The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Recombinant alpha Ketoglutarate Dehydrogenase (alphaKGDHC) Protein (His tag). Species: Mouse (Murine). Source: Insect Cells. Order product ABIN3135266.
1PMR: Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli.
article{f8b07abe-92c8-4537-b245-9a80b7fe538f, abstract = {The 2-oxoglutarate dehydrogenase multienzyme complex is composed of three different subenzymes: 2-oxoglutarate dehydrogenase (E1o), dihydrolipoamide transsuccinylase (E2o), and dihydrolipoamide dehydrogenase (E3). Bacillus subtilis E1o and E2o are encoded by the citK and citM genes, respectively. A 3.4-kb BamHI DNA fragment containing citK and citM markers was isolated from a library of B. subtilis DNA in Escherichia coli. Functional E2o was expressed from the cloned DNA both in B. subtilis and E. coli. E2o had an apparent Mr of 60000 when expressed in E. coli. The B. subtilis E2o component complemented an E. coli E2o-defective mutant in vivo and in vitro. It is concluded that functional B. subtilis E2o can be produced in E. coli and can interact with E. coli and E1o and E3 to form an active chimeric enzyme complex.}, author = {Carlsson, Peter and Hederstedt, Lars}, issn = {1879-0038}, keyword = {Recombinant DNA,2-oxoglutarate ...
Németh, Beáta and Dóczi, Judit and Csete, Dániel and Kacsó, Gergely and Ravasz, Dóra and Kiss, Gergely and Nagy, Ádám Miklós and Horváth, Gergő and Tretter, László and Mócsai, Attila and Csépányi-Kömi, Roland and Iordanov, Iordan and Ádám, Veronika and Chinopoulos, Christos (2016) Abolition of mitochondrial substrate-level phosphorylation by itaconic acid produced by LPS-induced Irg1 expression in cells of murine macrophage lineage. FASEB JOURNAL, 30 (1). pp. 286-300. ISSN 0892-6638 Ambrus, Attila and Nemeria, Natalia S. and Törőcsik, Beáta and Tretter, László and Nilsson, M. and Ádám, Veronika (2015) Formation of reactive oxygen species by human and bacterial pyruvate and 2- oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components. FREE RADICAL BIOLOGY AND MEDICINE, 89. pp. 642-650. ISSN 0891-5849 Dobolyi, Árpád and Bagó, Attila György and Gál, Anikó and Molnár, Mária Judit and Palkovits, M. and Ádám, Veronika and ...
GenBank) dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (E2)(dihydrolipoamide succinyltransferase component of 2-oxoglutaratedehydrogenase complex ...
The 2-oxoglutarate dehydrogenase (OGDH) complex is an important control point in vertebrate mitochondrial oxidative metabolism, including in the citrate cycle and catabolism of alternative fuels including glutamine. It is subject to allosteric regulation by NADH and the ATP/ADP ratio, and by Ca2+ through binding to the E1 subunit. The latter involves a unique Ca2+-binding site which includes D114ADLD (site 1). Here, we describe three splice variants of E1 in which either the exon expressing this site is replaced with another exon (loss of site 1, LS1) or an additional exon is expressed leading to the insertion of 15 amino acids just downstream of site 1 (Insert), or both changes occur together (LS1/Insert). We show that all three variants are essentially Ca2+-insensitive. Comparison of massive parallel sequence (RNA-Seq) databases demonstrates predominant expression of the Ca2+-sensitive archetype form in heart and skeletal muscle, but substantial expression of the Ca2+-insensitive variants in ...
enzyme of the Krebs cycle that catalyzes the oxidation of alpha-ketoglutarate to succinyl CoA. It is one of 3 alpha-ketoacid dehydrogenase enzymes, the others being pyruvate dehydrogenase and branched-chain ketoacid dehydrogenase. Each of these enzymes is a complex of multiple units. Each unit has 3 distinct subunits. The E1 (alpha-ketoacid decarboxylase), E2 (dihydrolipoyl transacetylase) and E3 (dihydrolipoyl dehydrogenase or lipoamide dehydrogenase) are identical in all 3 alpha-ketoacid dehydrogenases. Alpha-ketoglutarate dehydrogenase, fumarase, and succinate dehydrogenase are the only enzymes of the human Krebs cycle in which a single enzyme deficiency state has been defined. ...
Opens the Highlight Feature Bar and highlights feature annotations from the FEATURES table of the record. The Highlight Feature Bar can be used to navigate to and highlight other features and provides links to display the highlighted region separately. Links in the FEATURES table will also highlight the corresponding region of the sequence. More... ...
KGD1 유전자는 비허용온도에서 세포벽에 결함을 보이는 Saccharomyces cerevisiae LP0353 균주의 베타-1,3-글루칸 합성 효소의 활성을 회복시키는 유전자로 분리되었다. $\alpha$ -ketoglutarate dehydrogenase를 암호화하는 KGD1 유전자의 효모의 세포벽 합성과 연관된 기능을 분석하기 위하여 유전자 파괴를 시도하였다...
1C4T: Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase.
Complete information for OGDH gene (Protein Coding), Oxoglutarate Dehydrogenase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
K00164 2-oxoglutarate dehydrogenase E1 component [EC:1.2.4.2] , (GenBank) sucA; E1(0) component of 2-oxoglutarate dehydrogenase, subunit of 2-oxoglutarate decarboxylase, thiamin-requiring and 2-oxoglutarate dehydrogenase ...
sep:SE1097 K00164 2-oxoglutarate dehydrogenase E1 component [EC:1.2.4.2] , (RefSeq) sucA; 2-oxoglutarate dehydrogenase subunit E1 (A) MTKNKKEFTEAPVNFGANLGLMLDLYDDYLQDPSSVPEDLQVLFSTIKTGEAHIEAKPTT DGGGSQAGDSTIKRVMRLIDNIRQYGHLKADIYPVNPPERQNVPKLEIEDFDLDKETLEK ISSGIVSEHFKDIYDNAYDAIVRMERRYKGPIAFEYTHINNNKERVWLKRRIETPYKASL NDNQKKELFKKLAHVEGFEKYLHKNFVGAKRFSIEGVDTLVPMLQHTITLAGNEGIKNIQ IGMAHRGRLNVLTHVLEKPYEMMISEFMHTDPMKFLPEDGSLELTSGWTSDVKYHLGGVK TTNSYGIEQRISLANNPSHLEIVAPVVAGKTRAAQDNTHQVGAPSTDFHKAMPIIIHGDA AYPGQGINFETMNLGSLKGYSTGGSLHIITNNRIGFTTEPIDGRSTTYSSDVAKGYDVPI LHVNADDVEATIEAIEIAMEFRKEFHKDVVIDLVGYRRYGHNEMDEPSITNPVPYQNIRK HDSVEILYGKKLVDEGIISEDEMNEVIDGVQKEMRTAHDKIDKNDKMNNPDMEKPESLQL PLQSDTKDFSFDHLKEINDAMLDYPKDFHVLKKLNKVLEKRREPFEKEEGLVDWAQAEQL AFATILQDGTSIRLTGQDSERGTFSHRHAVLHDEENGNTFTPLHHVPQQQATFDIHNSPL SEAAVVGFEYGYNVENKGNFNIWEAQYGDFSNMSQMMFDNFLSSSRAKWGERSGLTLFLP HAFEGQGPEHSSARLERFLQLAAENNSTVVNLSSASNYFHLLRAQAASLDTLEMRPLIVM SPKSLLRNKTVAKPIDEFTSGGFKPIITEDIDEQKVKKVILASGKMYIDLKEYLAKNPND ...
Principal Investigator:KOIKE Kichiko, Project Period (FY):1993 - 1994, Research Category:Grant-in-Aid for General Scientific Research (C), Research Field:Pathological medical chemistry
MetabolismEnergy metabolismTCA cycledihydrolipoyllysine-residue succinyltransferase, E2 component of oxoglutarate dehydrogenase (succinyl-transferring) complex (TIGR01347; EC 2.3.1.61; HMM-score: 23.7) ...
An international team of scientists has discovered that the gene, OGDHL, a key protein required for normal function of the mitochondria -- the energy-producing factory of the cell -- and its chaperone, nardilysin (NRD1) are linked to progressive loss of neurological function in humans.
Ya memang benar. Jika kita menerima donor darah dikarenakan suatu alasan, belum tentu darah donor tersebut bebas 100% dari HIV. Meskipun kita mendapatkannya dari PMI lho.. Incoming search terms:odha indonesiaperiode jendela hivdonor darah hivscreening darah PMIPeriode jendelaapakah donor darah bisa ...
Mereka bersikap diskriminatif karena ketidak mengertian pada masalah yg sesungguh nya, sejalan dengan pengalaman, saya semakin lama makin menyadari bahwa kepercayaan itu begitu kecil dan rapuh, seperti cahaya lilin di tempat berangin. Saya ingin melihat orang melihat dan berkomunikasi kepada ...
Healthy Kids, Healthy Portland (HKHP), the group behind the campaign advocating to fluoridate the city of Portland, Oregons drinking water, has made a number of claims to justify their cause. Portland is the last major metropolitan city in the US to continually oppose the national trend of water fluoridation. On May 21st, 2013 Portland residents…
TY - JOUR. T1 - Specific reactivity of recombinant human PDC-E1α in primary biliary cirrhosis. AU - Iwayama, T.. AU - Leung, Patrick S. AU - Coppel, R. L.. AU - Roche, T. E.. AU - Patel, M. S.. AU - Mizushima, Y.. AU - Nakagawa, T.. AU - Dickson, R.. AU - Gershwin, M. Eric. PY - 1991. Y1 - 1991. N2 - The mitochondrial autoantigens recognized by autoantibodies in patients with primary biliary cirrhosis have been identified as components of related multi-enzyme complexes, including acyltransferases of the pyruvate dehydrogenase complex (PDC), the branched-chain α-keto acid dehydrogenase complex (BCODH), the α-ketoglutarate dehydrogenase complex (OGDC), protein X and pyruvate dehydrogenase (PDC) E1α and E1β. The major autoantigens, PDC-E2, BCODH-E2 and OGDC-E2, share some sequence homology; the epitopes on these antigens appear to be close to, or identical with, the lipoic acid binding site. Furthermore, all three antigens share some structural homology. In contrast, antibodies to PDC-E1α are ...
As something of an aside, the Deanna Protocol is interesting in its own right. The core supplement is (arginine-linked) alpha ketoglutarate. From the Protons point of view, if the alpha ketoglutarate enters the TCA at alpha ketoglutarate dehydrogenase and leaves it at malate, it would appear to be a very FADH2 selective input at complex II, generating an NADH:FADH2 ratio of 1:1, i.e. it is functioning as a rather specific FADH2 input. Were all aware that complex I dysfunction is a hallmark of neurodegenerative diseases and, in the absence of beta oxidation (were in neurons here), complex II is the primary route in to the CoQ couple for electrons via FADH2. Along with mtG3Pdh of course, if that happens to be active. I can see the logic to using this AKG to push complex II without the excess rise in non-usable NADH, which large amounts of acetyl-CoA provide. Im not surprised AKG is the core component of the Deanna Protocol and hats off to her father for picking this up ...
As something of an aside, the Deanna Protocol is interesting in its own right. The core supplement is (arginine-linked) alpha ketoglutarate. From the Protons point of view, if the alpha ketoglutarate enters the TCA at alpha ketoglutarate dehydrogenase and leaves it at malate, it would appear to be a very FADH2 selective input at complex II, generating an NADH:FADH2 ratio of 1:1, i.e. it is functioning as a rather specific FADH2 input. Were all aware that complex I dysfunction is a hallmark of neurodegenerative diseases and, in the absence of beta oxidation (were in neurons here), complex II is the primary route in to the CoQ couple for electrons via FADH2. Along with mtG3Pdh of course, if that happens to be active. I can see the logic to using this AKG to push complex II without the excess rise in non-usable NADH, which large amounts of acetyl-CoA provide. Im not surprised AKG is the core component of the Deanna Protocol and hats off to her father for picking this up ...
As something of an aside, the Deanna Protocol is interesting in its own right. The core supplement is (arginine-linked) alpha ketoglutarate. From the Protons point of view, if the alpha ketoglutarate enters the TCA at alpha ketoglutarate dehydrogenase and leaves it at malate, it would appear to be a very FADH2 selective input at complex II, generating an NADH:FADH2 ratio of 1:1, i.e. it is functioning as a rather specific FADH2 input. Were all aware that complex I dysfunction is a hallmark of neurodegenerative diseases and, in the absence of beta oxidation (were in neurons here), complex II is the primary route in to the CoQ couple for electrons via FADH2. Along with mtG3Pdh of course, if that happens to be active. I can see the logic to using this AKG to push complex II without the excess rise in non-usable NADH, which large amounts of acetyl-CoA provide. Im not surprised AKG is the core component of the Deanna Protocol and hats off to her father for picking this up ...
Thiamine or vitamin B1 is useful by acting as precursor for TPP. TPP is a form of coenzyme for enzymes such as transketolase in phosphate pathway, alpha ketoglutarate dehydrogenase in citric acid cycle, pyruvate dehydrogenase in glycolysis and branched
Arginine Alpha Ketoglutarate joaca un rol important in volumizarea celulelor, astfel incat nutrientii sunt transportati mai bine in muschi. Din acest motiv, Arginine Alpha Ketoglutarate de la MyProtein este un supliment care ajuta la imbunatatirea performantelor fizice si sprijina refacerea musculara dupa antrenament ...
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Compare Lipoamide Dehydrogenase ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
The regulatory properties of NAD(+)-isocitrate dehydrogenase and oxoglutarate dehydrogenase in extracts of yeast and rat heart mitochondria were studied under identical conditions. Yeast NAD(+)-isocitrate dehydrogenase exhibits a low K0.5 for isocitrate and is activated by AMP and ADP, but is insensitive to ATP and Ca2+. In contrast, the rat heart NAD(+)-isocitrate dehydrogenase was insensitive to AMP, but was activated by ADP and by Ca2+ in the presence of ADP or ATP. Both yeast and rat heart oxoglutarate dehydrogenase were stimulated by ADP, but only the heart enzyme was activated by Ca2+. All the enzymes studied were activated by decreases in pH, but to differing extents. The effects of Ca2+, adenine nucleotides and pH were through K0.5 for isocitrate or 2-oxoglutarate. These observations are discussed with reference to the deduced amino acid sequences of the constituent subunits of the enzymes, where they are available. ...
Molecular cloning of the Corynebacterium glutamicum (Brevibacterium lactofermentum AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase
U83218 Pseudomonas putida MnB1; ATCC 23483 Pseudomonas putida genomic clone transposon-tagged mutant UT6403 similar to 2-oxoglutarate dehydrogenase E1o subunit (sucA), genomic survey ...
U83218 Pseudomonas putida MnB1; ATCC 23483 Pseudomonas putida genomic clone transposon-tagged mutant UT6403 similar to 2-oxoglutarate dehydrogenase E1o subunit (sucA), genomic survey ...
Succinyl-CoA is an important intermediate in the citric acid cycle, where it is synthesized from α-Ketoglutarate by α-ketoglutarate dehydrogenase (EC 1.2.4.2) through decarboxylation, and is converted into succinate through the hydrolytic release of coenzyme A by succinyl-CoA synthetase (EC 6.2.1.5). Succinyl-CoA may be an end product of peroxisomal beta-oxidation of dicarboxylic fatty acids; the identification of an apparently specific succinyl-CoA thioesterase (ACOT4, EC 3.1.2.3, hydrolyzes succinyl-CoA) in peroxisomes strongly suggests that succinyl-CoA is formed in peroxisomes. Acyl-CoA thioesterases (ACOTs) are a family of enzymes that catalyze the hydrolysis of the CoA esters of various lipids to the free acids and coenzyme A, thereby regulating levels of these compounds. (PMID: 16141203 ...
Looking for online definition of lipoamide dehydrogenase in the Medical Dictionary? lipoamide dehydrogenase explanation free. What is lipoamide dehydrogenase? Meaning of lipoamide dehydrogenase medical term. What does lipoamide dehydrogenase mean?
Fingerprint Dive into the research topics of Purification of branched chain α-ketoacid dehydrogenase complex from rat liver. Together they form a unique fingerprint. ...
EC 1.8.1.4; other names: lipoamide reductase (NADH); lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; diaphorase; the E3 component of α‐ketoacid dehydrogenase complexes, an FAD‐flavoprotein enzyme that catalyses the oxidation by NAD+ of dihydrolipoamide ... ...
Each bottle contains 90 capsules. Product contains: 3500mg Complex Blend per 3 capsules containing: L-Arginine HCL, L-Arginine AKG (Alpha KetoGlutarate), Citrulline Malate.. ...
Direct Food Ingredients are suppliers of Ornithine Alpha Ketoglutarate 1:1 but we also stock other products in the Amino Acids range
During studies 44 years ago, researchers concluded that cyanobacteria were missing an essential enzyme of the metabolic pathway that is found in most other life forms," Bryant explained. "They concluded that cyanobacteria lacked the ability to make one enzyme, called 2-oxoglutarate dehydrogenase, and that this missing enzyme rendered the bacteria unable to produce a compound -- called succinyl-coenzyme A -- for the next step in the TCA cycle. The absence of this reaction was assumed to render the organisms unable to oxidize metabolites for energy production, although they could still use the remaining TCA-cycle reactions to produce substrates for biosynthetic reactions. As it turns out, the researchers just werent looking hard enough, so there was more work to be done." ...
The enzyme contains thiamine diphosphate and two [4Fe-4S] clusters. Highly specific for 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family
The G-protein-coupled receptors (GPCRs) family of proteins play essential roles in the heart, including in the regulation of cardiac hypertrophy. One member of this family, the oxoglutarate receptor 1 (OXGR1), may have a crucial role in the heart because it acts as a receptor for α-ketoglutarate, a metabolite that is elevated in heart failure patients. OXGR1 is expressed in the heart but its preci ...
ALT catalyzes the transfer of the amino group from L-alanine to α-ketoglutarate resulting in the formation of pyruvate and L-glutamate. Lactate dehydrogenase catalyzes the reduction of pyruvate and the simultaneous oxidation of NADH to NAD. The resulting rate of decrease in absorbance is directly proportional to ALT activity.. ...
OXGR1 - OXGR1 (Myc-DDK-tagged)-Human oxoglutarate (alpha-ketoglutarate) receptor 1 (OXGR1) available for purchase from OriGene - Your Gene Company.
GO:0015742. The directed movement of alpha-ketoglutarate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. ...
Thiamine (vitamin B1) is a water-soluble vitamin. It is absorbed from the gastrointestinal tract and taken up into tissues by transport proteins and converted to thiamine pyrophosphate (TPP) by thiamine pyrophosphokinase (TPPK). TPP is a co-factor of pyruvate dehydrogenase (PDH), α-ketoglutarate dehydrogenase and transketolase (TKT)-enzymes involved in the metabolism of glucose.. Various transport proteins are involved in the transport of thiamine monophosphate (TMP) and TPP across membranes. These include thiamine transported isoform-1 (THTR1) and thiamine transporter isoform-2 (THTR2), reduced folate carrier-1 (RFC-1), which transports TMP and TPP across cell plasma membranes and the mitochondrial TPP transporter (mTHTR). Thiamine and TMP/TPP transporters may have abnormal expression in diabetes. Increased THTR1 levels are found in red blood cells (RBCs) and mononuclear leucocytes of patients with diabetes compared to those of healthy subjects. RBC precursors and leucocytes appeared to ...
TY - JOUR. T1 - An nad synthetic reaction bypasses the lipoate requirement for aerobic growth of Escherichia coli strains blocked in succinate catabolism. AU - Hermes, Fatemah A.. AU - Cronan, John E.. PY - 2014/12/1. Y1 - 2014/12/1. N2 - The lipoate coenzyme is essential for function of the pyruvate (PDH) and 2-oxoglutarate (OGDH) dehydrogenases and thus for aerobic growth of Escherichia coli. LipB catalyzes the first step in lipoate synthesis, transfer of an octanoyl moiety from the fatty acid synthetic intermediate, octanoyl-ACP, to PDH and OGDH. E. coli also encodes LplA, a ligase that in presence of exogenous octanoate (or lipoate) can bypass loss of LipB. LplA imparts ΔlipB strains with a leaky growth phenotype on aerobic glucose minimal medium supplemented with succinate (which bypasses the OGDH-catalyzed reaction), because it scavenges an endogenous octanoate pool to activate PDH. Here we characterize a ΔlipB suppressor strain that did not require succinate supplementation, but did ...
In enzymology, an arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction succinyl-CoA + L-arginine ⇌ {\displaystyle \rightleftharpoons } CoA + N2-succinyl-L-arginine Thus, the two substrates of this enzyme are succinyl-CoA and L-arginine, whereas its two products are CoA and N2-succinyl-L-arginine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:L-arginine N2-succinyltransferase. Other names in common use include arginine succinyltransferase, AstA, arginine and ornithine N2-succinyltransferase, AOST, AST, and succinyl-CoA:L-arginine 2-N-succinyltransferase. This enzyme participates in arginine and proline metabolism. As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YLE. Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V (1988). "N2-succinylornithine ...
The activity of lipoamide dehydorgenase (E.C.1.6.4.3) was measured in arterial homogenates from very young pigeons (5-8 weeks old) known to differ in their susceptibility to atherosclerosis. The activity of the arterial enzyme was significantly lower in the atherosclerosis-susceptible White Carneau pigeons than it was in the atherosclerosis-resistant Show Racer pigeons. Lipoamide dehydrogenase is a component of the pyruvate dehydrogenase and alpha-ketoglutarate multienzyme complexes. The first complex catalyzes the conversion of pyruvate to oxaloacetate via acetyl-CoA, and this reaction represents a crucial link between glycolysis and the Krebs cycle. The second complex is essential for the oxidative breakdown of carbohydrates, fats, and amino acids via the Krebs cycle. Reduced activity of these complexes, resulting from low activity of lipoamide dehydrogenase, favors reduction of pyruvate to lactate and a shift to glycolysis. This situation is in accord with other results obtained in avian and ...
An enzyme that catalyzes the formation of 2 molecules of glutamate from Glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13 ...