Acad. E2), which uses lipoamide as a cofactor, and the dihydrolipoamide dehydrogenase (or E3). Griffin MC, Griffin WG, Perham RN. This is the dihydrolipoamide dehydrogenase … A47, 110–119 (1991). Both coenzymes function only when covalently attached to key metabolic enzymes. Navaza, J. AMoRe: an automated package for molecular replacement. a. The branched-chain α-ketoacid dehydrogenase complex (BCKDC or BCKDH complex) is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. Nat Struct Mol Biol 2, 63–68 (1995). Carson, M. Ribbon 2.0 . & Perham, R.N. 7, 40–46 (1974). The three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex J. molec. Cohen‐Addad C, Pares S, Sieker L, Neuberger M and Douce R (1995) The lipoamide arm in the glycine decarboxylase complex is not freely swinging. The lipoamide acts as a swinging arm in the complex. Both E1 and E3 bind to the E2 core to allow substrate channelling, which is facilitated by the so-called ‘swinging arm’, referring to the lipoamide co-factor that is covalently attached to the lipoyl-domains of PDC E2 . Brocklehurst, S.M. Molec. • Step 2: The hydroxyethyl group is transferred to E2 where it reacts with lipoamide (Swinging arm). The situation with the E 1 subunit is more complicated. Pares, S., Cohen-Addad, C., Sieker, L., Neuburger, M. & Douce, R. X-ray structure determination at 2. Glycine decarboxylase consists of four protein components. Aspects of the molecular biology of lipoamide dehydrogenase. U.S.A. 91, 4850–4853 (1994). 22, 184–188 (1994). (2019), Journal of Structural and Functional Genomics 229, 1037–1048 (1993). Planta. The lipoamide arm in the glycine decarboxylase complex is not freely swinging. How do specific substrates effect the activity of pyruvate dehydrogenase? 2, 877–887 (1992). The resulting 1,3-dipole reductively acetylates lipoamide-E2. The inner core: •60 E 2 enzymes •in the shape of a pentagonal Dodecahedron •with one E 2 CAS Jones, T.A., Zou, J.Y., Couran, S.W. Biochemistry 2000, 39 (29) , 8448-8459 ... Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 2, 63 –68. a. lipoamide b. FAD c. Coenzyme A d. A and C All reactions of citric acid cycle occur in the mitochondrial matrix. The hydroxyethyl attacks the reactive center of the lipoamide. The situation with the E 1 subunit is more complicated. Biol. Douce, R., Bourguignon, J., Macherel, D. & Neuburger, M. The glycine decarboxylase system in higher plant mitochondria: Structure, function and biogenesis. This reaction is set up so it is easy to cleave acetyl via CoA. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. (C) The reduced form of the lipoyl cofactor, ... and as a swinging arm that chan-nels the bound substrate between the active sites of different subunits (reviewed in references 171, 185, and 187). Lipoic acid attached to a specific lysine side chain is assumed to act as a ‘swinging arm’ conveying the reactive dithiolane ring from one … A similar reaction mechanism is also employed by the 2- Get time limited or full article access on ReadCube. E3, lipoamide dehydrogenase, carries an FAD cofactor which reoxidizes the lipoic acid of E2. Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily. Crossref CAS PubMed Web of Science® Google Scholar; Cronan JE (1989) The E.coli bio operon: transcriptional repression by an essential protein modification enzyme. We find that Lpd and SucB support Mtb's antioxidant defense. The swinging arm mechanism of lipoamide • The various subunits of the complex are arranged in a way –to ensure that •the product of one reaction •does not diffuse into the medium but is •immediately acted on by the next component • This arrangement is called –the –swinging arm mechanism of lipoamide Multienzyme complexes. Its structural and mechanistic heart is provided by the lipoic acid-containing H-protein which undergoes a cycle of reductive methylamination, methylamine transfer and electron transfer. Biochem J. Biochem. Lipoic acid attached to a specific lysine side chain is assumed to act as a ‘swinging arm’ conveying the reactive dithiolane ring from one catalytic centre to another. PDH kinase binds to the E2 subunits, specifically the lipoamide swinging arm [The Structure of the Pyruvate Dehydrogenase Complex]. “swinging arm”) on E2, and then the reduced dihydrolipoamide is reoxidized by the E3 (dihydrolipoamide dehydrogenase) component. & Perham, R.N. Glycine decarboxylase consists of four protein components. Electron-spin-resonance studies of the lipoamide 'swinging arm' of the pyruvate dehydrogenase multienzyme complex of Escherichia coli [proceedings]. Acetyl CoA enters the citric acid cylce via what . Biochem Soc Trans. Sieker, L., Cohen-Addad, C., Neuburger, M. & Douce, R. Crystallographic data for H-protein from the glycine decarboxylase complex. There is only one E 3 gene and it supplies the dihydrolipoamide dehydrogenase activity for BCOADH, PDC, and OADH. Clipboard, Search History, and several other advanced features are temporarily unavailable. COVID-19 is an emerging, rapidly evolving situation. Reed, L.J. Bethesda, MD 20894, Copyright TPP is released and E1 is regenerated. The lipoyl moieties are attached via an amide linkage to a lysine residue within each lipoyl domain in E2 that forms a lipoamide-swinging arm, though recent studies have shown the swinging arm to have a preferred orientation and thus restricted movement (Jones et al., 2000) . E2 to CoASH is then facilitated via the swinging arm of the lipoic-acid-lipoyl domain, leaving lipoamide moieties in a re- duced state, ready for reoxidation and hence, regeneration by E3 (Pate1 and Roche, 1990; Perham, 1991). The pyruvate dehydrogenase multienzyme complex. J. molec. Proc. The X-ray crystal structures of two forms of the H-protein have been determined. This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids.BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and … The Lipoamide Arm in the Glycine Decarboxylase is not Freely Swinging Cohen-Addad, C., Pares, S., Sieker, L., Neuburger, M., Douce, R. (1995) Nat Struct Biol 2: 63; Refined Structures at 2 and 2.2 A Resolution of Two Forms of the H-Protein, a Lipoamide-Containing Protein of … Biochem J. Pyruvate dehydrogenase complex (PDC) is a complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. citrate . Ambrose-Griffin MC, Danson MJ, Griffin WG, Hale G, Perham RN. Both NADPH and ATP are needed but not ribose 5 phosphate So you feed in G6P to from BIOCHEM 3361 at University of Texas, Dallas The kinases and phosphatases are allosteric enzymes . Cell. A50, 157–163 (1994). Accepts hydroxyethyl carbanion from TPP as an acetyl group. Lipoic acid was discovered nearly 60 years ago and was shown to be covalently attached to proteins in several multicomponent dehydrogenases. Article The hydroxyethyl attacks the reactive center of the lipoamide. The lipoamide arm in the glycine decarboxylase complex is not freely swinging. TPP is released and E1 is regenerated. LA: Lipoic Acid - the lipoamide “swinging arm” bound to a lysine residue on E2 - catalytic 3. Meths Enzymol. (2013), Nature Structural & Molecular Biology Structure 1, 217–222 (1993). They contain the lipoamide swinging arm that carries substrate to three different active sites. J. • Step 2: The hydroxyethyl group is transferred to E2 where it reacts with lipoamide (Swinging arm). ‘swinging arm’, referring to the lipoamide co-factor that is cova-lently attached to the lipoyl-domains of PDC E2 [13]. Brunger, A.T., Kuriyan, J. and Karplus, M., Crystallographics R-factor refinement by molecular dynamics. 278, 765–769 (1991). Bourguignon, J., Neuburger, M. & Douce, R. Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. 8600 Rockville Pike Together with the movement of lipoyl domains, the lipoamide-swinging arm provides the ability to span the gaps between the catalytic sites of each of the subunits (Mande et al., 1996) and provides the basis of the active-site coupling. E2), which uses lipoamide as a cofactor, and the dihydrolipoamide dehydrogenase (or E3). In the meantime, to ensure continued support, we are displaying the site without styles & Douce, R. Isolation of H-protein loaded with methylamine as a transient species in glycine decarboxylase reactions. Now we have a reduced E2 (dihydrolipoamide)-substrate (acetyl) complex. The 2-oxoglutarate dehydrogenase complex of (2-OGDH) Escherichia coli (M, -5 X lo6) is composed of three subunit enzymes: Elo, … Molecular shuttles play decisive roles in many multi-enzyme systems such as the glycine cleavage system (GCS) for one-carbon (C1) metabolism. To obtain J. Prot. des Martyrs, F38027, Grenoble Cedex, France, Department of Biological Structure, SM 20, University of Washington, Seattle, Washington, 98195, USA, Physiologie Cellulaire Végétale, Centre National de la Recherche Scientifique et Commisariat à I'Energie Atomique, Département de Biologie Moléculaire et Structural, 17 rue des Martyrs, F38054, Grenoble, Cedex 9, France, You can also search for this author in The next site visited by the swinging arm is the site where electrons are passed to another cofactor called FAD. Unable to load your collection due to an error, Unable to load your delegates due to an error. (2016), Microbiology and Molecular Biology Reviews This site needs JavaScript to work properly. 1977 Jul 28;268(5618):313-6. doi: 10.1038/268313a0. What functions as a swinging arm in PDC . The lipoamide acts as a swinging arm in the complex. Biol. -lipoamide prosthetic group acts as swing arm that visits the 3 active sites in the complex -subunits of complex arranged to accommodate swinging arm mechanism of lipoamide Pyruvate dehydrogenase reactions are a series of oxidation-reduction reactions J.appl.Crystallogr. Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step, Classification of ligand molecules in PDB with graph match-based structural superposition, Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic Pathway, Knockdown ofGDCHgene reveals reactive oxygen species-induced leaf senescence in rice. 6 Å-resolution of a lipoate containing protein: The H-protein of the glycine decarboxylase complex from pea leaves. This domain acts as a “swinging arm” and can reach the different catalytic sites on E1, E2, and E3 and thus allows an extreme form of substrate shuttling and of tight coupling of oxidation Thank you for visiting nature.com. Google Scholar. Biochem J. You are using a browser version with limited support for CSS. Purification and properties of the pyruvate dehydrogenase complex from Salmonella typhimurium and formation of hybrids with the enzyme complex from Escherichia coli. Now we have a reduced E2 (dihydrolipoamide)-substrate (acetyl) complex. As in the oxidized form, the reduced lipoate arm is localized at the surface of the protein and is able to move in the solvent. There they act as "swinging arms" that shuttle intermediates between two active sites (= covalent substrate channeling) of key metabolic enzymes. ... also called swinging arms” (Hezaveh et al., 2018). Opin. In eukaryotes, PDC is located in the mitochondria, linking cytosolic glycolysis to the mitochondrial TCA (tricarboxylic acid) cycle; plants possess mitochondrion- and chloroplast- In a fashion, similar to the three lipoate-dependent alpha-ketoacid dehydrogenases, the lipoamide arm acts as an acceptor for a methylene group from glycine, transfers it to folate, and is reduced in the process. Identification and purification of a distinct dihydrolipoamide dehydrogenase from pea chloroplasts. Get the most important science stories of the day, free in your inbox. Swinging arm can interact with the active sites of both E1 and E2 components of the PDH complex. Two vitamins, biotin and lipoic acid, are essential in all three domains of life. Acta crystallogr. The swinging arm carries excess electrons from the previous reaction in the form of two -SH groups. chem. Nature Structural Biology Neuburger, M., Jourdain, A. Another enzyme called PDH phosphatase (PDP) removes the phosphate groups making the enzyme active again. https://doi.org/10.1038/nsb0195-63, Communications Biology LA: Lipoic Acid - the lipoamide “swinging arm” bound to a lysine residue on E2 - catalytic 3. There they act as “swinging arms” that shuttle intermediates between two active sites (= covalent substrate channeling) of key metabolic enzymes. volume 2, pages63–68(1995)Cite this article. 255, 169–178 (1988). Mérand, V. et al. Lipoamide. This type of reaction typically involves redox coupled acyl transfer to CoA or phosphate and is mediated by additional cofactors, such as flavins, iron‐sulfur clusters or lipoamide swinging arms, which transmit the reducing equivalents that arise during keto acid oxidation to a final electron acceptor. Article PubMed Google Scholar, Cohen-Addad, C., Pares, S., Sieker, L. et al. Together with the movement of lipoyl domains, the lipoamide-swinging arm provides the ability to span the gaps between the catalytic sites of each of the subunits (Mande et al., 1996) and provides the basis of the active-site coupling. 4) Reaction 4: E3 reoxidizes the reduced lipoamide swinging arm by transferring two electrons to an E3 Cys-Cys disulfide bond. & Perham, R.N. Tax calculation will be finalised during checkout. E2-lipoamide . Sci. (2016), Plant, Cell & Environment Kinetic analysis of the role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Temperature-dependence of intramolecular coupling of active sites in pyruvate dehydrogenase multienzyme complexes. How do specific substrates effect the activity of pyruvate dehydrogenase? Coenzyme lipoamide is the protein-bound form of lipoic acid ; Animals can synthesize lipoic acid, it is not a vitamin ; Lipoic acid is an 8-carbon carboxylic acid with sulfhydryl groups on C-6 and C-8 ; Lipoamide functions as a swinging arm that carries acyl groups between active sites in multienzyme complexes ; 61 Lipoamide Electron-spin-resonance studies of the lipoamide 'swinging arm' of the pyruvate dehydrogenase multienzyme complex of Escherichia coli [proceedings]. Dihydrolipoamide Dehydrogenase* Electron Spin Resonance Spectroscopy; Escherichia coli/enzymology* Ethylmaleimide Bates DL, Danson MJ, Hale G, Hooper EA, Perham RN. E3, lipoamide dehydrogenase, carries an FAD cofactor which reoxidizes the lipoic acid of E2. Biochem Soc Trans, 6(1):225-226, 01 Jan 1978 Cited by: 2 articles | PMID: 205464 Trans. 148, 403–415 (1987). Lipoamide. (A) oxidation (B) reduction (C) condensation (D) ligation (E) None of the answers is correct. The lipoyl moieties are attached via an amide linkage to a lysine residue within each lipoyl domain in E2 that forms a lipoamide-swinging arm, though recent studies have shown the swinging arm to have a preferred orientation and thus restricted movement (Jones et al., 2000). SUMMARY Lipoic acid [( R )-5-(1,2-dithiolan-3-yl)pentanoic acid] is an enzyme cofactor required for intermediate metabolism in free-living cells. natn. Lipoamide and dihydrolipoamide are also attached to the H protein of the glycine cleavage complex. FAD: Flavin Adenine Nucleotide - bound to E3 & re-oxidizes lipoic acid - catalytic 4. PDH kinase binds to the E2 subunits, specifically the lipoamide swinging arm. Nature Struct Biol, 2, 63 – 68. Crossref CAS PubMed Web of Science® Google Scholar; Cronan JE (1989) The E.coli bio operon: transcriptional repression by an essential protein modification enzyme. Amongst a wide variety of different biochemical reactions in cellular carbon metabolism, thiamin diphosphate‐dependent enzymes catalyze the oxidative decarboxylation of 2‐keto acids. Electron-spin-resonance studies of the lipoamide 'swinging arm' of the pyruvate dehydrogenase multienzyme complex of Escherichia coli [proceedings]. Prevention and treatment information (HHS), National Library of Medicine FOIA The X-ray crystal structures of two forms of the H-protein have been determined. Which of the following functions as a "flexible swinging arm" when it transfers the reaction intermediate from one active site to the next? Selective inactivation of the transacylase components of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli. 1976 May 1;155(2):419-27. doi: 10.1042/bj1550419. Acta crystallogr. Amide bond links them, so forms a lipoamide. Please enable it to take advantage of the complete set of features! –swinging arm mechanism of lipoamide . PDH kinase binds to the E2 subunits, specifically the lipoamide swinging arm. and JavaScript. Biochem. 1996. 1983 Aug 1;213(2):331-8. doi: 10.1042/bj2130331. The substrate is held by the lipoamide-lysine ‘swinging arm’ Two different cofactors that contain the thiol group participate in the reaction Biotin is used for the decarboxylation step. TPP is released and E1 is regenerated. Acct. The substrate is held by the lipoamide-lysine ‘swinging arm’ Two different cofactors that contain the thiol group participate in the reaction Biotin is used for the decarboxylation step. Soc. They contain the lipoamide swinging arm that carries substrate to three different active sites. The position of lipoamide arm found in the molecule a was superposed (in red). This causes TPP to regenerate and oxidizes the hydrozxethyl group to acetyl • Step 3: E2 transfers acetyl group to CoA which fully reduces the lipoamide • Step 4: E3 reoxidizes lipoamide group of E2, Cys-Cys disuflide bond in enzyme is reduced 220, 223–224 (1991). Acetyl-CoA may then be used in the citric acid cycle to carry out cellular respiration, and this … The hydroxyethyl attacks the reactive center of the lipoamide. 1982 Jul 26;705(2):210-7. doi: 10.1016/0167-4838(82)90180-7. 2, 626–639 (1993). The lipoyl domain is therefore critical in … Nature. (2020), Photosynthesis Research Structural model of the pyruvate dehydrogenase complex The eukaryotic pyruvate dehydrogenase complex is the largest multienzyme complex known. the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Characterization of the primary structure of H-protein from Pisum sativum and localisation of a lipoic acid residue by combined LC-MS and LC-MS-MS. Biol Mass Spectrometry 22, 447–456 (1993). Both E1 and E3 bind to the E2 core to allow substrate channelling, which is facilitated by the so-called ‘swinging arm’, referring to the lipoamide co-factor that is covalently attached to the lipoyl-domains of PDC E2 . Privacy, Help Lipoic acid attached to a specific lysine side chain is assumed to act as a 'swinging arm' conveying the reactive dithiolane ring from one catalytic centre to another. Its structural and mechanistic heart is provided by the lipoic acid-containing H-protein which undergoes a cycle of reductive methylamination, methylamine transfer and electron transfer. Restricted Motion of the Lipoyl-Lysine Swinging Arm in the Pyruvate Dehydrogenase Complex of Escherichia coli,. Biochim Biophys Acta. Nature Struct Biol, 2, 63 – 68. The lipoamide dehydrogenase component of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli. all enzymes exept for what are in the mitochondrial matrix for citric acid cycle . Now we have a reduced E2 (dihydrolipoamide)-substrate (acetyl) complex. The pyruvate dehydrogenase complex consists of a core of E2 to which the other enzymes are attached. Careers. 1978;6(1):47-50. doi: 10.1042/bst0060047. Formation of citrate from acetyl CoA and oxaloacetate is a(n) _____ reaction. The kinases and phosphatases are allosteric enzymes . Bound through an amide bond linking the carboxyl group of lipoic acid with the ε-NH2 group of a lysine ("swinging arm"). 4) Reaction 4: E3 reoxidizes the reduced lipoamide swinging arm by transferring two electrons to an E3 Cys-Cys disulfide bond 5) Reaction 5 : E3 catalyzes transfer of electrons from the Cys sulfhydryl groups to NAD+, regenerating the oxidized form of E3 and releasing reduced NADH. Mattevi, A., de Kok, A. Would you like email updates of new search results? Many years of effort by scientists to elucidate the structural intracellular organization and interaction of the enzymes in the PDC led to the understanding of PDC as a great macromolecular machine consisting of many interacting enzymes “that are connected and regulated by highly flexible domains, also called swinging arms” (Hezaveh et al., 2018). Griffin MC, Griffin WG, Perham RN. Biochem Soc Trans, 6(1):225-226, 01 Jan 1978 Cited by: 2 articles | PMID: 205464 FATTY ACID METABOLISM IN APICOMPLEXAN PARASITES By Gustavo A. Afanador A dissertation submitted to Johns Hopkins University in conformity with the Google Scholar. CoA: Coenzyme A - acyl carrier - … The lipoamide is covalently bound to a lysine of the 80-amino-acid-long lipoyl domain of E2. Institut de Biologie Structural, Centre National de la Recherche Scientifique et Commisariat à I'Energie Atomique, 41 av. ConnerM, Krell T, Lindsay JG. The lipoamide acts as a swinging arm in the complex. Douce, R., Bourguignon, J., Brouquisse, R. & Neuburger, M. Isolation of plant mitochondria: general principles and criteria of integrity. ISSN 1545-9985 (online). LA is post-translationally attached to E2 and functions as the so-called ‘‘swinging arm’’ in the reaction catalysed by KADH complexes, accepting the acyl-moiety from E1 and transferring it … The implication of this observation in terms of the mechanism of the interaction of the H protein with the T protein, its physiological partner during the catalytic cycle, is discussed. 5) Reaction 5: E3 catalyzes transfer of electrons from the Cys sulfhydryl groups to NAD+, regenerating the oxidized form of E3 and releasing reduced NADH. Both NADPH and ATP are needed but not ribose 5 phosphate So you feed in G6P to from BIOCHEM 3361 at University of Texas, Dallas The active center of E1 with the ThDP cofactor is located at the bottom of a long funnel‐shaped substrate channel, which is suitable organized to accommodate a flexible E2‐linked lipoamide swinging arm for chemical coupling and intermediate channeling. CoA: Coenzyme A - acyl carrier - stoichiometric 5. Accessibility Chothia, C. & Murzin, A.G. New folds for all-β proteins. The phosphorylated form of PDC is inactive. Coenzyme lipoamide is the protein-bound form of lipoic acid ; Animals can synthesize lipoic acid, it is not a vitamin ; Lipoic acid is an 8-carbon carboxylic acid with sulfhydryl groups on C-6 and C-8 ; Lipoamide functions as a swinging arm that carries acyl groups between active sites in multienzyme complexes ; 61 Lipoamide PMID: 205464 [PubMed - indexed for MEDLINE] MeSH Terms. The Lipoamide Arm in the Glycine Decarboxylase is not Freely Swinging Cohen-Addad, C., Pares, S., Sieker, L., Neuburger, M., Douce, R. (1995) Nat Struct Biol 2: 63; Refined Structures at 2 and 2.2 A Resolution of Two Forms of the H-Protein, a Lipoamide-Containing Protein … There is only one E 3 gene and it supplies the dihydrolipoamide dehydrogenase activity for BCOADH, PDC, and OADH. 24, 958–961 (1991). Science 35, 458–460 (1987). Biol. Sci. Nature Structural Biology . Electron-spin-resonance studies of the lipoamide 'swinging arm' of the pyruvate dehydrogenase multienzyme complex of Escherichia coli [proceedings]. Our results indicate that the model of a freely swinging arm proposed for other lipoate-containing proteins is not acceptable in solution for the GDC. The pyruvate dehydrogenase complex consists of a core of E2 to which the other enzymes are attached. Res. Kikuchi, G. and Hiraga, K. The mitochondrial glycine cleavage system. True False Which of the following statements about the Citric acid cycle is FALSE? FAD: Flavin Adenine Nucleotide - bound to E3 & re-oxidizes lipoic acid - catalytic 4. That of the methylaminated form [] was drawn in blue. The E 3 subunits of the three enzymes are identical. Dardel, F., Davis, A.L., Laue, E.D. LA is post-translationally attached to E2 and functions as the so-called ‘‘swinging arm’’ in the reaction catalysed by KADH complexes, accepting the acyl-moiety from E1 and transferring it to coenzyme A to form acyl-CoA [1]. struct. Internet Explorer). Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipoylated H-protein from the pea leaf glycine cleavage system: A new automated method for the prediction of protein tertiary sructure. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of α-ketoacid dehydrogenase complexes that are central to intermediary metabolism. This reaction is set up so it is easy to cleave acetyl via CoA. Biochem., 45, 137–149 (1982). Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response.
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