Glutathione S-transferase (GST) isoenzymes of human pancreas were purified, characterized and evaluated for their possible role in the metabolism of ethanol. Human pancreas has at least two GST isoenzymes belonging to the Alpha class (pI 8.8 and 8.1), one belonging to the Mu class (pI 6.4) and one belonging to the Pi class (pI 4.9). During the purification of GSTs from pancreas as well as from heart, liver, lung, brain and muscle, the fatty acid ethyl ester synthase (FAEES) activity was monitored in order to evaluate the role of GSTs in metabolism of ethanol, as suggested in earlier studies. Both t.l.c. and h.p.l.c. were used to identify ethyl oleate in reaction mixtures to monitor FAEES activity. During the purification of GSTs with the use of affinity chromatography on GSH linked to epoxy-activated Sepharose 6B, FAEES and GST activities from each of these tissues segregated independently. Purified GST isoenzymes from these tissues did not exhibit any FAEES activity. Antibodies raised against ...
Shop Acyl-coenzyme A amino acid N-acyltransferase ELISA Kit, Recombinant Protein and Acyl-coenzyme A amino acid N-acyltransferase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Lecithin retinol acyltransferase (LRAT) is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester. This reaction is essential for the retinoid cycle in retinal photopigmentation and to metabolize vitamin A in the liver. Mutations in the LRAT gene have been associated with early-onset severe retinal dystrophy. LRAT is also known as phosphatidylcholine--retinol O-acyltransferase, LCA14, AI449251, and 1300010A18Rik.. ...
Lecithin retinol acyltransferase (LRAT) is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester. This reaction is essential for the retinoid cycle in retinal photopigmentation and to metabolize vitamin A in the liver. Mutations in the LRAT gene have been associated with early-onset severe retinal dystrophy. LRAT is also known as phosphatidylcholine--retinol O-acyltransferase, LCA14, AI449251, and 1300010A18Rik.. ...
A novel location of the bile-acid-conjugating enzyme bile acid-CoA:amino acid N-acyltransferase (BAT) has been discovered in the cytosolic fraction of rat kidney. Both taurine and glycine were utilized as substrates. Formation of bile acid N-acyl amidates was verified by h.p.l.c. by comparison with authentic standards and by specific hydrolysis using cholylglycine hydrolase. Immunoblot analysis using a human liver anti-BAT polyclonal antibody indicated that rat kidney BAT has the same molecular mass as rat liver BAT. These findings suggest that the kidney has a role in bile acid metabolism and physiology.. ...
This study has demonstrated the importance of NOME in mediating acute pancreatic toxicity and inflammation induced by alcohol, damage arising primarily from Ca2+-dependent mitochondrial dysfunction in PACs. Many theories have been proposed to explain the detrimental effects of alcohol in AP,22 ,23 including direct actions on Ca2+-release mechanisms,24 OME-sensitised mitochondrial dysfunction25 and formation of toxic FAEEs.26 The association between alcohol and fat in pancreatic damage is particularly intriguing; diets rich in corn oil and alcohol induce chronic pancreatic injury in rats.24 Epidemiological studies suggest that high fat diets may be linked to development of acute and chronic alcoholic pancreatitis,27 while hypertriglyceridaemia is an independent risk factor for both.28 The present data highlight the importance of NOME in mediating acute PAC damage leading to AP. It is likely that under conditions of OME inhibition, available alcohol and fatty acid from triglyceride hydrolysis are ...
Glycylpeptide N-tetradecanoyltransferase 1 also known as myristoyl-CoA:protein N-myristoyltransferase 1 (NMT-1) is an enzyme that in humans is encoded by the NMT1 gene. GRCh38: Ensembl release 89: ENSG00000136448 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000020936 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Duronio RJ, Reed SI, Gordon JI (May 1992). "Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae". Proc Natl Acad Sci U S A. 89 (9): 4129-33. doi:10.1073/pnas.89.9.4129. PMC 525646 . PMID 1570339. "Entrez Gene: NMT1 N-myristoyltransferase 1". Rajala RV, Datla RS, Moyana TN, et al. (2000). "N-myristoyltransferase". Mol. Cell. Biochem. 204 (1-2): 135-55. doi:10.1023/A:1007012622030. PMID 10718634. Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580-5. doi:10.1093/embo-reports/kve141. PMC 1083955 . ...
A combination of site-directed and random mutagenesis generated sequence variants of a plastidial lysophosphatidic acid acyltransferase. Alanine substitutions of residues present within two conserved motifs including the putative catalytic histidine resulted in a loss of acyltransferase activity assessed as complementation competance. Substitutions at five sites within the central core resulted in reduced or loss of activity. Truncation mutants reveal that sequences in the C-terminal moiety are essential for function.. ...
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This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 2012 ...
Using 5-rapid amplification of cDNA ends, we have identified an extended 5-end of mRNA coding for human myristoyl-CoA:protein N-myristoyltransferase (NMT). PCR using primers based on this new 5-sequence and reverse primers within the currently accepted coding sequence of the enzyme resulted in the identification of a novel splice variant of NMT. In vitro translation of these cDNAs resulted in the production of proteins with apparent molecular masses of 63 kDa and 48 kDa. Immunoprecipitation of NMT from human cell lines and immunoblotting of a range of rat tissues has identified proteins with molecular masses corresponding to those derived from these cDNAs, and provided evidence that their relative abundance differs among tissues. Our results provide evidence that this enzyme exists in different forms resulting from alternative splicing of the mRNA ...
GPI transamidase component PIG-T is an enzyme that in humans is encoded by the PIGT gene. This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. PIGT has been shown to interact with PIGK and GPAA1. GRCh38: Ensembl release 89: ENSG00000124155 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000017721 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Vainauskas S, Menon AK (Apr 2005). "Endoplasmic reticulum localization of Gaa1 and PIG-T, subunits of the glycosylphosphatidylinositol transamidase complex". J Biol Chem. 280 (16): 16402-9. doi:10.1074/jbc.M414253200. PMID 15713669. "Entrez Gene: ...
Proteins that have a GPI glycolipid modification are acknowledged to be key in the lifecycle of Plasmodium; for example the involvement of the GPI-anchored MSP1 on merozoites in erythrocyte invasion. The enzyme that transfers the preformed GPI to the proteins such as MSP1 is named GPI:protein transamidase, however, studying this enzyme biochemically has been arduous, due to the following hurdles. Firstly, the GPI:protein transamidase functions as a subunit in multidomain complex, some components of which maybe membrane associated, and there are no reports of functional recombinant reconstitution of this complex. Secondly, there are no convenient and sensitive transamidase assays available that are amenable to medium/high throughput studies, even though large small molecule cysteine peptidase inhibitor libraries exist and can be used to studying this enzyme.. Any input/thoughts on how to overcome the aforementioned obstacles in studying the Plasmodium GPI:protein transamidase would be most ...
Complete information for BAAT gene (Protein Coding), Bile Acid-CoA:Amino Acid N-Acyltransferase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
BioAssay record AID 144067 submitted by ChEMBL: Tested for Inhibitory concentration against human N-myristoyltransferase (NMT) in radiochemical HPLC end point assay with peptide GNAASARR-NH2 and [3H]myristoyl-CoA radioligand at 1 uM; ND=Not determined.
Site-directed mutagenesis of rodent liver bile acid CoA: amino acid N-acyltransferase (BAT) - this project involves a combination of molecular biology, enzymology and protein mass ...
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Поиск диссертаций, авторефератов, научных статей и публикаций в русскоязычных источниках и периодике. LpxM(msbB) mutant
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
lipoyltransferase II: transfers lipoyl group from lipoyl-AMP to the specific lysine residue of lipoate-dependent enzymes; isolated from bovine liver; amino acid sequence in first source; GenBank AB006441
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This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in lysine
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BY MARY L. CHANG. Diglyceride acyltransferase, known to lipidologists as DGAT, gets a lot of attention in the April issue of the Journal of Lipid Research, where its the focus of an article by researchers at Columbia University and AstraZeneca and a related commentary. ...
Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. ...
Támogatás a teljes projektciklus folyamán a partnerkereséstől a projekt lezárásáig, és az eredmények hasznosításáig. Szolgáltatások: képzés, pályázatbeadás, eredmények hasznosítása, népszerűsítés, projekt menedzsment és audit támogatás.
The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor. Not identical with EC 2.3.1.68 glut
MOGAT2山羊多克隆抗体(ab106247)可与人样本反应并经WB实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
A RUGALMAS FOGLALKOZTATÁS ELTERJESZTÉSE A SZÉCHENYI 2020 PROGRAM TÁMOGATÁSÁVAL 11 KONZORCIUM EGYÜTTMŰKÖDÉSÉBEN. 2,007 milliárd forint európai uniós támogatás segítségével valósul meg a rugalmas foglalkoztatás elterjesztését célzó Széchenyi 2020 pályázat GINOP 5.3.1., „A" komponense. A pályázat célkitűzése, hogy a konvergencia régiókban működő kis- illetve közepes vállalatok (kkv-k) szakmailag magas szintű, száz százalékosan finanszírozott átvilágítási, tanácsadói és fejlesztői szolgáltatást vehessenek igénybe munkaszervezésük rugalmasabbá tételéhez. A Széchenyi 2020 Program keretében 2014-ben jelent meg „A rugalmas foglalkoztatás elterjesztése a konvergencia régiókban" című pályázat, melynek „A munkáltatói átvilágítást végző szervezetek kiválasztása és az átvilágítás lefolytatása" elnevezésű „A" komponense a szervezeti kultúra fejlesztésének és a munka-magánélet összhangjának támogatását ...
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Genetic information processingProtein fateProtein modification and repairapolipoprotein N-acyltransferase (TIGR00546; EC 2.3.1.-; HMM-score: 15.1) ...
The Ca2+ ionophore 4-Br A23187 is effective in increasing [Ca2+]i and eliciting secretion when ICRAC is inhibited by SK&F 96365. Antigen (Ag) (1 μg/ml) sti
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(R)-Lisofylline ((R)-Lisophylline) is a (R)-enantiomer of the metabolite of Pentoxifylline with anti-inflammatory properties. (R)-Lisofylline is a lysophosphatidic acid acyltransferase inhibitor with an IC50 of 0.6 µM and interrupts IL-12 signaling-mediated STAT4 activation. (R)-Lisofylline has the potential for type 1 diabetes, autoimmune disorders research. - Mechanism of Action & Protocol.
Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors (By similarity). Converts lysophosphatidylcholine to phosphatidycholine.
Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors ...
The budding yeast ALE1 gene encodes a lysophospholipid acyltransferase (LPLAT) with broad specificity. We show that yeast LPLAT (ScLPLAT) belongs to a distinct protein family that includes human MBOAT1, MBOAT2, MBOAT4, and several closely related proteins from other eukaryotes. We further show that two plant proteins within this family, the Arabidopsis proteins AtLPLAT1 and AtLPLAT2, possess lysophospholipid acyltransferase activities similar to ScLPLAT. We propose that other members of this protein family, which we refer to as the LPLAT family, also are likely to possess LPLAT activity. Finally, we show that ScLPLAT differs from the specific lysophosphatidic acid acyltransferase that is encoded by SLC1 in that it cannot efficiently use lysophosphatidic acid produced by acylation of glycerol-3-phosphate in vitro.. ...
1C4T: Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase.
Mice with genetic disruption of the DGAT1 or DGAT2 genes have been made by the Farese laboratory at UCSF. Surprisingly, DGAT1−/− mice[8] are healthy and fertile and have no changes in triglyceride levels. These mice are also lean and resistant to diet-induced obesity, consequently generating interest in DGAT1 inhibitors for the treatment of obesity. However, these mice also fail to lactate, showing a complete lack of milk production due to their inability to produce milk lipid droplets.[8] In contrast, DGAT2−/− mice[9] have reduced triglyceride levels but are lipopenic, suffer from skin barrier abnormalities (including the inability to retain moisture), and die shortly after birth. ...
BioAssay record AID 143943 submitted by ChEMBL: The compound was tested for the affinity against Candida albicans N-myristoyltransferase (NMT).
Falany, C.N., Johnson, M.R., Barnes, S. and Diasio, R.B. (1994). „Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase". J. Biol. Chem. 269: 19375-19379. PMID 8034703 ...
Acyltransferase which contributes to the regulation of free arachidonic acid (AA) in the cell through the remodeling of phospholipids. Mediates the conversion of lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Required for cortical lamination during brain development (By similarity).
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Seed triacylglycerol (TAG) biosynthesis involves a metabolic network containing multiple different diacylglycerol (DAG) and acyl donor substrate pools. This network of pathways overlaps with those for essential membrane lipid synthesis and utilizes multiple different classes of TAG biosynthetic enzymes. Acyl flux through this network ultimately dictates the final oil fatty acid composition. Most strategies to alter seed oil composition involve the overexpression of lipid biosynthetic enzymes, but how these enzymes are assembled into metabolons and which substrate pools are used by each is still not well understood. To understand the roles of different classes of TAG biosynthetic acyltransferases in seed oil biosynthesis, we utilized the Arabidopsis thaliana diacylglycerol acyltransferase mutant dgat1-1, (in which phosphatidylcholine:diacylglycerol acyltransferase (AtPDAT1) is the major TAG biosynthetic enzyme), and enhanced TAG biosynthesis by expression of Arabidopsis acyltransferases AtDGAT1 ...
jats:p,Several years of extensive research using the new powerful techniques of molecular biology have enabled the direct comparison of functionally or evolutionarily related genes and their products at the nucleotide and aminoacid sequence levels. Two types of synthase with similar functions are discussed as an interesting example. Stilbene synthases, e.g. resveratrol synthase, produce the stilbene backbone as a key reaction in the biosynthesis of stilbene-type phytoalexins. Chalcone synthase is a key enzyme in the biosynthesis of flavonoids, including certain phytoalexins derived from a 6′-deoxychalcone which is synthesized by cooperation of chalcone synthase with a reductase. Resveratrol and chalcone synthases utilize the same substrates (4-coumaroyl-CoA and 3 molecules of malonyl-CoA ) and catalyze the same condensing type of enzyme reaction (resulting in sequential addition of acetate units via malonyl-CoA ), but the products differ in the newly formed ring systems (resveratrol and ...
Triacylglycerol (TAG) is a major component of lipid storage in yeast. The acyl CoA: diacylgycerol acyltransferase (DGAT) that catalyzes the final and rate-limiting step in the production of TAG is rather interesting. Consequently, cloning and analysis of the gene-encoding TAG synthase, diacylglycerol acyltransferase gene (DGA1), of the oleaginous yeast Rhodosporidiobolus fluvialis DMKU-RK253 were undertaken. Analysis of the deduced amino acid sequence of DGA1 from R. fluvialis DMKU-RK253 (RfDGA1) showed similarity with the acyl-CoA:diacylglycerol acyltransferase 2 (DGAT2) from other organisms. The cDNA of RfDGA1 was cloned into the yeast expression vector pYES2 and heterologously overexpressed in Saccharomyces cerevisiae. One of the transformants showed a 1.6-fold increase in lipid content compared with the wild-type strain harbouring the pYES2 empty vector. Furthermore, DGA1 overexpression in R. fluvialis DMKU-RK253 resulted in a 2.5-fold increase in lipid content when compared with the wild-type
GenBank) dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (E2)(dihydrolipoamide succinyltransferase component of 2-oxoglutaratedehydrogenase complex ...