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  • protein
  • Here, the authors describe pathogenic variants in the GatCAB protein complex genes required for the generation of glutaminyl-mt-tRNA Gln , that impairs mitochondrial translation and presents with cardiomyopathy. (nature.com)
  • The exosome complex (or PM/Scl complex, often just called the exosome) is a multi-protein intracellular complex capable of degrading various types of RNA (ribonucleic acid) molecules. (wikipedia.org)
  • In the case of PNPase, which is a phosphorolytic RNA-degrading protein found in bacteria and the chloroplasts and mitochondria of some eukaryotic organisms, two RNase PH domains, and both an S1 and KH RNA binding domain are part of a single protein, which forms a trimeric complex that adopts a structure almost identical to that of the exosome. (wikipedia.org)
  • Because of this high similarity in both protein domains and structure, these complexes are thought to be evolutionarily related and have a common ancestor. (wikipedia.org)
  • While a human homologue of the protein exists, no evidence was found for a long time that its human homologue was associated with the human exosome complex. (wikipedia.org)
  • The multi-protein complex also serves as a machine for processing structured RNA precursors in the course of their maturation. (wikipedia.org)
  • gene
  • Here the authors use evolutionary alignments of NRPS/PKS gene clusters to guide rational design of complexes that can produce novel lactones. (nature.com)
  • acid
  • This complex catalyzes the overall conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA and CO2 during the citric acid cycle. (wikipedia.org)
  • yeast
  • Not long after, in 1999, it was realized that the exosome was in fact the yeast equivalent of an already described complex in human cells called the PM/Scl complex, which had been identified as an autoantigen in patients with certain autoimmune diseases years earlier (see below). (wikipedia.org)
  • In yeast, Rrp44 is associated with all exosome complexes and has a crucial role in the activity of the yeast exosome complex. (wikipedia.org)
  • interact
  • So the structure is like a molecular domain where RNA can interact as a substrate with each of the components and when this happens, it is really difficult for RNA to scape from the complex. (wikipedia.org)
  • forms
  • In Methanosarcina acetivorans , Hdr forms a multienzyme complex with acetyl-CoA decarbonylase synthase (ACDS), and F 420 -dependent methylene-H 4 MPT reductase (Mer). (unl.edu)
  • human
  • The entire human complex is 9.5 MDa in size, and has been described as 60-meric, meaning there are over 60 components that are assembled to make the entire complex. (wikipedia.org)
  • carbon
  • Existence of a Hdr:ACDS:Mer complex is consistent with growth phenotypes of ACDS and Mer mutant strains in which the complex samples the redox status of electron carriers and directs carbon flux to acetyl-CoA or methanogenesis. (unl.edu)
  • further
  • This is fast acting, and occurs within a few hours after a high dose At the molecular level and in further detail, nodularin is processed in a complex manner to induce toxic effects. (wikipedia.org)
  • links
  • We propose the Hdr:ACDS:Mer complex comprises a special class of multienzyme redox complex which functions as a ''biological router'' that physically links methanogenesis and acetyl-CoA biosynthesis pathways. (unl.edu)
  • Protein
  • DLD deficiency manifests itself in a great degree of variability, which has been attributed to varying effects of different DLD mutations on the stability of the protein and its ability to dimerize or interact with other components of the three α-ketoacid dehydrogenase complexes. (wikipedia.org)
  • In the case of PNPase, which is a phosphorolytic RNA-degrading protein found in bacteria and the chloroplasts and mitochondria of some eukaryotic organisms, two RNase PH domains, and both an S1 and KH RNA binding domain are part of a single protein, which forms a trimeric complex that adopts a structure almost identical to that of the exosome. (wikipedia.org)
  • Because of this high similarity in both protein domains and structure, these complexes are thought to be evolutionarily related and have a common ancestor. (wikipedia.org)
  • While a human homologue of the protein exists, no evidence was found for a long time that its human homologue was associated with the human exosome complex. (wikipedia.org)
  • The multi-protein complex also serves as a machine for processing structured RNA precursors in the course of their maturation. (wikipedia.org)
  • coenzymes
  • This complex requires the following 5 coenzymes: Thiamine pyrophosphate Flavin adenine dinucleotide (FAD) Nicotinamide adenine dinucleotide (NAD+) Lipoate Coenzyme A In animal tissue, BCKDC catalyzes an irreversible step in the catabolism of the branched-chain amino acids L-isoleucine, L-valine, and L-leucine, acting on their deaminated derivatives (L-alpha-keto-beta-methylvalerate, alpha-ketoisovalerate, and alpha-ketoisocaproate, respectively). (wikipedia.org)
  • components
  • Macroscopic investigations have revealed that the responses of the vessels and other local components of the damaged tissue are far more complex than might be thought of from macroscopic observation. (writtenproject.com)
  • domains
  • Many of these allosteric regulators act at the E1 domain of the enzyme complex, but all three domains of the enzyme complex can be allosterically controlled. (wikipedia.org)