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75387 Ensembl ENSG00000089163 ENSMUSG00000029524 UniProt Q9Y6E7 Q8R216 RefSeq (mRNA) NM_012240 NM_001385733 NM_001385734 NM_001385735 NM_001167691 NM_133760 RefSeq (protein) NP_036372 NP_001161163 NP_598521 Location (UCSC) Chr 12: 120.3 – 120.31 Mb Chr 5: 115.48 – 115.48 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Sirtuin 4, also known as SIRT4, is a mitochondrial protein ...
[2] [3] They are ancient in animal evolution and appear to possess a highly conserved structure throughout all kingdoms of life. [2] Chemically, sirtuins are a class of proteins that possess either mono- ADP-ribosyltransferase or deacylase activity, including deacetylase, desuccinylase , demalonylase , demyristoylase and depalmitoylase activity.
2,4,6-Triisopropylbenzenesulfonyl azide (trisyl azide) is an organic chemical used as a reagent to supply azide for electrophilic amination reactions, such as for the asymmetric synthesis of unnatural amino acids. [2]
Thus, the two substrates of this enzyme are ATP and 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine, whereas its two products are AMP and (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate. This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases).
Sirtuin 6 (SIRT6 or Sirt6) is a stress responsive protein deacetylase and mono-ADP ribosyltransferase enzyme encoded by the SIRT6 gene. [ 5 ] [ 6 ] [ 7 ] In laboratory research, SIRT6 appears to function in multiple molecular pathways related to aging, including DNA repair, telomere maintenance, glycolysis and inflammation . [ 5 ]
Individual PH domains possess specificities for phosphoinositides phosphorylated at different sites within the inositol ring, e.g., some bind phosphatidylinositol (4,5)-bisphosphate but not phosphatidylinositol (3,4,5)-trisphosphate or phosphatidylinositol (3,4)-bisphosphate, while others may possess the requisite affinity.
S-Aminoethyl-l-cysteine, also known as thialysine, is a toxic analog of the amino acid lysine in which the second carbon of the amino acid's R-group (side chain) has been replaced with a sulfur atom. Strictly speaking, L-thialysine is actually considered an S-(2-aminoethyl) analogue of L-cysteine.
ADDA ((all-S,all-E)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid) is a non-proteinogenic amino acid found in toxins made by cyanobacteria. Toxins which include this amino acid include microcystins [1] and nodularins. Along with leucine and arginine, it is found in microcystin-LR, an extremely toxic compound produced by ...