Acid Dehydrogenase Complex Research Articles

Dldhcri3 zebrafish exhibit altered mitochondrial ultrastructure, morphology, and dysfunction partially rescued by probucol or thiamine.

Dihydrolipoamide dehydrogenase (DLD) deficiency is a recessive mitochondrial disease caused by variants in DLD, the E3 subunit of mitochondrial α-keto (or 2-oxo) acid dehydrogenase complexes. DLD disease symptoms are multisystemic, variably manifesting as Leigh syndrome, neurodevelopmental disability, seizures, cardiomyopathy, liver disease, fatigue, and lactic acidemia. While most DLD disease symptoms are attributed to dysfunction of the pyruvate dehydrogenase complex, the effects of other α-keto acid dehydrogenase deficiencies remain unclear. Current therapies for DLD deficiency are ineffective, with no vertebrate animal model available for preclinical study. We created a viable Danio rerio (zebrafish) KO model of DLD deficiency, dldhcri3. Detailed phenotypic characterization revealed shortened larval survival, uninflated swim bladder, hepatomegaly and fatty liver, and reduced swim activity. These animals displayed increased pyruvate and lactate levels, with severe disruption of branched-chain amino acid catabolism manifest as increased valine, leucine, isoleucine, α-ketoisovalerate, and α-ketoglutarate levels. Evaluation of mitochondrial ultrastructure revealed gross enlargement, severe cristae disruption, and reduction in matrix electron density in liver, intestines, and muscle. Therapeutic modeling of candidate therapies demonstrated that probucol or thiamine improved larval swim activity. Overall, this vertebrate model demonstrated characteristic phenotypic and metabolic alterations of DLD disease, offering a robust platform to screen and characterize candidate therapies.

Administration of branched-chain amino acids alters epigenetic regulatory enzymes in an animal model of Maple Syrup Urine Disease.

Maple Syrup Urine Disease (MSUD) is an autosomal recessive inherited disorder that affects the activity of the branched-chainα-keto acid dehydrogenase complex (BCDK). This deficiency on BCDK complex results in the accumulation of branched-chain amino acids (BCAA) leucine, isoleucine, valine, and their corresponding α-keto acids. Epigenetic changes can negatively affect the metabolism of BCAA. These changes are catalyzed by the epigenetic regulatory enzymes, e.g., DNA methyltransferase (DNMT), histone deacetylases (HDAC), and histone acetyltransferases (HAT). However, the impacts of BCAA administration on the activity of epigenetic regulatory enzymes in the brain of MSUD patients are still unknown. In this study, we aimed to demonstrate the impact of BCAA administration on the activity of DNMT, HDAC, and HAT in the brain structures of infant rats, an animal model of MSUD. For that, we administered a BCAA pool to infant rats for 21 days. We demonstrated that BCAA administration significantly increased the DNMT and HDAC activities in the hippocampus and striatum, but not in the cerebral cortex of MSUD infant rats. A positive correlation was observed between HDAC and DNMT activities in the hippocampus and striatum of animals exposed to BCAA injections. Our results showed that the BCAA administration could modulate epigenetic regulatory enzymes, mainly DNMT and HDAC, in the brains of infant rats. Therefore, we suggest that the increase in the activity of DNMT and HDAC in the hippocampus and striatum could partially explain the neurological impairments presented in animal models of MSUD.

Analysis of Branched‐Chain α‐Keto Acid Dehydrogenase Complex (BCKDC) Activity and Activity State in Rat Skeletal Muscle by Isotope Ratio Mass Spectrometry (IRMS) using 13C‐Labeled Stable Isotope Substrate

The BCKDC is the rate‐limiting enzyme in the catabolism of branched‐chain amino acids (BCAA). The radiochemical method has been used to measure the low level of the BCKDC activity in tissues such as skeletal muscle. In the present report, we introduced a non‐radioisotope method, using the α‐keto[1‐13C]‐isocaproate ([1‐13C]‐KIC) as stable isotope substrate. 13CO2 was released from [1‐13C]‐KIC in the reaction catalyzed by BCKDC. The ratio of 13CO2/12CO2 was measured by isotope ratio mass spectrometry. The detection limit of 13CO2 was estimated a few times lower than that of the radiochemical method. Using the purified BCKDC from bovine kidney, the production of 13CO2 was found to be linear with respect to reaction time (r2 = 0.9978) and quantity (r2 = 0.9920) of the enzyme. The muscle BCKDC activity measured by the new method was almost the same as that by the radiochemical method reported previously. Thus, we concluded that the novel assay method for the BCKDC activity is applicable to tissues containing the low level of the enzyme activity.

Recall rate and positive predictive value of MSUD screening is not influenced by hydroxyproline

Maple syrup urine disease (MSUD) is an autosomal recessive inherited disorder caused by the deficiency of the branched-chain 2-oxo acid dehydrogenase (BCOA-DH) complex. The worldwide incidence is approximately 1 in 185,000. MSUD is integrated in many "expanded" newborn screening (NBS) programs that use electrospray ionization tandem mass spectrometry (ESI-MS/MS). Elevated leucine, isoleucine, and alloisoleucine in the dried blood samples (DBS) of newborns are diagnostic parameters. However, with the applied method, it is not possible to distinguish the amino acids from each other, and also not from the other isobaric amino acid, hydroxyproline. While the branched chain amino acids (BCAA) leucine, isoleucine, and alloisoleucine are no diagnostic problem, because they are all elevated in MSUD patients, and, rather, increase the diagnostic sensitivity and specificity, hydroxyproline may cause false-positive screening results. Hydroxyproline is elevated in the benign familial condition hyperhydroxyprolinemia, which needs no medical intervention. The detection of cases with hyperhydroxyprolinemia have formerly been reported from screening programs that used thin-layer chromatography for phenylketonuria (PKU) screening, and, recently, two more cases have been reported, detected by ESI-MS/MS-based NBS. However, the detection of non-diseases is a heavy burden for screening programs and should be avoided if possible. With optimal settings for the quantitation of BCAAs and interpretation rules, elevated hydroxyproline should not cause false-positive screening results.

Plasmodium falciparum possesses organelle-specific α-keto acid dehydrogenase complexes and lipoylation pathways

The human malaria parasite Plasmodium falciparum possesses a single mitochondrion and a plastid-like organelle called the apicoplast. Both organelles contain members of the KADH (alpha-keto acid dehydrogenase) complexes--multienzyme complexes that are involved in intermediate metabolism. In the asexual blood stage forms of the parasites, the alpha-ketoglutarate dehydrogenase and branched chain KADH complexes are both located in the mitochondrion, whereas the pyruvate dehydrogenase is exclusively found in the apicoplast. In agreement with this distribution, Plasmodium parasites have two separate and organelle-specific pathways that guarantee lipoylation of the KADH complexes in both organelles. A biosynthetic pathway comprised of lipoic acid synthase and lipoyl (octanoyl)-ACP:protein Nepsilon-lipoyltransferase B is present in the apicoplast, whereas the mitochondrion is supplied with exogenous lipoic acid, and ligation of the metabolite to the KADH complexes is accomplished by a lipoate protein ligase A similar to that of bacteria and plants. Both pathways are excellent potential targets for the design of new antimalarial drugs.

Stimulatory effect of cold acclimation on skeletal muscle branched-chain α-keto acid dehydrogenase in rats

The effects of cold-acclimation (3 weeks at 4°C) on the actual activities of branched-chain α-keto acid dehydrogenase (BCKDH) and pyruvate dehydrogenase (PDH) complexes in the skeletal muscle and liver of normal 6-week-old rats were studied. The activities of BCKDH and PDH complexes were assayed using [1–14C] α-ketoisocaproate and [1-14C]pyruvate, respectively. Cold-acclimation markedly stimulated the activity of BCKDH, and slightly but significantly increased the activities of PDH and citrate synthase (CS) in the skeletal muscle, but did not alter PDH, BCKDH or CS activities in the liver. The increase in muscle BCKDH activity (control rats, 1.45 ± 0.54 mU/g wet wt; cold-acclimated rats, 2.54 ± 0.50 mU/g wet wt; 75% increase: P = 0.001) was much greater than the increases in PDH activity (84 ± 16 mU/g wet wt and 111 ± 25 mU/g wet wt; 32% increase: P = 0.020) or CS activities (27 ± 3 μmol/min per g wet wt and 31 ± 2 μmol/min per g wet wt; 14% increase: P = 0.046). These results suggest that, unlike PDH, BCKDH is not directly associated with the mitochondrial oxidative activity of the skeletal muscle of cold-acclimated rats. This study provides the first evidence that BCKDH in skeletal muscle responds selectively to cold-acclimation.

Hepatic branched-chain alpha-keto acid dehydrogenase complex in female rats: activation by exercise and starvation.

The effects of acute exercise and starvation on hepatic branched-chain alpha-keto acid dehydrogenase (BCKDH) complex activity were examined in female rats fed high (30%)- or low (8%)-protein diets. The total activity of the complex was significantly higher in the high protein-fed rats than in the low protein-fed rats but was not affected by acute exercise and starvation in either diet group. The proportion of the active form of BCKDH complex was less than 10% in both diet groups. Acute exercise and starvation markedly increased the active form of the complex in both diet groups. The activity of BCKDH kinase, which is responsible for inactivation of the BCKDH complex by phosphorylation, tended to be decreased by acute exercise and starvation in both diet groups. These results suggest that the activity of the BCKDH kinase is an important factor determining the proportion of the active form of BCKDH complex in exercise and starvation, and that the female rat is a useful model for studying the regulation of hepatic BCKDH complex activity.

Mammalian alpha-keto acid dehydrogenase complexes: gene regulation and genetic defects.

Recent application of the tools of molecular biology has provided insight with respect to the structure, regulation, and defects of the genes encoding the PDC and the BCKADC. cDNAs for the alpha-KGDC have only recently been cloned. Evidence for long-term regulation of the expression of the subunits of the PDC and the BCKADC has been obtained. Detailed analyses of the promoter-regulatory regions of the genes encoding the individual subunits of these complexes have provided leads as to molecular mechanisms involved. Evidence for coordinated regulation of expression of the subunits of the complexes has been obtained under some conditions but not others. Except for the PDC E1 alpha (X) promoter, the other promoters of the genes encoding PDC and BCKADC components are TATA-less with characteristics of housekeeping genes. Most cases of PDC deficiency, which produces lactic acidosis, are caused by defects in the coding region of the E1 alpha subunit. In contrast, gene defects that cause maple syrup urine disease are more heterogeneous, involving errors in any one of the subunits of the BCKADC. Alpha-KGDC deficiency has been reported but specific mutations have not been identified. Future work is expected to include detailed studies of the genes encoding the protein kinases and phosphatases that specifically regulate the PDC and the BCKADC by covalent modification.

Molecular basis of maple syrup urine disease and stable correction by retroviral gene transfer.

Maple syrup urine disease (MSUD) or branched-chain ketoaciduria is caused by a deficiency of the branched-chain alpha-keto acid dehydrogenase (BCKAD) complex. This results in the accumulation of the branched-chain amino acids (BCAA) and branched-chain alpha-keto acids (BCKA), which often produce severe neurological damage and mental retardation. The present studies focus on mutations in the E1 alpha gene of the BCKAD complex and their effects on the assembly of the E1 decarboxylase component of the enzyme complex. We have developed an efficient histidine-tagged bacterial expression system that allows the folding and assembly of E1 alpha and E1 beta subunits into the E1 heterotetramer (alpha 2 beta 2) in the presence of overexpressed chaperonins GroEL and GroES. The results of pulse-chase experiments with this bacterial expression system showed that a majority of the 15 known E1 alpha mutations, including the prevalent Y393N of Mennonite MSUD patients, decrease the rate of association of normal E1 beta with mutant E1 alpha. This results in limited or no assembly of mutant E1. It is concluded that the carboxy-terminal region of the E1 alpha subunit encoded by exons 7-9 is important for subunit interaction. To stably correct MSUD, we have developed a retroviral vector that contains a normal E1 alpha precursor complementary DNA. Transduction of cultured lymphoblasts from a Mennonite MSUD patient with this recombinant retroviral vector completely restored the rate of decarboxylation of BCKA. The normal decarboxylation activity in transduced MSUD cells remained stable without antibiotic selection during the 14-week study.(ABSTRACT TRUNCATED AT 250 WORDS)

Regulation of the alpha-keto acid dehydrogenase complexes and their involvement in primary biliary cirrhosis.

Annals of the New York Academy of SciencesVolume 573, Issue 1 p. 183-191 Regulation of the α-Keto Acid Dehydrogenase Complexes and Their Involvement in Primary Biliary Cirrhosis S. J. YEAMAN, S. J. YEAMAN Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Lister Institute Research Fellow.Search for more papers by this authorM. F. BASSENDINE, M. F. BASSENDINE Department of Medicine University of Newcastle upon Tyne NE2 4HH United Kingdom Supported by the Sir James Knott Trust.Search for more papers by this authorD. FITTES, D. FITTES Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorD. R. HODGSON, D. R. HODGSON Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Held a Vacation Scholarship from the Wellcome Trust.Search for more papers by this authorL. HESELTINE, L. HESELTINE Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorH. J. BROWN, H. J. BROWN Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Held a Schoolteacher Fellowship from the Biochemical Society.Search for more papers by this authorD. J. MUTIMER, D. J. MUTIMER Department of Medicine University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorO. F. W. JAMES, O. F. W. JAMES Department of Medicine University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorS. P. M. FUSSEY, S. P. M. FUSSEY Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Holder of a Research Studentship from the Science and Engineering Research Council, U.K.Search for more papers by this author S. J. YEAMAN, S. J. YEAMAN Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Lister Institute Research Fellow.Search for more papers by this authorM. F. BASSENDINE, M. F. BASSENDINE Department of Medicine University of Newcastle upon Tyne NE2 4HH United Kingdom Supported by the Sir James Knott Trust.Search for more papers by this authorD. FITTES, D. FITTES Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorD. R. HODGSON, D. R. HODGSON Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Held a Vacation Scholarship from the Wellcome Trust.Search for more papers by this authorL. HESELTINE, L. HESELTINE Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorH. J. BROWN, H. J. BROWN Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Held a Schoolteacher Fellowship from the Biochemical Society.Search for more papers by this authorD. J. MUTIMER, D. J. MUTIMER Department of Medicine University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorO. F. W. JAMES, O. F. W. JAMES Department of Medicine University of Newcastle upon Tyne NE2 4HH United KingdomSearch for more papers by this authorS. P. M. FUSSEY, S. P. M. FUSSEY Department of Biochemistry and Genetics University of Newcastle upon Tyne NE2 4HH United Kingdom Holder of a Research Studentship from the Science and Engineering Research Council, U.K.Search for more papers by this author First published: December 1989 https://doi.org/10.1111/j.1749-6632.1989.tb14996.x AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Volume573, Issue1Alpha‐Keto Acid Dehydrogenase Complexes: Organization, Regulation, and Biomedical RamificationsDecember 1989Pages 183-191 RelatedInformation

Isolated and Combined Deficiencies of the α‐Keto Acid Dehydrogenase Complexesa

Annals of the New York Academy of SciencesVolume 573, Issue 1 p. 337-346 Isolated and Combined Deficiencies of the α-Keto Acid Dehydrogenase Complexesa BRIAN H. ROBINSON, BRIAN H. ROBINSON Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorKATHY CHUN, KATHY CHUN Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorNEVENA MACKAY, NEVENA MACKAY Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorGAIL OTULAKOWSKI, GAIL OTULAKOWSKI Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorROUMYANA PETROVA-BENEDICT, ROUMYANA PETROVA-BENEDICT Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorHUNT WILLARD, HUNT WILLARD Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this author BRIAN H. ROBINSON, BRIAN H. ROBINSON Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorKATHY CHUN, KATHY CHUN Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorNEVENA MACKAY, NEVENA MACKAY Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorGAIL OTULAKOWSKI, GAIL OTULAKOWSKI Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorROUMYANA PETROVA-BENEDICT, ROUMYANA PETROVA-BENEDICT Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this authorHUNT WILLARD, HUNT WILLARD Departments of Genetics and Biochemistry University of Toronto and The Research Institute Hospital for Sick Children Toronto, Canada M5G 1X8Search for more papers by this author First published: December 1989 https://doi.org/10.1111/j.1749-6632.1989.tb15009.xCitations: 24 a This work was supported by the Medical Research Council of Canada, the National Foundation, the March of Dimes, and the Beta Sigma Phi Sorority. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Citing Literature Volume573, Issue1Alpha‐Keto Acid Dehydrogenase Complexes: Organization, Regulation, and Biomedical RamificationsDecember 1989Pages 337-346 RelatedInformation

Biochemical Basis of Pyruvate Dehydrogenase Complex Deficiency: Polypeptide Heterogeneity of E1α Subunit

Annals of the New York Academy of SciencesVolume 573, Issue 1 p. 461-462 Biochemical Basis of Pyruvate Dehydrogenase Complex Deficiency: Polypeptide Heterogeneity of E1α Subunit A. KITANO, A. KITANO Department of Pediatrics Kumamoto University Medical School Kumamoto 860, JapanSearch for more papers by this authorF. ENDO, F. ENDO Department of Pediatrics Kumamoto University Medical School Kumamoto 860, JapanSearch for more papers by this authorI. MATSUDA, I. MATSUDA Department of Pediatrics Kumamoto University Medical School Kumamoto 860, JapanSearch for more papers by this author A. KITANO, A. KITANO Department of Pediatrics Kumamoto University Medical School Kumamoto 860, JapanSearch for more papers by this authorF. ENDO, F. ENDO Department of Pediatrics Kumamoto University Medical School Kumamoto 860, JapanSearch for more papers by this authorI. MATSUDA, I. MATSUDA Department of Pediatrics Kumamoto University Medical School Kumamoto 860, JapanSearch for more papers by this author First published: December 1989 https://doi.org/10.1111/j.1749-6632.1989.tb15040.xAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL No abstract is available for this article. Volume573, Issue1Alpha‐Keto Acid Dehydrogenase Complexes: Organization, Regulation, and Biomedical RamificationsDecember 1989Pages 461-462 RelatedInformation

Cross‐Linking Studies of the Pyruvate Dehydrogenase Complex of Escherichia coli K‐12

Annals of the New York Academy of SciencesVolume 573, Issue 1 p. 400-401 Cross-Linking Studies of the Pyruvate Dehydrogenase Complex of Escherichia coli K-12 S. STEWART, S. STEWART Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorJ. BORVÁK, J. BORVÁK Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorP. BOIVIN, P. BOIVIN Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorT. TWOMEY, T. TWOMEY Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorW. H. SCOUTEN, W. H. SCOUTEN Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this author S. STEWART, S. STEWART Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorJ. BORVÁK, J. BORVÁK Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorP. BOIVIN, P. BOIVIN Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorT. TWOMEY, T. TWOMEY Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this authorW. H. SCOUTEN, W. H. SCOUTEN Department of Chemistry Baylor University Waco. Texas 76798Search for more papers by this author First published: December 1989 https://doi.org/10.1111/j.1749-6632.1989.tb15017.xAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume573, Issue1Alpha‐Keto Acid Dehydrogenase Complexes: Organization, Regulation, and Biomedical RamificationsDecember 1989Pages 400-401 RelatedInformation

Characterization and Conservation of the Inner E2 Core Domain Structure of the Bovine Branched‐Chain α‐Keto Acid Dehydrogenase Complexa

Characterization and Conservation of the Inner E2 Core Domain Structure of the Bovine Branched‐Chain α‐Keto Acid Dehydrogenase Complex^a

Molecular genetic basis for inherited human disorders of branched-chain alpha-keto acid dehydrogenase complex.

Molecular genetic basis for inherited human disorders of branched-chain alpha-keto acid dehydrogenase complex.

Expression and Assembly of Active Bovine Dihydrolipoyl Transacylase (E2b) Precursor in Escherichia colia

Annals of the New York Academy of SciencesVolume 573, Issue 1 p. 435-437 Expression and Assembly of Active Bovine Dihydrolipoyl Transacylase (E2b) Precursor in Escherichia colia THOMAS A. GRIFFIN, THOMAS A. GRIFFIN Departments of Medicine and Biochemistry Case Western Reserve University Cleveland, Ohio 44106 Medical Scientist Trainee supported by Grant 07250 from the National Institutes of Health.Search for more papers by this authorDAVJD T. CHUANG, Corresponding Author DAVJD T. CHUANG Departments of Medicine and Biochemistry Case Western Reserve University Cleveland, Ohio 44106cTo whom correspondence should be addressed at the Department of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, Texas 75235.Search for more papers by this author THOMAS A. GRIFFIN, THOMAS A. GRIFFIN Departments of Medicine and Biochemistry Case Western Reserve University Cleveland, Ohio 44106 Medical Scientist Trainee supported by Grant 07250 from the National Institutes of Health.Search for more papers by this authorDAVJD T. CHUANG, Corresponding Author DAVJD T. CHUANG Departments of Medicine and Biochemistry Case Western Reserve University Cleveland, Ohio 44106cTo whom correspondence should be addressed at the Department of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, Texas 75235.Search for more papers by this author First published: December 1989 https://doi.org/10.1111/j.1749-6632.1989.tb15031.xCitations: 1 a This work was supported by Grants DK 37373 and DK 26758 from the National Institutes of Health, by Grant 1-796 from the March of Dimes Birth Defects Foundation, and by the Veterans Administration. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL No abstract is available for this article.Citing Literature Volume573, Issue1Alpha‐Keto Acid Dehydrogenase Complexes: Organization, Regulation, and Biomedical RamificationsDecember 1989Pages 435-437 RelatedInformation

α‐Keto Acid Dehydrogenase Complexes: Organisation, Regulation, and Biomedical Aspects, Radission Plaza Hotel, Austin Texas‐November 16‐18, 1988.

α‐Keto Acid Dehydrogenase Complexes: Organisation, Regulation, and Biomedical Aspects, Radission Plaza Hotel, Austin Texas‐November 16‐18, 1988.

On the involvement of lipoic acid in .alpha.-keto acid dehydrogenase complexes

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTOn the involvement of lipoic acid in .alpha.-keto acid dehydrogenase complexesWilliam H. Rastetter, Julian Adams, John W. Frost, Larry J. Nummy, Jane E. Frommer, and Kenneth B. RobertsCite this: J. Am. Chem. Soc. 1979, 101, 10, 2752–2753Publication Date (Print):May 1, 1979Publication History Published online1 May 2002Published inissue 1 May 1979https://doi.org/10.1021/ja00504a055RIGHTS & PERMISSIONSArticle Views135Altmetric-Citations20LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (283 KB) Get e-Alerts Get e-Alerts