keyword
MENU ▼
Read by QxMD icon Read
search

Aldehyde decarbonylase

keyword
https://www.readbyqxmd.com/read/27439866/cytochrome-p450-associated-with-insecticide-resistance-catalyzes-cuticular-hydrocarbon-production-in-anopheles-gambiae
#1
Vasileia Balabanidou, Anastasia Kampouraki, Marina MacLean, Gary J Blomquist, Claus Tittiger, M Patricia Juárez, Sergio J Mijailovsky, George Chalepakis, Amalia Anthousi, Amy Lynd, Sanou Antoine, Janet Hemingway, Hilary Ranson, Gareth J Lycett, John Vontas
The role of cuticle changes in insecticide resistance in the major malaria vector Anopheles gambiae was assessed. The rate of internalization of (14)C deltamethrin was significantly slower in a resistant strain than in a susceptible strain. Topical application of an acetone insecticide formulation to circumvent lipid-based uptake barriers decreased the resistance ratio by ∼50%. Cuticle analysis by electron microscopy and characterization of lipid extracts indicated that resistant mosquitoes had a thicker epicuticular layer and a significant increase in cuticular hydrocarbon (CHC) content (∼29%)...
August 16, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/26556131/modular-and-selective-biosynthesis-of-gasoline-range-alkanes
#2
Micah J Sheppard, Aditya M Kunjapur, Kristala L J Prather
Typical renewable liquid fuel alternatives to gasoline are not entirely compatible with current infrastructure. We have engineered Escherichia coli to selectively produce alkanes found in gasoline (propane, butane, pentane, heptane, and nonane) from renewable substrates such as glucose or glycerol. Our modular pathway framework achieves carbon-chain extension by two different mechanisms. A fatty acid synthesis route is used to generate longer chains heptane and nonane, while a more energy efficient alternative, reverse-β-oxidation, is used for synthesis of propane, butane, and pentane...
January 2016: Metabolic Engineering
https://www.readbyqxmd.com/read/25773521/biosynthesis-of-odd-chain-fatty-alcohols-in-escherichia-coli
#3
Ying-Xiu Cao, Wen-Hai Xiao, Duo Liu, Jin-Lai Zhang, Ming-Zhu Ding, Ying-Jin Yuan
Engineered microbes offer the opportunity to design and implement artificial molecular pathways for renewable production of tailored chemical commodities. Targeted biosynthesis of odd-chain fatty alcohols is very challenging in microbe, due to the specificity of fatty acids synthase for two-carbon unit elongation. Here, we developed a novel strategy to directly tailor carbon number in fatty aldehydes formation step by incorporating α-dioxygenase (αDOX) from Oryza sativa (rice) into Escherichia coli αDOX oxidizes Cn fatty acids (even-chain) to form Cn-1 fatty aldehydes (odd-chain)...
May 2015: Metabolic Engineering
https://www.readbyqxmd.com/read/24319622/aldehyde-decarbonylases-enigmatic-enzymes-of-hydrocarbon-biosynthesis
#4
E Neil G Marsh, Matthew W Waugh
No abstract text is available yet for this article.
November 1, 2013: ACS Catalysis
https://www.readbyqxmd.com/read/23741473/rice-osgl1-6-is-involved-in-leaf-cuticular-wax-accumulation-and-drought-resistance
#5
Lingyan Zhou, Erdong Ni, Jiawei Yang, Hai Zhou, Hong Liang, Jing Li, Dagang Jiang, Zhonghua Wang, Zhenlan Liu, Chuxiong Zhuang
Cuticular wax is a class of organic compounds that comprises the outermost layer of plant surfaces. Plant cuticular wax, the last barrier of self-defense, plays an important role in plant growth and development. The OsGL1-6 gene, a member of the fatty aldehyde decarbonylase gene family, is highly homologous to Arabidopsis CER1, which is involved in cuticular wax biosynthesis. However, whether OsGL1-6 participates in cuticular wax biosynthesis remains unknown. In this study, an OsGL1-6 antisense-RNA vector driven by its own promoter was constructed and introduced into the rice variety Zhonghua11 by Agrobacterium-mediated transformation to obtain several independent transgenic plants with decreased OsGL1-6 expression...
2013: PloS One
https://www.readbyqxmd.com/read/23610415/synthesis-of-customized-petroleum-replica-fuel-molecules-by-targeted-modification-of-free-fatty-acid-pools-in-escherichia-coli
#6
Thomas P Howard, Sabine Middelhaufe, Karen Moore, Christoph Edner, Dagmara M Kolak, George N Taylor, David A Parker, Rob Lee, Nicholas Smirnoff, Stephen J Aves, John Love
Biofuels are the most immediate, practical solution for mitigating dependence on fossil hydrocarbons, but current biofuels (alcohols and biodiesels) require significant downstream processing and are not fully compatible with modern, mass-market internal combustion engines. Rather, the ideal biofuels are structurally and chemically identical to the fossil fuels they seek to replace (i.e., aliphatic n- and iso-alkanes and -alkenes of various chain lengths). Here we report on production of such petroleum-replica hydrocarbons in Escherichia coli...
May 7, 2013: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/23514600/probing-the-mechanism-of-cyanobacterial-aldehyde-decarbonylase-using-a-cyclopropyl-aldehyde
#7
Bishwajit Paul, Debasis Das, Benjamin Ellington, E Neil G Marsh
Cyanobacterial aldehyde decarbonylase (cAD) is a non-heme diiron oxygenase that catalyzes the conversion of fatty aldehydes to alkanes and formate. The mechanism of this chemically unusual reaction is poorly understood. We have investigated the mechanism of C1-C2 bond cleavage by cAD using a fatty aldehyde that incorporates a cyclopropyl group, which can act as a radical clock. When reacted with cAD, the cyclopropyl aldehyde produces 1-octadecene as the rearranged product, providing evidence for a radical mechanism for C-C bond scission...
April 10, 2013: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/23248280/carboxylic-acid-reductase-is-a-versatile-enzyme-for-the-conversion-of-fatty-acids-into-fuels-and-chemical-commodities
#8
M Kalim Akhtar, Nicholas J Turner, Patrik R Jones
Aliphatic hydrocarbons such as fatty alcohols and petroleum-derived alkanes have numerous applications in the chemical industry. In recent years, the renewable synthesis of aliphatic hydrocarbons has been made possible by engineering microbes to overaccumulate fatty acids. However, to generate end products with the desired physicochemical properties (e.g., fatty aldehydes, alkanes, and alcohols), further conversion of the fatty acid is necessary. A carboxylic acid reductase (CAR) from Mycobacterium marinum was found to convert a wide range of aliphatic fatty acids (C(6)-C(18)) into corresponding aldehydes...
January 2, 2013: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/22947199/evidence-for-only-oxygenative-cleavage-of-aldehydes-to-alk-a-e-nes-and-formate-by-cyanobacterial-aldehyde-decarbonylases
#9
Ning Li, Wei-Chen Chang, Douglas M Warui, Squire J Booker, Carsten Krebs, J Martin Bollinger
Cyanobacterial aldehyde decarbonylases (ADs) catalyze the conversion of C(n) fatty aldehydes to formate (HCO(2)(-)) and the corresponding C(n-1) alk(a/e)nes. Previous studies of the Nostoc punctiforme (Np) AD produced in Escherichia coli (Ec) showed that this apparently hydrolytic reaction is actually a cryptically redox oxygenation process, in which one O-atom is incorporated from O(2) into formate and a protein-based reducing system (NADPH, ferredoxin, and ferredoxin reductase; N/F/FR) provides all four electrons needed for the complete reduction of O(2)...
October 9, 2012: Biochemistry
https://www.readbyqxmd.com/read/22927409/an-insect-specific-p450-oxidative-decarbonylase-for-cuticular-hydrocarbon-biosynthesis
#10
Yue Qiu, Claus Tittiger, Claude Wicker-Thomas, Gaëlle Le Goff, Sharon Young, Eric Wajnberg, Thierry Fricaux, Nathalie Taquet, Gary J Blomquist, René Feyereisen
Insects use hydrocarbons as cuticular waterproofing agents and as contact pheromones. Although their biosynthesis from fatty acyl precursors is well established, the last step of hydrocarbon biosynthesis from long-chain fatty aldehydes has remained mysterious. We show here that insects use a P450 enzyme of the CYP4G family to oxidatively produce hydrocarbons from aldehydes. Oenocyte-directed RNAi knock-down of Drosophila CYP4G1 or NADPH-cytochrome P450 reductase results in flies deficient in cuticular hydrocarbons, highly susceptible to desiccation, and with reduced viability upon adult emergence...
September 11, 2012: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/22074177/oxygen-independent-alkane-formation-by-non-heme-iron-dependent-cyanobacterial-aldehyde-decarbonylase-investigation-of-kinetics-and-requirement-for-an-external-electron-donor
#11
Bekir E Eser, Debasis Das, Jaehong Han, Patrik R Jones, E Neil G Marsh
Cyanobacterial aldehyde decarbonylase (cAD) is, structurally, a member of the di-iron carboxylate family of oxygenases. We previously reported that cAD from Prochlorococcus marinus catalyzes the unusual hydrolysis of aldehydes to produce alkanes and formate in a reaction that requires an external reducing system but does not require oxygen [Das et al. (2011) Angew. Chem. 50, 7148-7152]. Here we demonstrate that cADs from divergent cyanobacterial classes, including the enzyme from N. puntiformes that was reported to be oxygen dependent, catalyze aldehyde decarbonylation at a much faster rate under anaerobic conditions and that the oxygen in formate derives from water...
December 13, 2011: Biochemistry
https://www.readbyqxmd.com/read/21671322/oxygen-independent-decarbonylation-of-aldehydes-by-cyanobacterial-aldehyde-decarbonylase-a-new-reaction-of-diiron-enzymes
#12
Debasis Das, Bekir E Eser, Jaehong Han, Aaron Sciore, E Neil G Marsh
No abstract text is available yet for this article.
July 25, 2011: Angewandte Chemie
https://www.readbyqxmd.com/read/21462983/conversion-of-fatty-aldehydes-to-alka-e-nes-and-formate-by-a-cyanobacterial-aldehyde-decarbonylase-cryptic-redox-by-an-unusual-dimetal-oxygenase
#13
Ning Li, Hanne Nørgaard, Douglas M Warui, Squire J Booker, Carsten Krebs, J Martin Bollinger
Cyanobacterial aldehyde decarbonylase (AD) catalyzes conversion of fatty aldehydes (R-CHO) to alka(e)nes (R-H) and formate. Curiously, although this reaction appears to be redox-neutral and formally hydrolytic, AD has a ferritin-like protein architecture and a carboxylate-bridged dimetal cofactor that are both structurally similar to those found in di-iron oxidases and oxygenases. In addition, the in vitro activity of the AD from Nostoc punctiforme (Np) was shown to require a reducing system similar to the systems employed by these O(2)-utilizing di-iron enzymes...
April 27, 2011: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/21341652/detection-of-formate-rather-than-carbon-monoxide-as-the-stoichiometric-coproduct-in-conversion-of-fatty-aldehydes-to-alkanes-by-a-cyanobacterial-aldehyde-decarbonylase
#14
Douglas M Warui, Ning Li, Hanne Nørgaard, Carsten Krebs, J Martin Bollinger, Squire J Booker
The second of two reactions in a recently discovered pathway through which saturated fatty acids are converted to alkanes (and unsaturated fatty acids to alkenes) in cyanobacteria entails scission of the C1-C2 bond of a fatty aldehyde intermediate by the enzyme aldehyde decarbonylase (AD), a ferritin-like protein with a dinuclear metal cofactor of unknown composition. We tested for and failed to detect carbon monoxide (CO), the proposed C1-derived coproduct of alkane synthesis, following the in vitro conversion of octadecanal (R-CHO, where R = n-C(17)H(35)) to heptadecane (R-H) by the Nostoc punctiforme AD isolated following its overproduction in Escherichia coli...
March 16, 2011: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/20671186/microbial-biosynthesis-of-alkanes
#15
Andreas Schirmer, Mathew A Rude, Xuezhi Li, Emanuela Popova, Stephen B del Cardayre
Alkanes, the major constituents of gasoline, diesel, and jet fuel, are naturally produced by diverse species; however, the genetics and biochemistry behind this biology have remained elusive. Here we describe the discovery of an alkane biosynthesis pathway from cyanobacteria. The pathway consists of an acyl-acyl carrier protein reductase and an aldehyde decarbonylase, which together convert intermediates of fatty acid metabolism to alkanes and alkenes. The aldehyde decarbonylase is related to the broadly functional nonheme diiron enzymes...
July 30, 2010: Science
https://www.readbyqxmd.com/read/20202935/tight-coupling-of-partial-reactions-in-the-acetyl-coa-decarbonylase-synthase-acds-multienzyme-complex-from-methanosarcina-thermophila-acetyl-c-c-bond-fragmentation-at-the-a-cluster-promoted-by-protein-conformational-changes
#16
Simonida Gencic, Evert C Duin, David A Grahame
Direct synthesis and cleavage of acetyl-CoA are carried out by the bifunctional CO dehydrogenase/acetyl-CoA synthase enzyme in anaerobic bacteria and by the acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex in Archaea. In both systems, a nickel- and Fe/S-containing active site metal center, the A cluster, catalyzes acetyl C-C bond formation/breakdown. Carbonyl group exchange of [1-(14)C]acetyl-CoA with unlabeled CO, a hallmark of CODH/ACS, is weakly active in ACDS, and exchange with CO(2) was up to 350 times faster, indicating tight coupling of CO release at the A cluster to CO oxidation to CO(2) at the C cluster in CO dehydrogenase...
May 14, 2010: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/18621675/structure-of-the-alpha2epsilon2-ni-dependent-co-dehydrogenase-component-of-the-methanosarcina-barkeri-acetyl-coa-decarbonylase-synthase-complex
#17
Weimin Gong, Bing Hao, Zhiyi Wei, Donald J Ferguson, Thomas Tallant, Joseph A Krzycki, Michael K Chan
Ni-dependent carbon monoxide dehydrogenases (Ni-CODHs) are a diverse family of enzymes that catalyze reversible CO:CO(2) oxidoreductase activity in acetogens, methanogens, and some CO-using bacteria. Crystallography of Ni-CODHs from CO-using bacteria and acetogens has revealed the overall fold of the Ni-CODH core and has suggested structures for the C cluster that mediates CO:CO(2) interconversion. Despite these advances, the mechanism of CO oxidation has remained elusive. Herein, we report the structure of a distinct class of Ni-CODH from methanogenic archaea: the alpha(2)epsilon(2) component from the alpha(8)beta(8)gamma(8)delta(8)epsilon(8) CODH/acetyl-CoA decarbonylase/synthase complex, an enzyme responsible for the majority of biogenic methane production on Earth...
July 15, 2008: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/18442256/two-separate-one-electron-steps-in-the-reductive-activation-of-the-a-cluster-in-subunit-beta-of-the-acds-complex-in-methanosarcina-thermophila
#18
Simonida Gencic, David A Grahame
Acetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex found in methanogens and certain other Archaea that carries out the overall synthesis and cleavage of the acetyl C-C and C-S bonds of acetyl-CoA. The reaction is involved both in the autotrophic fixation of carbon and in the process of methanogenesis from acetate, and takes place at a unique active site metal center known as the A cluster, located on the beta subunit of the ACDS complex and composed of a binuclear Ni-Ni site bridged by a cysteine thiolate to an Fe4S4 center...
May 20, 2008: Biochemistry
https://www.readbyqxmd.com/read/16044263/a-single-operon-encoded-form-of-the-acetyl-coa-decarbonylase-synthase-multienzyme-complex-responsible-for-synthesis-and-cleavage-of-acetyl-coa-in-methanosarcina-thermophila
#19
David A Grahame, Simonida Gencic, Edward DeMoll
Methanogens growing on C-1 substrates synthesize 2-carbon acetyl groups in the form of acetyl-CoA for carbon assimilation using the multienzyme complex acetyl-CoA decarbonylase/synthase (ACDS) which contains five different subunits encoded within an operon. In species growing on acetate ACDS also functions to cleave the acetate C-C bond for energy production by methanogenesis. A number of species of Methanosarcina that are capable of growth on either C-1 compounds or acetate contain two separate ACDS operons, and questions have been raised about whether or not these operons play separate roles in acetate synthesis and cleavage...
October 2005: Archives of Microbiology
https://www.readbyqxmd.com/read/14709073/chemically-distinct-ni-sites-in-the-a-cluster-in-subunit-beta-of-the-acetyl-coa-decarbonylase-synthase-complex-from-methanosarcina-thermophila-ni-l-edge-absorption-and-x-ray-magnetic-circular-dichroism-analyses
#20
Tobias Funk, Weiwei Gu, Stephan Friedrich, Hongxin Wang, Simonida Gencic, David A Grahame, Stephen P Cramer
The 5-subunit-containing acetyl-CoA decarbonylase/synthase (ACDS) complex plays an important role in methanogenic Archaea that convert acetate to methane, by catalyzing the central reaction of acetate C-C bond cleavage in which acetyl-CoA serves as the acetyl donor substrate reacting at the ACDS beta subunit active site. The properties of Ni in the active site A-cluster in the ACDS beta subunit from Methanosarcina thermophila were investigated. A recombinant, C-terminally truncated form of the beta subunit was employed, which mimics the native subunit previously isolated from the ACDS complex, and contains an A-cluster composed of an [Fe(4)S(4)] center bridged to a binuclear Ni-Ni site...
January 14, 2004: Journal of the American Chemical Society
keyword
keyword
6860
1
2
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"