{"entity": "journal", "iuid": "de90a86d542c4b22b04e1bdbf35a13d6", "timestamp": "2026-08-13T18:32:57.647Z", "links": {"self": {"href": "https://publications.scilifelab.se/journal/Biochim.%20Biophys.%20Acta.json"}, "display": {"href": "https://publications.scilifelab.se/journal/Biochim.%20Biophys.%20Acta"}}, "title": "Biochim. Biophys. Acta", "issn": "1878-2434", "issn-l": "0006-3002", "publications_count": 9, "publications": [{"entity": "publication", "iuid": "00da8bb63d494469a50387cdec49cd5f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/00da8bb63d494469a50387cdec49cd5f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/00da8bb63d494469a50387cdec49cd5f"}}, "title": "Replacement of two amino acids of 9R-dioxygenase-allene oxide synthase of Aspergillus niger inverts the chirality of the hydroperoxide and the allene oxide.", "authors": [{"family": "Sooman", "given": "Linda", "initials": "L"}, {"family": "Wennman", "given": "Anneli", "initials": "A"}, {"family": "Hamberg", "given": "Mats", "initials": "M"}, {"family": "Hoffmann", "given": "Inga", "initials": "I"}, {"family": "Oliw", "given": "Ernst H", "initials": "EH"}], "type": "journal article", "published": "2016-02-00", "journal": {"volume": "1861", "issn": "0006-3002", "issue": "2", "pages": "108-118", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "The genome of Aspergillus niger codes for a fusion protein (EHA25900), which can be aligned with ~50% sequence identity to 9S-dioxygenase (DOX)-allene oxide synthase (AOS) of Fusarium oxysporum, homologues of the Fusarium and Colletotrichum complexes and with over 62% sequence identity to homologues of Aspergilli, including (DOX)-9R-AOS of Aspergillus terreus. The aims were to characterize the enzymatic activities of EHA25900 and to identify crucial amino acids for the stereospecificity. Recombinant EHA25900 oxidized 18:2n-6 sequentially to 9R-hydroperoxy-10(E),12(Z)-octadecadienoic acid (9R-HPODE) and to a 9R(10)-allene oxide. 9S- and 9R-DOX-AOS catalyze abstraction of the pro-R hydrogen at C-11, but the direction of oxygen insertion differs. A comparison between twelve 9-DOX domains of 9S- and 9R-DOX-AOS revealed conserved amino acid differences, which could contribute to the chirality of products. The Gly616Ile replacement of 9R-DOX-AOS (A. niger) increased the biosynthesis of 9S-HPODE and the 9S(10)-allene oxide, whereas the Phe627Leu replacement led to biosynthesis of 9S-HPODE and the 9S(10)-allene oxide as main products. The double mutant (Gly616Ile, Phe627Leu) formed over 90% of the 9S stereoisomer of HPODE. 9S-HPODE was formed by antarafacial hydrogen abstraction and oxygen insertion, i.e., the original H-abstraction was retained but the product chirality was altered. We conclude that 9R-DOX-AOS can be altered to 9S-DOX-AOS by replacement of two amino acids (Gly616Ile, Phe627Leu) in the DOX domain.", "doi": "10.1016/j.bbalip.2015.11.009", "pmid": "26603902", "labels": {"National Genomics Infrastructure": "Service", "NGI Uppsala (Uppsala Genome Center)": "Service"}, "xrefs": [{"db": "pii", "key": "S1388-1981(15)00214-0"}], "notes": [], "created": "2017-05-02T12:57:43.643Z", "modified": "2020-01-21T13:56:00.469Z"}, {"entity": "publication", "iuid": "53e1d8e81eed49af8521e5c3d8db3053", "links": {"self": {"href": "https://publications.scilifelab.se/publication/53e1d8e81eed49af8521e5c3d8db3053.json"}, "display": {"href": "https://publications.scilifelab.se/publication/53e1d8e81eed49af8521e5c3d8db3053"}}, "title": "Trimeric microsomal glutathione transferase 2 displays one third of the sites reactivity.", "authors": [{"family": "Ahmad", "given": "Shabbir", "initials": "S"}, {"family": "Thulasingam", "given": "Madhuranayaki", "initials": "M"}, {"family": "Palombo", "given": "Isolde", "initials": "I"}, {"family": "Daley", "given": "Daniel O", "initials": "DO"}, {"family": "Johnson", "given": "Kenneth A", "initials": "KA"}, {"family": "Morgenstern", "given": "Ralf", "initials": "R"}, {"family": "Haeggstr\u00f6m", "given": "Jesper Z", "initials": "JZ"}, {"family": "Rinaldo-Matthis", "given": "Agnes", "initials": "A"}], "type": "journal article", "published": "2015-10-00", "journal": {"volume": "1854", "issn": "0006-3002", "issue": "10 Pt A", "pages": "1365-1371", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "Human microsomal glutathione transferase 2 (MGST2) is a trimeric integral membrane protein that belongs to the membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG) family. The mammalian MAPEG family consists of six members where four have been structurally determined. MGST2 activates glutathione to form a thiolate that is crucial for GSH peroxidase activity and GSH conjugation reactions with electrophilic substrates, such as 1-chloro-2,4-dinitrobenzene (CDNB). Several studies have shown that MGST2 is able to catalyze a GSH conjugation reaction with the epoxide LTA4 forming the pro-inflammatory LTC4. Unlike its closest homologue leukotriene C4 synthase (LTC4S), MGST2 appears to activate its substrate GSH using only one of the three potential active sites [Ahmad S, et al. (2013) Biochemistry. 52, 1755-1764]. In order to demonstrate and detail the mechanism of one-third of the sites reactivity of MGST2, we have determined the enzyme oligomeric state, by Blue native PAGE and Differential Scanning Calorimetry, as well as the stoichiometry of substrate and substrate analog inhibitor binding to MGST2, using equilibrium dialysis and Isothermal Titration Calorimetry, respectively. Global simulations were used to fit kinetic data to determine the catalytic mechanism of MGST2 with GSH and CDNB (1-chloro-2,4-dinitrobenzene) as substrates. The best fit was observed with 1/3 of the sites catalysis as compared with a simulation where all three sites were active. In contrast to LTC4S, MGST2 displays a 1/3 the sites reactivity, a mechanism shared with the more distant family member MGST1 and recently suggested also for microsomal prostaglandin E synthase-1.", "doi": "10.1016/j.bbapap.2015.06.003", "pmid": "26066610", "labels": {"Protein Science Facility (PSF)": null}, "xrefs": [{"db": "pii", "key": "S1570-9639(15)00169-7"}], "notes": [], "created": "2017-05-02T12:56:29.586Z", "modified": "2017-09-06T11:42:09.098Z"}, {"entity": "publication", "iuid": "d940eb6c61cc4b4b89b657178123b6fc", "links": {"self": {"href": "https://publications.scilifelab.se/publication/d940eb6c61cc4b4b89b657178123b6fc.json"}, "display": {"href": "https://publications.scilifelab.se/publication/d940eb6c61cc4b4b89b657178123b6fc"}}, "title": "Integration of genome-wide of Stat3 binding and epigenetic modification mapping with transcriptome reveals novel Stat3 target genes in glioma cells.", "authors": [{"family": "Kruczyk", "given": "Marcin", "initials": "M"}, {"family": "Przanowski", "given": "Piotr", "initials": "P"}, {"family": "Dabrowski", "given": "Michal", "initials": "M"}, {"family": "Swiatek-Machado", "given": "Karolina", "initials": "K"}, {"family": "Mieczkowski", "given": "Jakub", "initials": "J"}, {"family": "Wallerman", "given": "Ola", "initials": "O"}, {"family": "Ronowicz", "given": "Anna", "initials": "A"}, {"family": "Piotrowski", "given": "Arkadiusz", "initials": "A"}, {"family": "Wadelius", "given": "Claes", "initials": "C"}, {"family": "Kaminska", "given": "Bozena", "initials": "B"}, {"family": "Komorowski", "given": "Jan", "initials": "J"}], "type": "journal article", "published": "2014-11-00", "journal": {"volume": "1839", "issn": "0006-3002", "issue": "11", "pages": "1341-1350", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "Signal transducer and activator of transcription 3 (STAT3) is constitutively activated in many human tumors, including gliomas, and regulates the expression of genes implicated in proliferation, survival, apoptosis, angiogenesis and immune regulation. Only a small fraction of those genes has been proven to be direct STAT3 targets. In gliomas, STAT3 can play tumor suppressive or oncogenic roles depending on the tumor genetic background with target genes being largely unknown.\n\nWe used chromatin immunoprecipitation, promoter microarrays and deep sequencing to assess the genome-wide occupancy of phospho (p)-Stat3 and epigenetic modifications of H3K4me3 and H3ac in C6 glioma cells. This combined assessment identified a list of 1200 genes whose promoters have both Stat3 binding sites and epigenetic marks characteristic for actively transcribed genes. The Stat3 and histone markings data were also intersected with a set of microarray data from C6 glioma cells after inhibition of Jak2/Stat3 signaling. Subsequently, we found 284 genes characterized by p-Stat3 occupancy, activating histone marks and transcriptional changes. Novel genes were screened for their potential involvement in oncogenesis, and the most interesting hits were verified by ChIP-PCR and STAT3 knockdown in human glioma cells.\n\nNon-random association between silent genes, histone marks and p-Stat3 binding near transcription start sites was observed, consistent with its repressive role in transcriptional regulation of target genes in glioma cells with specific genetic background.", "doi": "10.1016/j.bbagrm.2014.07.010", "pmid": "25111868", "labels": {"National Genomics Infrastructure": null, "NGI Uppsala (Uppsala Genome Center)": null}, "xrefs": [{"db": "pii", "key": "S1874-9399(14)00198-9"}], "notes": [], "created": "2017-05-04T15:02:31.898Z", "modified": "2020-01-21T13:56:05.574Z"}, {"entity": "publication", "iuid": "fe6e349a1ea84787b886bf8a2484ca82", "links": {"self": {"href": "https://publications.scilifelab.se/publication/fe6e349a1ea84787b886bf8a2484ca82.json"}, "display": {"href": "https://publications.scilifelab.se/publication/fe6e349a1ea84787b886bf8a2484ca82"}}, "title": "Protein biomarker validation via proximity ligation assays.", "authors": [{"family": "Blokzijl", "given": "A", "initials": "A"}, {"family": "Nong", "given": "R", "initials": "R"}, {"family": "Darmanis", "given": "S", "initials": "S"}, {"family": "Hertz", "given": "E", "initials": "E"}, {"family": "Landegren", "given": "U", "initials": "U"}, {"family": "Kamali-Moghaddam", "given": "M", "initials": "M", "orcid": "0000-0002-1303-2218", "researcher": {"href": "https://publications.scilifelab.se/researcher/290dd535fb414c68bc49a8a2b7995770.json"}}], "type": "journal article", "published": "2014-05-00", "journal": {"volume": "1844", "issn": "0006-3002", "issue": "5", "pages": "933-939", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "The ability to detect minute amounts of specific proteins or protein modifications in blood as biomarkers for a plethora of human pathological conditions holds great promise for future medicine. Despite a large number of plausible candidate protein biomarkers published annually, the translation to clinical use is impeded by factors such as the required size of the initial studies, and limitations of the technologies used. The proximity ligation assay (PLA) is a versatile molecular tool that has the potential to address some obstacles, both in validation of biomarkers previously discovered using other techniques, and for future routine clinical diagnostic needs. The enhanced specificity of PLA extends the opportunities for large-scale, high-performance analyses of proteins. Besides advantages in the form of minimal sample consumption and an extended dynamic range, the PLA technique allows flexible assay reconfiguration. The technology can be adapted for detecting protein complexes, proximity between proteins in extracellular vesicles or in circulating tumor cells, and to address multiple post-translational modifications in the same protein molecule. We discuss herein requirements for biomarker validation, and how PLA may play an increasing role in this regard. We describe some recent developments of the technology, including proximity extension assays, the use of recombinant affinity reagents suitable for use in proximity assays, and the potential for single cell proteomics. This article is part of a Special Issue entitled: Biomarkers: A Proteomic Challenge.", "doi": "10.1016/j.bbapap.2013.07.016", "pmid": "23933049", "labels": {"PLA and Single Cell Proteomics": "", "Affinity Proteomics Uppsala": "Technology development"}, "xrefs": [{"db": "pii", "key": "S1570-9639(13)00288-4"}], "notes": [], "created": "2017-05-04T14:55:27.365Z", "modified": "2023-04-14T13:56:27.888Z"}, {"entity": "publication", "iuid": "ccafdb8f28c341f78c42b9c2635cc244", "links": {"self": {"href": "https://publications.scilifelab.se/publication/ccafdb8f28c341f78c42b9c2635cc244.json"}, "display": {"href": "https://publications.scilifelab.se/publication/ccafdb8f28c341f78c42b9c2635cc244"}}, "title": "Product formation controlled by substrate dynamics in leukotriene A4 hydrolase.", "authors": [{"family": "Stsiapanava", "given": "Alena", "initials": "A"}, {"family": "Tholander", "given": "Fredrik", "initials": "F"}, {"family": "Kumar", "given": "Ramakrishnan B", "initials": "RB"}, {"family": "Qureshi", "given": "Abdul Aziz", "initials": "AA"}, {"family": "Niegowski", "given": "Damian", "initials": "D"}, {"family": "Hasan", "given": "Mahmudul", "initials": "M"}, {"family": "Thunnissen", "given": "Marjolein", "initials": "M"}, {"family": "Haeggstr\u00f6m", "given": "Jesper Z", "initials": "JZ"}, {"family": "Rinaldo-Matthis", "given": "Agnes", "initials": "A"}], "type": "journal article", "published": "2014-02-00", "journal": {"volume": "1844", "issn": "0006-3002", "issue": "2", "pages": "439-446", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "Leukotriene A4 hydrolase/aminopeptidase (LTA4H) (EC 3.3.2.6) is a bifunctional zinc metalloenzyme with both an epoxide hydrolase and an aminopeptidase activity. LTA4H from the African claw toad, Xenopus laevis (xlLTA4H) has been shown to, unlike the human enzyme, convert LTA4 to two enzymatic metabolites, LTB4 and another biologically active product \u0394(6)-trans-\u0394(8)-cis-LTB4 (5(S),12R-dihydroxy-6,10-trans-8,14-cis-eicosatetraenoic acid). In order to study the molecular aspect of the formation of this product we have characterized the structure and function of xlLTA4H. We solved the structure of xlLTA4H to a resolution of 2.3\u00c5. It is a dimeric structure where each monomer has three domains with the active site in between the domains, similar as to the human structure. An important difference between the human and amphibian enzyme is the phenylalanine to tyrosine exchange at position 375. Our studies show that mutating F375 in xlLTA4H to tyrosine abolishes the formation of the LTB4 isomeric product \u0394(6)-trans-\u0394(8)-cis-LTB4. In an attempt to understand how one amino acid exchange leads to a new product profile as seen in the xlLTA4H, we performed a conformer analysis of the triene part of the substrate LTA4. Our results show that the Boltzmann distribution of substrate conformers correlates with the observed distribution of products. We suggest that the observed difference in product profile between the human and the xlLTA4H arises from different level of discrimination between substrate LTA4 conformers.", "doi": "10.1016/j.bbapap.2013.12.003", "pmid": "24333438", "labels": {"Protein Science Facility (PSF)": null}, "xrefs": [{"db": "pii", "key": "S1570-9639(13)00425-1"}], "notes": [], "created": "2017-05-04T15:03:51.494Z", "modified": "2017-09-06T11:42:09.341Z"}, {"entity": "publication", "iuid": "d3162e61d4ce4afb9b8b0254b9f21ab1", "links": {"self": {"href": "https://publications.scilifelab.se/publication/d3162e61d4ce4afb9b8b0254b9f21ab1.json"}, "display": {"href": "https://publications.scilifelab.se/publication/d3162e61d4ce4afb9b8b0254b9f21ab1"}}, "title": "Data processing methods and quality control strategies for label-free LC-MS protein quantification.", "authors": [{"family": "Sandin", "given": "Marianne", "initials": "M"}, {"family": "Teleman", "given": "Johan", "initials": "J"}, {"family": "Malmstr\u00f6m", "given": "Johan", "initials": "J"}, {"family": "Levander", "given": "Fredrik", "initials": "F"}], "type": "journal article", "published": "2014-01-00", "journal": {"volume": "1844", "issn": "0006-3002", "issue": "1 Pt A", "pages": "29-41", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "Protein quantification using different LC-MS techniques is becoming a standard practice. However, with a multitude of experimental setups to choose from, as well as a wide array of software solutions for subsequent data processing, it is non-trivial to select the most appropriate workflow for a given biological question. In this review, we highlight different issues that need to be addressed by software for quantitative LC-MS experiments and describe different approaches that are available. With focus on label-free quantification, examples are discussed both for LC-MS/MS and LC-SRM data processing. We further elaborate on current quality control methodology for performing accurate protein quantification experiments. This article is part of a Special Issue entitled: Computational Proteomics in the Post-Identification Era. Guest Editors: Martin Eisenacher and Christian Stephan.", "doi": "10.1016/j.bbapap.2013.03.026", "pmid": "23567904", "labels": {"Bioinformatics Support, Infrastructure and Training": null, "Bioinformatics Support and Infrastructure": null, "Bioinformatics (NBIS)": null}, "xrefs": [{"db": "pii", "key": "S1570-9639(13)00139-8"}], "notes": [], "created": "2017-05-04T14:56:28.593Z", "modified": "2020-01-21T13:53:20.886Z"}, {"entity": "publication", "iuid": "a011177aefea4d8dbac7e0bc51c6509f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/a011177aefea4d8dbac7e0bc51c6509f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/a011177aefea4d8dbac7e0bc51c6509f"}}, "title": "Long indels are disordered: a study of disorder and indels in homologous eukaryotic proteins.", "authors": [{"family": "Light", "given": "Sara", "initials": "S"}, {"family": "Sagit", "given": "Rauan", "initials": "R"}, {"family": "Ekman", "given": "Diana", "initials": "D"}, {"family": "Elofsson", "given": "Arne", "initials": "A"}], "type": "journal article", "published": "2013-05-00", "journal": {"volume": "1834", "issn": "0006-3002", "issue": "5", "pages": "890-897", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "Proteins evolve through point mutations as well as by insertions and deletions (indels). During the last decade it has become apparent that protein regions that do not fold into three-dimensional structures, i.e. intrinsically disordered regions, are quite common. Here, we have studied the relationship between protein disorder and indels using HMM-HMM pairwise alignments in two sets of orthologous eukaryotic protein pairs. First, we show that disordered residues are much more frequent among indel residues than among aligned residues and, also are more prevalent among indels than in coils. Second, we observed that disordered residues are particularly common in longer indels. Disordered indels of short-to-medium size are prevalent in the non-terminal regions of proteins while the longest indels, ordered and disordered alike, occur toward the termini of the proteins where new structural units are comparatively well tolerated. Finally, while disordered regions often evolve faster than ordered regions and disorder is common in indels, there are some previously recognized protein families where the disordered region is more conserved than the ordered region. We find that these rare proteins are often involved in information processes, such as RNA processing and translation. This article is part of a Special Issue entitled: The emerging dynamic view of proteins: Protein plasticity in allostery, evolution and self-assembly.", "doi": "10.1016/j.bbapap.2013.01.002", "pmid": "23333420", "labels": {"Bioinformatics Support, Infrastructure and Training": null, "Bioinformatics Support and Infrastructure": null, "Bioinformatics (NBIS)": null}, "xrefs": [{"db": "pii", "key": "S1570-9639(13)00007-1"}], "notes": [], "created": "2017-05-04T14:56:20.632Z", "modified": "2020-01-21T13:53:20.724Z"}, {"entity": "publication", "iuid": "0dbbf8978547434d8ec6c1926d36edeb", "links": {"self": {"href": "https://publications.scilifelab.se/publication/0dbbf8978547434d8ec6c1926d36edeb.json"}, "display": {"href": "https://publications.scilifelab.se/publication/0dbbf8978547434d8ec6c1926d36edeb"}}, "title": "Manipulating the genetic code for membrane protein production: what have we learnt so far?", "authors": [{"family": "N\u00f8rholm", "given": "Morten H H", "initials": "MH"}, {"family": "Light", "given": "Sara", "initials": "S"}, {"family": "Virkki", "given": "Minttu T I", "initials": "MT"}, {"family": "Elofsson", "given": "Arne", "initials": "A"}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications.scilifelab.se/researcher/f663c0a9e9e1455cbbf8e6aea13af4a9.json"}}, {"family": "Daley", "given": "Daniel O", "initials": "DO"}], "type": "journal article", "published": "2012-04-00", "journal": {"volume": "1818", "issn": "0006-3002", "issue": "4", "pages": "1091-1096", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "With synthetic gene services, molecular cloning is as easy as ordering a pizza. However choosing the right RNA code for efficient protein production is less straightforward, more akin to deciding on the pizza toppings. The possibility to choose synonymous codons in the gene sequence has ignited a discussion that dates back 50 years: Does synonymous codon use matter? Recent studies indicate that replacement of particular codons for synonymous codons can improve expression in homologous or heterologous hosts, however it is not always successful. Furthermore it is increasingly apparent that membrane protein biogenesis can be codon-sensitive. Single synonymous codon substitutions can influence mRNA stability, mRNA structure, translational initiation, translational elongation and even protein folding. Synonymous codon substitutions therefore need to be carefully evaluated when membrane proteins are engineered for higher production levels and further studies are needed to fully understand how to select the codons that are optimal for higher production. This article is part of a Special Issue entitled: Protein Folding in Membranes.", "doi": "10.1016/j.bbamem.2011.08.018", "pmid": "21884679", "labels": {"Bioinformatics Support, Infrastructure and Training": null, "Bioinformatics Support and Infrastructure": null, "Bioinformatics (NBIS)": ""}, "xrefs": [{"db": "pii", "key": "S0005-2736(11)00280-X"}, {"db": "pmc", "key": "PMC3288168"}, {"db": "mid", "key": "NIHMS328986"}], "notes": [], "created": "2017-05-04T14:56:14.844Z", "modified": "2021-06-16T15:21:58.633Z"}, {"entity": "publication", "iuid": "9ef62eced5e1409b90aec4ff52553390", "links": {"self": {"href": "https://publications.scilifelab.se/publication/9ef62eced5e1409b90aec4ff52553390.json"}, "display": {"href": "https://publications.scilifelab.se/publication/9ef62eced5e1409b90aec4ff52553390"}}, "title": "Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus.", "authors": [{"family": "Jerner\u00e9n", "given": "Fredrik", "initials": "F"}, {"family": "Garscha", "given": "Ulrike", "initials": "U"}, {"family": "Hoffmann", "given": "Inga", "initials": "I"}, {"family": "Hamberg", "given": "Mats", "initials": "M"}, {"family": "Oliw", "given": "Ernst H", "initials": "EH"}], "type": "journal article", "published": "2010-04-00", "journal": {"volume": "1801", "issn": "0006-3002", "issue": "4", "pages": "503-507", "title": "Biochim. Biophys. Acta", "issn-l": null}, "abstract": "Aspergilli express fusion proteins of an animal haem peroxidase domain with fatty acid dioxygenase (DOX) activity ( approximately 600 amino acids) and a functional or non-functional hydroperoxide isomerase/cytochrome P450 domain ( approximately 500 amino acids with EXXR and GPHXCLG motifs). 5,8-Linoleate diol synthases (LDS; ppoA) and 10R-DOX (ppoC) of Aspergillusnidulans and A. fumigatus belong to this group. Our objective was to determine the oxylipins formed from linoleic acid by A. clavatus and their mechanism of biosynthesis. A. clavatus oxidized linoleic acid to (8R)-hydroperoxylinoleic acid (8R-HPODE), (10R)-hydroperoxy-8(E),12(Z)-octadecadienoic acid (10R-HPODE), and to (5S,8R)-dihydroxy- and (8R,11S)-dihydroxylinoleic acids (DiHODE) as major products. This occurred by abstraction of the pro-S hydrogen at C-8 and antarafacial dioxygenation at C-8 or at C-10 with double bond migration. 8R-HPODE was then isomerized to 5S,8R-DiHODE and to 8R,11S-DiHODE by abstraction of the pro-S hydrogens at C-5 and C-11 of 8R-HPODE, respectively, followed by suprafacial oxygenation. The genome of A. clavatus codes for two enzymes, which can be aligned with >65% amino acid identity to 10R-DOX and 5,8-LDS, respectively. The 5,8-LDS homologue likely forms and isomerizes 8R-HPODE to 5S,8R-DiHODE. A third gene (ppoB) codes for a protein which carries a serine residue at the cysteine position of the P450 motif. This Cys to Ser replacement is known to abolish P450 2B4 catalysis and the hydroperoxide isomerase activity of 5,8-LDS, suggesting that ppoB of A. clavatus may not be involved in the biosynthesis of 8R,11S-DiHODE.", "doi": "10.1016/j.bbalip.2009.12.012", "pmid": "20045744", "labels": {"National Genomics Infrastructure": null, "NGI Uppsala (Uppsala Genome Center)": null}, "xrefs": [{"db": "pii", "key": "S1388-1981(09)00292-3"}], "notes": [], "created": "2017-05-04T15:01:49.189Z", "modified": "2020-01-21T13:56:04.101Z"}], "created": "2017-05-09T09:12:12.585Z", "modified": "2020-11-27T13:14:07.771Z"}