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Human CRYM Protein expressed in Escherichia coli (E. coli) - ABIN666997
Kim, Gasser, Wistow: mu-crystallin is a mammalian homologue of Agrobacterium ornithine cyclodeaminase and is expressed in human retina. in Proceedings of the National Academy of Sciences of the United States of America 1992
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These findings confirm that, mechanistically, ketimine reductase/CRYM acts as a classical imine reductase and may explain the finding of bound pyruvate in the crystallized protein.
ketimine reductase is a key enzyme in the pipecolate pathway, which is the main lysine degradation pathway in the brain
The expression of mu-crystallin was regulated through the AP-1 (show FOSB Proteins) site in the promoter.
Its ketimine reductase activity is strongly inhibited by thyroid hormones.
This is the first report linking hyperglycemia with thyroid hormone (show PTH Proteins) binding protein CRYM and suggests that the role of CRYM in diabetic complications should be further investigated.
Identification of CRYM as a candidate responsible for nonsyndromic deafness, through cDNA microarray analysis of human cochlear and vestibular tissues
CRYM is a novel androgen-regulated gene whose expression is elevated in prostate cancer but down-regulated in castration therapy-resistant tumors.
Reduction of Crym expression in Huntington's disease (HD) could render striatal neurons more susceptible to mutant huntingtin (show HTT Proteins) suggesting that Crym may be a key determinant of the vulnerability of the striatum.
CRYM expression increases and sustains the T3 responsiveness of genes in cells, especially with alteration of the pericellular T3 concentration.
Comparison of the apo (show C9orf3 Proteins) and NADPH (show FDXR Proteins) forms reveals a rearrangement of the protein upon NADPH (show FDXR Proteins) binding that reduces the degrees of freedom of several residues and traps the conformation of the binding pocket in a more T3 competent state.
The expression of mu-crystallin was regulated through the AP-1 (show JUN Proteins) site in the promoter.
CRYM plays an important role in the development of the second peak of murine EIU.
Disruption of the CRYM gene decreases T(3) concentrations in tissues and serum without alteration of peripheral T(3) action in vivo.
Crystallins are separated into two classes and ubiquitous. The former class is also called phylogenetically-restricted crystallins. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. This gene encodes a taxon-specific crystallin protein that binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. The encoded protein does not perform a structural role in lens tissue, and instead it binds thyroid hormone for possible regulatory or developmental roles. Mutations in this gene have been associated with autosomal dominant non-syndromic deafness. Multiple alternatively spliced transcript variants have been found for this gene.
, mu-crystallin homolog
, mu-crystallin homolog-like
, mu-crystallin-like protein
, NADP-regulated thyroid-hormone binding protein
, ketimine reductase
, thiomorpholine-carboxylate dehydrogenase
, NADP-regulated thyroid-hormone-binding protein