Exporters for Production of Amino Acids and Other Small Molecules

2016 ◽  
pp. 199-225 ◽  
Author(s):  
Lothar Eggeling
Keyword(s):  
Amino Acids ◽  
Small Molecules

scholarly journals P450BM3-Catalyzed Oxidations Employing Dual Functional Small Molecules

Catalysts ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 567 ◽  
Author(s):  
Willot ◽  
Tieves ◽  
Girhard ◽  
Urlacher ◽  
Hollmann ◽  
...  
Keyword(s):  
Amino Acids ◽  
Hydrogen Peroxide ◽  
Cytochrome P450 ◽  
Small Molecules ◽  
Bacillus Megaterium ◽  
Cytochrome P450 Monooxygenase ◽  
Oxidation Reactions ◽  
P450 Monooxygenase ◽  
Dual Functional ◽  
Catalytic Epoxidation

A set of dual functional small molecules (DFSMs) containing different amino acids has been synthesized and employed together with three different variants of the cytochrome P450 monooxygenase P450BM3 from Bacillus megaterium in H2O2-dependent oxidation reactions. These DFSMs enhance P450BM3 activity with hydrogen peroxide as an oxidant, converting these enzymes into formal peroxygenases. This system has been employed for the catalytic epoxidation of styrene and in the sulfoxidation of thioanisole. Various P450BM3 variants have been evaluated in terms of activity and selectivity of the peroxygenase reactions.

Small Molecules that Mimic Components of Bioactive Protein Surfaces

2004 ◽  
Vol 57 (9) ◽  
pp. 855 ◽  
Author(s):  
David P. Fairlie
Keyword(s):  
Amino Acids ◽  
Antiviral Activity ◽  
Small Molecules ◽  
G Protein ◽  
Selective Inhibition ◽  
Structural Components ◽  
Protein Surfaces ◽  
Biological Responses ◽  
Anti Inflammatory ◽  
G Protein Coupled

Small molecules designed to mimic specific structural components of a protein (peptide strands, sheets, turns, helices, or amino acids) can be expected to display agonist or antagonist biological responses by virtue of interacting with the same receptors that recognize the protein. Here we describe some minimalist approaches to structural mimetics of amino acids and of strand, turn, or helix segments of proteins. The designed molecules show potent and selective inhibition of protease, transferase, and phospholipase enzymes, or antagonism of G-protein coupled or transcriptional receptors, and have potent anti-tumour, anti-inflammatory, or antiviral activity.

scholarly journals Corticotropin-releasing factor receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
Frank M. Dautzenberg ◽  
Dimitri E. Grigoriadis ◽  
Richard L. Hauger ◽  
Victoria B. Risbrough ◽  
Thomas Steckler ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Small Molecules ◽  
Corticotropin Releasing Factor ◽  
Releasing Hormone ◽  
Endogenous Peptides ◽  
Amino Acid Peptide ◽  
Kd Values ◽  
Urocortin 1 ◽  
Urocortin 3

Corticotropin-releasing factor (CRF, nomenclature as agreed by the NC-IUPHAR subcommittee on Corticotropin-releasing Factor Receptors [30]) receptors are activated by the endogenous peptides corticotrophin-releasing hormone, a 41 amino-acid peptide, urocortin 1, 40 amino-acids, urocortin 2, 38 amino-acids and urocortin 3, 38 amino-acids. CRF1 and CRF2 receptors are activated non-selectively by CRH and UCN. CRF2 receptors are selectively activated by UCN2 and UCN3. Binding to CRF receptors can be conducted using radioligands [125I]Tyr0-CRF or [125I]Tyr0-sauvagine with Kd values of 0.1-0.4 nM. CRF1 and CRF2 receptors are non-selectively antagonized by α-helical CRF, D-Phe-CRF-(12-41) and astressin. CRF1 receptors are selectively antagonized by small molecules NBI27914, R121919, antalarmin, CP 154,526, CP 376,395. CRF2 receptors are selectively antagonized by antisauvagine and astressin 2B.

scholarly journals Chemical Methods for N‐ and O‐Sulfation of Small Molecules, Amino Acids and Peptides

ChemBioChem ◽  
2020 ◽  
Vol 21 (7) ◽  
pp. 938-942 ◽  
Author(s):  
Anna Mary Benedetti ◽  
Daniel M. Gill ◽  
Chi W. Tsang ◽  
Alan M. Jones
Keyword(s):  
Amino Acids ◽  
Small Molecules ◽  
Chemical Methods

A metabolomic study of Antarctic krill (Euphausia superba) raises a warning about Antarctic pollution

Crustaceana ◽  
2018 ◽  
Vol 91 (8) ◽  
pp. 961-999
Author(s):  
Fengying Zhang ◽  
Ming Zhao ◽  
Chunyan Ma ◽  
Lumin Wang ◽  
Chunlei Feng ◽  
...  
Keyword(s):  
Amino Acids ◽  
Small Molecules ◽  
Antarctic Krill ◽  
Euphausia Superba ◽  
Dioctyl Phthalate ◽  
Chemical Contamination ◽  
Metabolic Intermediates ◽  
Metabolomic Study ◽  
Antarctic Krill Euphausia Superba ◽  
Biotic Resources

Abstract Antarctic krill (Euphausia superba) is one of the most successful species on Earth and serves as the largest potential protein bank for both Antarctic animals and humans. Research on this species is of great value for exploitation of Antarctic biotic resources. In this study, the metabolomics of E. superba were investigated using the GC-MS method. A total of 293 compounds were initially identified; these compounds could be divided into several classes, including amino acids, sugars and polyols, metabolic intermediates, small molecules and other metabolites. However, a serious problem was that both 2-hydroxybiphenyl and dioctyl phthalate were also detected in these krill tissues. Moreover, some intermediates of pesticides and medicinal or chemical compound products were found in krill tissue as well. This is the first survey to investigate the occurrence of chemical contamination in metabolites of Antarctic krill. These findings suggest that international contracts or policies should be developed to protect the pristine ocean.

Safety, Tolerability, and Effect on Quality of Life of a Mixture of Amino Acids and Other Small Molecules in Cancer Patients

2014 ◽  
Vol 29 (3) ◽  
pp. 124-134
Author(s):  
Tamás Czömpöly ◽  
Zoltán Langmár ◽  
Mária Bors ◽  
Csilla Zsákai ◽  
Mária Géczy ◽  
...  
Keyword(s):  
Quality Of Life ◽  
Amino Acids ◽  
Small Molecules ◽  
Cancer Patients

scholarly journals Molybdenum Nitrogenase Catalyzes the Reduction and Coupling of CO to Form Hydrocarbons

2011 ◽  
Vol 286 (22) ◽  
pp. 19417-19421 ◽  
Author(s):  
Zhi-Yong Yang ◽  
Dennis R. Dean ◽  
Lance C. Seefeldt
Keyword(s):  
Amino Acids ◽  
Partial Pressure ◽  
Small Molecules ◽  
Wild Type ◽  
Fischer Tropsch ◽  
Hydrocarbon Production ◽  
Mofe Protein ◽  
Femo Cofactor ◽  
Electron Reduction ◽  
The Relationship

The molybdenum-dependent nitrogenase catalyzes the multi-electron reduction of protons and N2 to yield H2 and 2NH3. It also catalyzes the reduction of a number of non-physiological doubly and triply bonded small molecules (e.g. C2H2, N2O). Carbon monoxide (CO) is not reduced by the wild-type molybdenum nitrogenase but instead inhibits the reduction of all substrates catalyzed by nitrogenase except protons. Here, we report that when the nitrogenase MoFe protein α-Val70 residue is substituted by alanine or glycine, the resulting variant proteins will catalyze the reduction and coupling of CO to form methane (CH4), ethane (C2H6), ethylene (C2H4), propene (C3H6), and propane (C3H8). The rates and ratios of hydrocarbon production from CO can be adjusted by changing the flux of electrons through nitrogenase, by substitution of other amino acids located near the FeMo-cofactor, or by changing the partial pressure of CO. Increasing the partial pressure of CO shifted the product ratio in favor of the longer chain alkanes and alkenes. The implications of these findings in understanding the nitrogenase mechanism and the relationship to Fischer-Tropsch production of hydrocarbons from CO are discussed.

The determination of the conformations of small molecules in solution by means of paramagnetic shift and relaxation perturbations of n.m.r. spectra

1975 ◽  
Vol 345 (1640) ◽  
pp. 5-22 ◽  
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Small Molecules ◽  
Lanthanide Complexes ◽  
Hydrophobic Interactions ◽  
Lanthanide Ions ◽  
Conformational Studies ◽  
Nuclear Magnetic Resonance Spectra ◽  
General Method

A general method for the determination of the conformations of molecules in solution which uses paramagnetic lanthanide ions as perturbing probes of nuclear magnetic resonance spectra is described in outline. Several examples of conformational studies on the lanthanide complexes of amino acids and peptides are given. It is clear that there are two very different groups of lanthanide complexes characterized by those of Pr in and Tm Ill. The conformations of the Tm III complexes are used to initiate an examination of peptide chain folding and to re-examine the nature of hydrophobic interactions.

scholarly journals EFFECT OF ANTIBODY AND COMPLEMENT ON PERMEABILITY CONTROL IN ASCITES TUMOR CELLS AND ERYTHROCYTES

1959 ◽  
Vol 110 (5) ◽  
pp. 699-713 ◽  
Author(s):  
H. Green ◽  
P. Barrow ◽  
B. Goldberg
Keyword(s):  
Amino Acids ◽  
Cell Membrane ◽  
Small Molecules ◽  
Osmotic Pressure ◽  
Tumor Cells ◽  
Animal Cell ◽  
Colloid Osmotic Pressure ◽  
Ascites Tumor ◽  
Low Protein ◽  
Sufficient Concentration

Rabbit antibody + complement alters the permeability properties of mouse Krebs ascites tumor cells and erythrocytes. When antibody + C' acts on ascites tumor cells in a low protein medium, intracellular K+ is lost from the cells at a rate far greater than the normal leak rate. At the same time the cells lose amino acids and ribonucleotides and become fully permeable to the Na+ of the medium. When antibody + C' acts in a low protein medium, the cells swell extensively and lose most of their macromolecules to the medium (hemoglobin from erythrocytes, protein and RNA from the ascites tumor cells). If the antibody + C' acts in a medium containing protein in sufficient concentration to balance the colloid osmotic pressure of the cells, the swelling is prevented; no macromolecules are then lost from the cells, but the loss of K+ and entrance of Na+ are not altered, and the loss of amino acids and ribonucleotides is only slightly affected. It therefore appears that the action of antibody + C' is to produce functional "holes" in the animal cell membrane which permit the equilibration of cations and small molecules between cell and medium. This leads to an increase in the osmotic pressure of the cell and a rapid influx of water. The cell membrane and its "holes" are thereby stretched, permitting macromolecules to escape from the cell.

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