Pimeloyl-coa synthetase
WebProtein Putative pimeloyl-CoA synthetase Gene BIO1 Status UniProtKB unreviewed (TrEMBL) Organism Saccharomyces cerevisiae (Baker's yeast) Amino acids 346 Protein existence Inferred from homology Annotation score 1/5 Entry Feature viewer Publications External links History BLAST Download Add a publication Entry feedback Function GO … WebJun 15, 1999 · A pimeloyl-CoA synthetase from Pseudomonas mendocina 35 was purified and characterized, the DNA sequence determined, and the gene cloned into Escherichia …
Pimeloyl-coa synthetase
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WebDec 9, 2011 · Background: Pimeloyl-CoA is an intermediate of the biotin pathway, but it is unknown how it is synthesized in fungi.Results: Aspergillus nidulans mutants in β-oxidation are biotin-deficient, and the enzyme utilizing pimeloyl-CoA is targeted to the peroxisome.Conclusion: Pimeloyl-CoA is synthesized in the peroxisome via the β … WebIn Bacillus subtilis and most organisms, pimeloyl CoA, as a precursor, can be generated by pimeloyl-CoA synthetase (bioW gene product) from pimelic acid taken up or derived from fatty acid, whereas in E. coli, pimeloyl CoA is generated from fatty acid not via free pimelic acid but rather by bioC and bioH gene products.
WebOct 29, 2015 · Bacterial pimeloyl-CoA synthetase (BioW) acts as a highly specific substrate-selection gate, ensuring the integrity of the carbon chain in biotin synthesis ... Macromolecules Find similar proteins by: (by identity cutoff) 3D Structure Small Molecules Experimental Data & Validation Experimental Data Method: X-RAY DIFFRACTION … WebPimeloyl-CoA synthetase of P. mendocina is also a fusion protein with the same domain structure. All homologs in Pyrococcus sp. consist of separate α- and β- subunits; however, the domain structure of these subunits differs from that in SCS. The α-subunit represents a combination of the SCS α-subunit with the domain 5 of the SCS β-subunit ...
Webpimeloyl-CoA and cofactor S-adenosylmethionine (SAM), pimeloyl-CoA synthetase gene bioW from B. subtilis and SAM synthetase gene sam2 from Saccha-romyces cerevisiae were simultaneously introduced into recombinant E. coli overexpressing P. putida biotin pathway, which was found to be more efficient in biotin accumulation. Under the optimal ... WebThe four last steps of biotin biosynthesis, starting from pimeloyl-CoA, are conserved among all the biotin-producing microorganisms. Two enzymes of this pathway, the 8-amino-7 …
WebApr 17, 2024 · The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes (Journal Article) OSTI.GOV skip to main content Sign In Create Account Show …
WebOct 4, 2024 · Distant homologs, however, may exist for members of both families as manual analysis revealed proteins sharing 30.5% identity across their full lengths with a predicted … great marketing strategies for small businessWebPutative pimeloyl-CoA synthetase involved in biotin biosynthesis Molecular Function Manually Curated enables 6-carboxyhexanoate-CoA ligase activity ( ISS ) Biological … great marlborough productionsWebApr 17, 2024 · ( a) The enzyme pimeloyl-CoA synthetase (BioW) catalyzes the conversion of pimelic acid to the pimeloyl-CoA thioester via the pimeloyl-adenylate intermediate. Next, … We would like to show you a description here but the site won’t allow us. We would like to show you a description here but the site won’t allow us. flooding in haywards heathWebPimeloyl-CoA synthetase: 177: 179: COG1427: H Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) 386: 612: COG1429: H Cobalamin biosynthesis protein CobN, Mg-chelatase: 97: 98: COG1441: H ... Phosphoribosyl-dephospho-CoA transferase (holo-ACP synthetase) 144: 145: COG3840: flooding in haywood county ncWebJul 12, 2024 · In addition, two other classes of adenylate-forming enzymes are the aminoacyl-tRNA synthetases and specific subunits of non-ribosomal peptide synthetase-independent siderophore synthetases [8]. Recently, pimelate-CoA ligase BioW has been identified as a fourth class of adenylate-forming enzymes [5]. flooding in hayward caWebRecently, the discovery of BioW, a pimeloyl-CoA synthetase with a new structural fold, further expanded the diversity of the superfamily of adenylating enzymes 8,9. In all known cases of carboxylic acid activation by CoA, a single enzyme catalyzes two inseparable “half” reactions: adenylation and thioesterification (Fig. 1a) 6,7. Due to the ... flooding in healdsburg caWebJul 11, 2024 · The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes. Nat Chem Biol. 2024;13(6):668–74. pmid:28414711. View Article PubMed/NCBI Google Scholar 34. Wang M, Moynie L, Harrison PJ, Kelly V, Piper A, Naismith JH, et al. Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters. great marlborough estates