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Selenocysteine lyase

selenocysteine lyase
Selenocysteine lyase (SCLY; EC 4.4.1.16) catalyzes the pyridoxal 5-prime phosphate-dependent conversion of L-selenocysteine to L-alanine and elemental selenium (Mihara et al., 2000 [PubMed 10692412]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Ethanolaminephosphotransferase, CK7, ACID, CAN, selenoprotein P
Papers on selenocysteine lyase
Diet-induced obesity in the selenocysteine lyase knockout mouse.
New
Berry et al., Honolulu, United States. In Antioxid Redox Signal, Nov 2015
AIMS: Selenocysteine lyase (Scly) mediates selenocysteine decomposition.
Interaction between vitamin B6 and source of selenium on the response of the selenium-dependent glutathione peroxidase system to oxidative stress induced by oestrus in pubertal pig.
New
Matte et al., Sherbrooke, Canada. In J Trace Elem Med Biol, Oct 2015
Gene expressions of GPX1, GPX3, GPX4, and selenocysteine lyase in liver and kidney were greatest in OSeB610 gilts (p<0.05).
Effects of acclimation salinity on the expression of selenoproteins in the tilapia, Oreochromis mossambicus.
Seale et al., Honolulu, United States. In J Trace Elem Med Biol, 2014
Gene expression of selenophosphate synthetase 1, Secp43, and selenocysteine lyase, factors involved in selenoprotein synthesis or in selenium metabolism, were also measured.
Hypoxia reduces and redirects selenoprotein biosynthesis.
Schomburg et al., Berlin, Germany. In Metallomics, 2014
Specifically, hypoxia decreases transcript concentrations of central factors controlling selenium and selenocysteine metabolism including selenophosphate synthetase-2, phosphoseryl-tRNA(SerSec) kinase and selenocysteine lyase, which are all proven to be rate-limiting enzymes in selenoprotein biosynthesis.
Mice lacking selenoprotein P and selenocysteine lyase exhibit severe neurological dysfunction, neurodegeneration, and audiogenic seizures.
Berry et al., Honolulu, United States. In J Biol Chem, 2014
Selenocysteine lyase (Scly) is an enzyme that plays an important role in selenium homeostasis, in that it catalyzes the decomposition of selenocysteine and allows selenium to be recycled for additional selenoprotein synthesis.
A novel upregulation of glutathione peroxidase 1 by knockout of liver-regenerating protein Reg3β aggravates acetaminophen-induced hepatic protein nitration.
Lei et al., Ithaca, United States. In Free Radic Biol Med, 2013
The enhanced GPX1 production in the KO mice was mediated by an 85% rise (p<0.05) in the activity of selenocysteine lyase (Scly), a key enzyme that mobilizes Se for selenoprotein biosynthesis.
Disruption of the selenocysteine lyase-mediated selenium recycling pathway leads to metabolic syndrome in mice.
Berry et al., Honolulu, United States. In Mol Cell Biol, 2012
Selenocysteine lyase (Scly) is the enzyme that supplies Se for selenoprotein biosynthesis via decomposition of the amino acid selenocysteine (Sec).
Absence of selenoprotein P but not selenocysteine lyase results in severe neurological dysfunction.
Berry et al., Honolulu, United States. In Genes Brain Behav, 2012
Almost all the known selenoproteins are found in brain, where expression is facilitated by selenocysteine (Sec)-laden selenoprotein P. The brain also expresses selenocysteine lyase (Scly), an enzyme that putatively salvages Sec and recycles the selenium for selenoprotein translation.
Biochemical discrimination between selenium and sulfur 2: mechanistic investigation of the selenium specificity of human selenocysteine lyase.
GeneRIF
Högbom et al., Stockholm, Sweden. In Plos One, 2011
A reaction mechanism whereby the Selenocysteine over Cysteine specificity is achieved using a combination of chemical and physico-mechanical control mechanisms.
Biochemical discrimination between selenium and sulfur 1: a single residue provides selenium specificity to human selenocysteine lyase.
GeneRIF
Högbom et al., Stockholm, Sweden. In Plos One, 2011
the X-ray crystal structure of human selenocysteine lyase and the key residue that provides the selenocysteine specificity
Proteomic characterization of a selenium-metabolizing probiotic Lactobacillus reuteri Lb2 BM for nutraceutical applications.
Pessione et al., Torino, Italy. In Proteomics, 2011
All the experimental results indicate that L. reuteri Lb2 BM is able to metabolize Se(IV), incorporating it into selenoproteins, through the action of a selenocysteine lyase, thus enhancing organic Se bioavailability.
Mammalian selenocysteine lyase is involved in selenoprotein biosynthesis.
Esaki et al., Uji, Japan. In J Nutr Sci Vitaminol (tokyo), 2010
Selenocysteine lyase (SCL) catalyzes the decomposition of L-selenocysteine to yield L-alanine and selenium by acting exclusively on l-selenocysteine.
Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.
Esaki et al., Uji, Japan. In J Biol Chem, 2010
Selenocysteine lyase (SCL) catalyzes the pyridoxal 5'-phosphate-dependent removal of selenium from l-selenocysteine to yield l-alanine.
[Differential display of messenger RNA and identification of selenocysteine lyase gene in hepatocellular carcinoma cells transiently expressing hepatitis C virus core protein].
GeneRIF
Gómez et al., Medellín, Colombia. In Biomedica, 2006
Results confirm that HCV core protein is associated with specific changes in mRNA expression, including the gene for selenocysteine lyase, which may be involved in the pathophysiology of hepatocellular carcinoma.
Selenocysteine Lyase.
Stadtman, In Ecosal Plus, 2004
The widespread distribution of selenocysteine lyase in numerous bacterial species was reported and the bacterial enzymes, like the pig liver enzyme, required pyridoxal phosphate as cofactor.
cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis.
GeneRIF
Esaki et al., Uji, Japan. In J Biol Chem, 2000
PMID:10692412 concerns mostly mouse selenocysteine lyase, however, refers to the sequence of the N-terminal region of putative human protein.
Use of selenite, selenide, and selenocysteine for the synthesis of formate dehydrogenase by a cysteine-requiring mutant ofEscherichia coli K-12.
Shrift et al., Binghamton, United States. In Biol Trace Elem Res, 1986
coli, and that selenocysteine is converted to elemental Se by the action of selenocysteine lyase, also present in the mutant.
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