

References 13 publications

A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

A novel unsaturated fatty acid hydratase toward C16 to C22 fatty acids from Lactobacillus acidophilus

Comparison of Biochemical Properties of the Original and Newly Identified Oleate Hydratases from Stenotrophomonas maltophilia

Functional and phenotypic characterization of a protein from Lactobacillus acidophilus involved in cell morphology, stress tolerance and adherence to intestinal cells

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