WebThe authors' structure with T3 reveals for the first time the location of the hormone binding site and shows its detailed interactions, as it demonstrates how a protein known as a thyroid hormone transporter can accommodate the ringed molecules required for its ketimine reductase activity. Mu‐crystallin (CRYM), first described as a structural component of … Webketimine reductase mu-crystallin, NADP-regulated thyroid-hormone binding protein, mu-crystallin homolog, thiomorpholine-carboxylate dehydrogenase. GeneRIFs: Gene …

Reactome CRYM [peroxisomal matrix]

WebDownload scientific diagram DMA was upregulated in CKD mice with platelet hyper-activation. A Serum DMA levels were measured at 6 weeks after left nephrectomy (n = … WebKetimine reductase mu-crystallin ecNumber1.5.1.25/ecNumber, CRYM_HUMAN Locations in the PathwayBrowser Expand all External Reference Information. External Reference … 91五十度灰

UniProt

Webal. 1989a). Wistow and Kim (1991) gave µ-crystallin its current name after they found the protein highly expressed in the lens of some marsupials. More recently, µ-crystallin has been shown to function as a ketimine reductase in addition to its activity as a NADPH-regulated thyroid hormone binding protein WebSpecifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. 91代内閣総理大臣