Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
Short sequence-paperCloning of murine cysteine sulfinic acid decarboxylase and its mRNA expression in murine tissues1
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Mammalian CSAD and GADL1 have distinct biochemical properties and patterns of brain expression
2015, Neurochemistry InternationalCitation Excerpt :The mRNA levels were determined by real-time reverse transcriptase (RT) -PCR quantification using specific DNA probes (Suppl. Table 1). As shown in Fig. 5A, the level of CSAD mRNA was much higher in mouse liver and kidney than in total brain extracts (4 (p = 1 × 10−6) and 7 times (p = 4 × 10−10) higher, respectively), and almost no CSAD mRNA was detected in the muscle, as reported previously (Ide et al., 2002; Park et al., 2002; Reymond et al., 2000). For GADL1 only low levels of mRNA were observed in adult brain compared with CSAD (p = 0.001), but was not detected in liver and kidney samples.
Role of glutamate decarboxylase-like protein 1 (GADL1) in taurine biosynthesis
2012, Journal of Biological ChemistryCitation Excerpt :Accordingly, it is reasonable to name it CSADC or CSADC isozyme. Although CSADC has generally been considered the primary enzyme for taurine synthesis, only a few mammalian CSADC enzymes have been experimentally characterized (16–18). Typical CSADC catalyzes cysteine sulfinic acid to hypotaurine that is the precursor of taurine and can be oxidized in vivo to taurine, but the enzyme has no activity to aspartate (9).
ID2 (inhibitor of DNA binding 2) is a rhythmically expressed transcriptional repressor required for circadian clock output in mouse liver
2009, Journal of Biological ChemistryCitation Excerpt :Taurine improves insulin sensitivity in Otsuka Long-Evans Tokushima Fatty rat, a model for type 2 diabetes (34). Taurine synthesis begins with the oxidation of cysteine to cysteine sulfinic acid, followed by decarboxylation to hypotaurine, which is catalyzed by the rate-limiting enzyme cysteine sulfinic acid decarboxylase (Csad or Csd) (35). Our microarray and qRT-PCR analyses reveal a dampened rhythm of Csad across all circadian phases.
Molecular dynamics simulations of the photoactive protein nitrile hydratase
2008, Biophysical JournalCitation Excerpt :By the end of 2007, 16 x-ray structures of Fe and Co-type NHases had been solved (6,14–18). There are a few proteins containing posttranslationally oxidized cysteines in the active site, such as reduced nicotinamide adenine dinucleotide peroxidase (24–26), peroxiredoxins (27–31), protein tyrosine phosphatase 1B (32), malate synthase (33), and cysteine sulfinic acid decarboxylase (34,35); but only NHases possess both Cys-SOH and Cys-SO2H in the catalytic center. The biological role of such modifications is not explained yet.
Taurine: New implications for an old amino acid
2003, FEMS Microbiology Letters
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The sequence presented in this paper is available from GenBank with the accession number AY033912.