Determination of coenzyme A and acetyl CoA in tissue extracts
Coenzyme A and acetyl CoA in tissue extracts determined for concentrations by recycling CoA through coupled enzyme system
Allred, J. B.↗
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Results for “CoAs”
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Recent NASA Dryden COA Experience
This viewgraph presentation concerns the experience that Dryden has had with Certificate of Authorization (COA) in reference to unmanned aerial systems (UAS). It reviews recent Certificate of Authorization UAS's i.e., 2005 Altair NOAA Mission, 2006 Altair Western States Fire Mission, and 2007 Ikhana. The priorities for the safety process is reviewed, as are typical UAS hazards. Slides also review the common COA provisions, best practices and lessons learned, the 2005 NOAA/NASA Science Demonstration Flights and the use of the UAS systems during fire emergencies.
Cobleigh, Brent↗
Feruloyl-CoA:monolignol transferases
The invention relates to feruloyl-CoA:monolignol transferase enzymes and nucleic acids encoding the feruloyl-CoA:monolignol transferase enzymes. The enzymes and/or the nucleic acids enable incorporation of monolignol ferulates into the lignin of plants. The monolignol ferulates include, for example, p-coumaryl ferulate, coniferyl ferulate, and/or sinapyl ferulate.
Ralph, John↗
Feruloyl-CoA:monolignol transferases
The invention relates to feruloyl-CoA:monolignol transferase enzymes and nucleic acids encoding the feruloyl-CoA:monolignol transferase enzymes. The enzymes and/or the nucleic acids enable incorporation of monolignol ferulates into the lignin of plants. The monolignol ferulates include, for example, p-coumaryl ferulate, coniferyl ferulate, and/or sinapyl ferulate.
Ralph, John↗
Materials Data on CoAs by Materials Project
CoAs is Molybdenum Carbide MAX Phase-like structured and crystallizes in the hexagonal P6_3/mmc space group. The structure is three-dimensional. Co3+ is bonded to six equivalent As3- atoms to form a mixture of face, edge, and corner-sharing CoAs6 octahedra. The corner-sharing octahedral tilt angles are 50°. All Co–As bond lengths are 2.41 Å. As3- is bonded in a 6-coordinate geometry to six equivalent Co3+ atoms.
36 MATERIALS SCIENCE↗
Materials Data on Ce(CoAs)2 by Materials Project
Ce(CoAs)2 crystallizes in the tetragonal I4/mmm space group. The structure is three-dimensional. Ce3+ is bonded in a distorted body-centered cubic geometry to eight equivalent As3- atoms. All Ce–As bond lengths are 3.16 Å. Co+1.50+ is bonded to four equivalent As3- atoms to form a mixture of edge and corner-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.34 Å. As3- is bonded in a 9-coordinate geometry to four equivalent Ce3+, four equivalent Co+1.50+, and one As3- atom. The As–As bond length is 2.72 Å.
36 MATERIALS SCIENCE↗
Materials Data on Ca(CoAs)2 by Materials Project
Ca(CoAs)2 crystallizes in the tetragonal I4/mmm space group. The structure is three-dimensional. Ca2+ is bonded in a body-centered cubic geometry to eight equivalent As3- atoms. All Ca–As bond lengths are 3.16 Å. Co2+ is bonded to four equivalent As3- atoms to form a mixture of edge and corner-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.33 Å. As3- is bonded in a 9-coordinate geometry to four equivalent Ca2+, four equivalent Co2+, and one As3- atom. The As–As bond length is 2.80 Å.
36 MATERIALS SCIENCE↗
Materials Data on K(CoAs)2 by Materials Project
K(CoAs)2 is alpha bismuth trifluoride-derived structured and crystallizes in the tetragonal I4/mmm space group. The structure is three-dimensional. K1+ is bonded in a body-centered cubic geometry to eight equivalent As3- atoms. All K–As bond lengths are 3.41 Å. Co+2.50+ is bonded to four equivalent As3- atoms to form a mixture of edge and corner-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.31 Å. As3- is bonded in a 8-coordinate geometry to four equivalent K1+ and four equivalent Co+2.50+ atoms.
36 MATERIALS SCIENCE↗
Materials Data on Sr(CoAs)2 by Materials Project
Sr(CoAs)2 is alpha bismuth trifluoride-derived structured and crystallizes in the tetragonal I4/mmm space group. The structure is three-dimensional. Sr2+ is bonded in a body-centered cubic geometry to eight equivalent As3- atoms. All Sr–As bond lengths are 3.29 Å. Co2+ is bonded to four equivalent As3- atoms to form a mixture of edge and corner-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.34 Å. As3- is bonded in a 8-coordinate geometry to four equivalent Sr2+ and four equivalent Co2+ atoms.
36 MATERIALS SCIENCE↗
Materials Data on Nd(CoAs)2 by Materials Project
Nd(CoAs)2 crystallizes in the tetragonal I4/mmm space group. The structure is three-dimensional. Nd3+ is bonded in a body-centered cubic geometry to eight equivalent As3- atoms. All Nd–As bond lengths are 3.18 Å. Co+1.50+ is bonded to four equivalent As3- atoms to form a mixture of corner and edge-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.35 Å. As3- is bonded in a 9-coordinate geometry to four equivalent Nd3+ and four equivalent Co+1.50+ atoms.
36 MATERIALS SCIENCE↗
Materials Data on CoAs by Materials Project
CoAs is Modderite structured and crystallizes in the orthorhombic Pnma space group. The structure is three-dimensional. Co3+ is bonded to six equivalent As3- atoms to form a mixture of distorted face, edge, and corner-sharing CoAs6 octahedra. The corner-sharing octahedra tilt angles range from 47–59°. There are a spread of Co–As bond distances ranging from 2.31–2.51 Å. As3- is bonded in a 6-coordinate geometry to six equivalent Co3+ atoms.
36 MATERIALS SCIENCE↗
Materials Data on Th(CoAs)2 by Materials Project
Th(CoAs)2 crystallizes in the tetragonal P4/nmm space group. The structure is three-dimensional. Th4+ is bonded in a 8-coordinate geometry to eight As3- atoms. There are four shorter (3.14 Å) and four longer (3.16 Å) Th–As bond lengths. There are two inequivalent Co1+ sites. In the first Co1+ site, Co1+ is bonded to four equivalent As3- atoms to form a mixture of edge and corner-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.43 Å. In the second Co1+ site, Co1+ is bonded in a 5-coordinate geometry to five As3- atoms. There are four shorter (2.35 Å) and one longer (2.37 Å) Co–As bond lengths. There are two inequivalent As3- sites. In the first As3- site, As3- is bonded in a 4-coordinate geometry to four equivalent Th4+ and four equivalent Co1+ atoms. In the second As3- site, As3- is bonded in a 9-coordinate geometry to four equivalent Th4+ and five Co1+ atoms.
36 MATERIALS SCIENCE↗
Materials Data on Cs(CoAs)2 by Materials Project
Cs(CoAs)2 crystallizes in the tetragonal I4/mmm space group. The structure is three-dimensional. Cs1+ is bonded in a distorted body-centered cubic geometry to eight equivalent As3- atoms. All Cs–As bond lengths are 3.66 Å. Co+2.50+ is bonded to four equivalent As3- atoms to form a mixture of edge and corner-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.31 Å. As3- is bonded in a 8-coordinate geometry to four equivalent Cs1+ and four equivalent Co+2.50+ atoms.
36 MATERIALS SCIENCE↗
Materials Data on Rb(CoAs)2 by Materials Project
Rb(CoAs)2 is alpha bismuth trifluoride-derived structured and crystallizes in the tetragonal I4/mmm space group. The structure is three-dimensional. Rb1+ is bonded in a body-centered cubic geometry to eight equivalent As3- atoms. All Rb–As bond lengths are 3.53 Å. Co+2.50+ is bonded to four equivalent As3- atoms to form a mixture of edge and corner-sharing CoAs4 tetrahedra. All Co–As bond lengths are 2.32 Å. As3- is bonded in a 8-coordinate geometry to four equivalent Rb1+ and four equivalent Co+2.50+ atoms.
36 MATERIALS SCIENCE↗
CRISPR/Cas9 editing of p-COUMAROYL-CoA:MONOLIGNOL TRANSFERASE 1 in maize alters phenolic metabolism, lignin structure, and lignin-first biomass processing
Valorization of lignocellulosic biomass for sustainable production of high-value chemicals is challenged by the complexity of lignin, a phenolic biopolymer. Beyond the classical lignin monomers derived from p-coumaryl, coniferyl, and sinapyl alcohol, grass lignins incorporate substantial amounts of monolignol p-coumarates that are produced by p-COUMAROYL-CoA:MONOLIGNOL TRANSFERASE (PMT). Here, the CRISPR/Cas9-mediated mutation of ZmPMT1 in maize enabled the design of biomass depleted in p-coumaroylated lignin and enriched in guaiacyl lignin. Lignin-first biorefining of stem biomass from zmpmt1 mutants by reductive catalytic fractionation (RCF) generated a lignin oil depleted in carboxylates and enriched in guaiacyl-derived alcohols, which are desirable substrates for bio-based polyurethane synthesis. Furthermore, the reported lignin engineering in maize is a promising strategy for designing a dual-purpose crop, providing both food and feed, along with a renewable feedstock for the production of plant-based chemicals.
59 BASIC BIOLOGICAL SCIENCES↗
Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for B 12 delivery and repair
G-proteins function as molecular switches to power cofactor translocation and confer fidelity in metal trafficking. The G-protein, MMAA, together with MMAB, an adenosyltransferase, orchestrate cofactor delivery and repair of B 12 -dependent human methylmalonyl-CoA mutase (MMUT). The mechanism by which the complex assembles and moves a >1300 Da cargo, or fails in disease, are poorly understood. Herein, we report the crystal structure of the human MMUT-MMAA nano-assembly, which reveals a dramatic 180° rotation of the B 12 domain, exposing it to solvent. The complex, stabilized by MMAA wedging between two MMUT domains, leads to ordering of the switch I and III loops, revealing the molecular basis of mutase-dependent GTPase activation. The structure explains the biochemical penalties incurred by methylmalonic aciduria-causing mutations that reside at the MMAA-MMUT interfaces we identify here.
59 BASIC BIOLOGICAL SCIENCES↗
Structural characterization of a GNAT family acetyltransferase from Elizabethkingia anophelis bound to acetyl-CoA reveals a new dimeric interface
General control non-repressible 5 (GCN5)-related N-acetyltransferases (GNATs) catalyse the acetylation of a diverse range of substrates, thereby orchestrating a variety of biological processes within prokaryotes and eukaryotes. GNAT enzymes can catalyze the transfer of an acetyl group from acetyl coenzyme A to substrates such as aminoglycoside antibiotics, amino acids, polyamines, peptides, vitamins, catecholamines, and large macromolecules including proteins. Although GNATs generally exhibit low to moderate sequence identity, they share a conserved catalytic fold and conserved structural motifs. In this current study we characterize the high-resolution X-ray crystallographic structure of a GNAT enzyme bound with acetyl-CoA from Elizabethkingia anophelis , an important multi-drug resistant bacterium. The tertiary structure is comprised of six α-helices and nine β-strands, and is similar with other GNATs. We identify a new and uncharacterized GNAT dimer interface, which is conserved in at least two other unpublished GNAT structures. This suggests that GNAT enzymes can form at least five different types of dimers, in addition to a range of other oligomers including trimer, tetramer, hexamer, and dodecamer assemblies. The high-resolution structure presented in this study is suitable for future in-silico docking and structure–activity relationship studies.
59 BASIC BIOLOGICAL SCIENCES↗
Expanding the use of ethanol as a feedstock for cell-free synthetic biochemistry by implementing acetyl-CoA and ATP generating pathways
Abstract Ethanol is a widely available carbon compound that can be increasingly produced with a net negative carbon balance. Carbon-negative ethanol might therefore provide a feedstock for building a wider range of sustainable chemicals. Here we show how ethanol can be converted with a cell free system into acetyl-CoA, a central precursor for myriad biochemicals, and how we can use the energy stored in ethanol to generate ATP, another key molecule important for powering biochemical pathways. The ATP generator produces acetone as a value-added side product. Our ATP generator reached titers of 27 ± 6 mM ATP and 59 ± 15 mM acetone with maximum ATP synthesis rate of 2.8 ± 0.6 mM/h and acetone of 7.8 ± 0.8 mM/h. We illustrated how the ATP generating module can power cell-free biochemical pathways by converting mevalonate into isoprenol at a titer of 12.5 ± 0.8 mM and a maximum productivity of 1.0 ± 0.05 mM/h. These proof-of-principle demonstrations may ultimately find their way to the manufacture of diverse chemicals from ethanol and other simple carbon compounds.
59 BASIC BIOLOGICAL SCIENCES↗