The principles of classification and a classification of mammals. Bulletin of the AMNH ; v. 85

Lipids and their constituent fatty acids are, along with proteins, the major organic constituents of fish, and they play major roles as sources of metabolic energy for growth including reproduction and movement, including migration. Furthermore, the fatty acids of fish lipids are rich in ω3 long chain, highly unsaturated fatty acids (n-3 HUFA) that have particularly important roles in animal nutrition, including fish and human nutrition, reflecting their roles in critical physiological processes. Indeed, fish are the most important food source of these vital nutrients for man. Thus, the longstanding interest in fish lipids stems from their abundance and their uniqueness. This review attempts to summarize our present state of knowledge of various aspects of the basic biochemistry, metabolism, and functions of fatty acids, and the lipids they constitute part of, in fish, seeking where possible to relate that understanding as much to fish in their natural environment as to farmed fish. In doing so, it highli...

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Metabolism and Functions of Lipids and Fatty Acids in Teleost Fish

Yarrowia lipolytica as a model for bio-oil production

The S100 proteins comprise at least 25 members, forming the largest group of EF-hand signalling proteins in humans. Although the proteins are expressed in many tissues, each S100 protein has generally been shown to have a preference for expression in one particular tissue or cell type. Three-dimensional structures of several S100 family members have shown that the proteins assume a dimeric structure consisting of two EF-hand motifs per monomer. Calcium binding to these S100 proteins, with the exception of S100A10, results in an approx. 40° alteration in the position of helix III, exposing a broad hydrophobic surface that enables the S100 proteins to interact with a variety of target proteins. More than 90 potential target proteins have been documented for the S100 proteins, including the cytoskeletal proteins tubulin, glial fibrillary acidic protein and F-actin, which have been identified mostly from in vitro experiments. In the last 5 years, efforts have concentrated on quantifying the protein interactions of the S100 proteins, identifying in vivo protein partners and understanding the molecular specificity for target protein interactions. Furthermore, the S100 proteins are the only EF-hand proteins that are known to form both homo- and hetero-dimers, and efforts are underway to determine the stabilities of these complexes and structural rationales for their formation and potential differences in their biological roles. This review highlights both the calcium-dependent and -independent interactions of the S100 proteins, with a focus on the structures of the complexes, differences and similarities in the strengths of the interactions, and preferences for homo- compared with hetero-dimeric S100 protein assembly.

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Calcium-dependent and -independent interactions of the S100 protein family

The ascomycetous yeast Yarrowia lipolytica (formerly Candida, Endomycopsis, or Saccharomyces lipolytica) is one of the more intensively studied 'non-conventional' yeast species. This yeast is quite different from the well-studied yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe with respect to its phylogenetic evolution, physiology, genetics, and molecular biology. However, Y. lipolytica is not only of interest for fundamental research, but also for biotechnological applications. It secretes several metabolites in large amounts (i.e. organic acids, extracellular proteins) and the tools are available for overproduction and secretion of foreign proteins. This review presents a comprehensive overview on the available data on physiology, cell biology, molecular biology and genetics of Y. lipolytica.

Physiology and genetics of the dimorphic fungus Yarrowia lipolytica

1
The study of the structure of the peptides arising from native, oxidized or reduced and maleinized bovine growth hormone on incubation with trypsin, chymotrypsin and pepsin is reported.

2
The data obtained permitted the assembly of a unique sequence of amino acids for the poly-peptide chain of the protein.

3
Various corrections and one addition to the sequence previously communicated are made.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1973.tb02971.x

Primary structure of bovine growth hormone.

The intracellular lipid-binding proteins are a group of homologous proteins which bind and facilitate the transport of fatty acids, bile acids and retinoids. The evolutionary relationship of 51 family members from vertebrates and invertebrates was analyzed. The inferred phylogeny implies the occurrence of at least 14 gene duplications and contains five regions where the branching order is statistically non-significant--this uncertainty explaining most inconsistencies between previous phylogenetic analyses. The phylogeny also suggests that the intestinal fatty acid-binding protein and the liver fatty acid-binding protein/ileal lipid-binding protein subfamilies diverged from the other subfamilies before the vertebrate-invertebrate split. Finally, results presented herein indicate that the putative fatty acid-binding domain of NMDA receptor 1 is unlikely to be a member of this family.

Molecular evolution of the multigene family of intracellular lipid-binding proteins.

Up until now, the primary structure of fatty-acid-binding proteins (FABPs) from the livers of four mammalian (rat, human, cow and pig) and three nonmammalian (chicken, catfish and iguana) species has been determined Based on amino acid sequence comparisons, it has been suggested that mammalian and nonmammalian liver FABPs may be paralogous proteins that originated by gene duplication, rather than as a consequence of mutations of the same gene In this paper we report the isolation and amino acid sequence determination of two FABPs from axolotl (Ambistoma mexicanum) liver One of them is similar to mammalian liver FABPs (L-FABPs) and the other to chicken, catfish and iguana liver FABPs (Lb-FABPs) The finding of both L-FABP and Lb-FABP in a single species, as reported here, indicates that they are paralogous proteins The time of divergence of these two liver FABP types is estimated to be of ≈ 694 million years ago The ligand-binding properties of axolotl liver FABPs were studied by means of parinaric-acid-binding and parinaric-acid-displacement assays L-FABP binds two fatty acids per molecule but Lb-FABP displays a fatty-acid-conformation-dependent binding stoichiometry; L-FABP shows a higher affinity for fatty acids, especially oleic acid, while Lb-FABP has a higher affinity for other hydrophobic ligands, especially retinoic acid In addition, the tissue-expression pattern is different, L-FABP is present in liver and intestinal mucosa while the expression of Lb-FABP is restricted to liver Data indicate distinct functional properties of both liver FABP types

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.1999.00015.x

Isolation, amino acid sequence determination and binding properties of two fatty‐acid‐binding proteins from axolotl (Ambistoma mexicanum) liver

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2871%2980132-1

The amino acid sequence of bovine growth hormone.

Two paralogous groups of fatty acid-binding proteins (FABPs) have been described in vertebrate liver: liver FABP (L-FABP) type, extensively characterized in mammals, and liver basic FABP (Lb-FABP) found in fish, amphibians, reptiles, and birds. We describe here the toad Lb-FABP complete amino acid sequence, its X-ray structure to 2.5 A resolution, ligand-binding properties, and mechanism of fatty acid transfer to phospholipid membranes. Alignment of the amino acid sequence of toad Lb-FABP with known L-FABPs and Lb-FABPs shows that it is more closely related to the other Lb-FABPs. Toad Lb-FABP conserves the 12 characteristic residues present in all Lb-FABPs and absent in L-FABPs and presents the canonical fold characteristic of all the members of this protein family. Eight out of the 12 conserved residues point to the lipid-binding cavity of the molecule. In contrast, most of the 25 L-FABP conserved residues are in clusters on the surface of the molecule. The helix-turn-helix motif shows both a negative and positive electrostatic potential surface as in rat L-FABP, and in contrast with the other FABP types. The mechanism of anthroyloxy-labeled fatty acids transfer from Lb-FABP to phospholipid membranes occurs by a diffusion-mediated process, as previously shown for L-FABP, but the rate of transfer is 1 order of magnitude faster. Toad Lb-FABP can bind two cis-parinaric acid molecules but only one trans-parinaric acid molecule while L-FABP binds two molecules of both parinaric acid isomers. Although toad Lb-FABP shares with L-FABP a broad ligand-binding specificity, the relative affinity is different.

José A. Santomé

Papers

Primary structure of bovine growth hormone.

Molecular evolution of the multigene family of intracellular lipid-binding proteins.

Isolation, amino acid sequence determination and binding properties of two fatty‐acid‐binding proteins from axolotl (Ambistoma mexicanum) liver

The amino acid sequence of bovine growth hormone.

Structural and biochemical characterization of toad liver fatty acid-binding protein.