Biochemical characterization and FAD-binding analysis of oleate hydratase from Macrococcus caseolyticus

Joo, Young-Chul; Jeong, Ki-Woong; Yeom, Soo‐Jin; Kim, Yeong-Su; Kim, Yangmee; Oh, Deok‐Kun

doi:10.1016/j.biochi.2011.12.011

Cited by 58 publications

(62 citation statements)

References 29 publications

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“…The same results were reported in OhyAs from S. pyogenes (10) and M. caseolyticus (12). Thus, apo-OhyAs were shown to be cofactor-dependent enzymes.…”

Section: Discussionsupporting

confidence: 82%

“…OhyAs contain the FAD-binding motifs GXGXXS (A/G) X 15 E (D) X 5 E with five conserved residues, where X denotes any amino acid (12). However, the fourth conserved amino acids of OhyA1 and OhyA2 from S. maltophilia and OhyA2 from S. nitritireducens differed as Glu at position 50, Ala at position 86, and Gln at position 80, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…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. These OhyAs showed low activity toward PUFAs.…”

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%

“…All OhyAs contain flavin adenine dinucleotide (FAD)-binding motifs. When FAD was not bound to OhyA, its catalytic activity was abolished (12) or significantly reduced (7). Thus, OhyAs are FAD-dependent enzymes belonging to the myosin cross-reactive antigen (MCRA) protein family, and they are widely distributed in bacteria, especially in pathogenic and intestinal bacteria.…”

mentioning

confidence: 99%

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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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“…The same results were reported in OhyAs from S. pyogenes (10) and M. caseolyticus (12). Thus, apo-OhyAs were shown to be cofactor-dependent enzymes.…”

Section: Discussionsupporting

confidence: 82%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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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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Organic Synthesis with Lyases

2022

Enzyme‐Based Organic Synthesis

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Biotransformation of Linoleic Acid into Hydroxy Fatty Acids and Carboxylic Acids Using a Linoleate Double Bond Hydratase as Key Enzyme

Kim

Song

et al. 2015

Adv Synth Catal

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Hydroxy fatty acids are used as starting materials for the production of secondary metabolites and signalling molecules as well as in the manufacture of industrial fine chemicals. However, these compounds are usually difficult to produce from renewable biomass by chemical means. In this study, linoleate double bond hydratases of Lactobacillus acidophilus NBRC 13951 were cloned for the first time. These enzymes were highly specific for the hydration of the C‐9 or the C‐12 double bond of unsaturated fatty acids (e.g., linoleic acid). Thereby, the enzymes allowed the selective production of hydroxy fatty acids such as 13‐hydroxy‐cis‐9‐octadecenoic acid and 10‐hydroxy‐cis‐12‐octadecenoic acid from linoleic acid. In addition, the hydroxy fatty acids were further converted into industrially relevant carboxylic acids (e.g., 12‐hydroxy‐cis‐9‐dodecenoic acid, α,ω‐tridec‐9‐enedioic acid) and lactones (i.e., δ‐decalactone, γ‐dodecelactone) via whole‐cell biocatalysis using an enzyme cascade. This study thus contributes to the preparation of hydroxy fatty acids, unsaturated carboxylic acids, and lactones from renewable unsaturated fatty acids.magnified image

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Biochemical characterization and FAD-binding analysis of oleate hydratase from Macrococcus caseolyticus

Cited by 58 publications

References 29 publications

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

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

Organic Synthesis with Lyases

Biotransformation of Linoleic Acid into Hydroxy Fatty Acids and Carboxylic Acids Using a Linoleate Double Bond Hydratase as Key Enzyme

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