CSAD Protein, Mouse (His-SUMO)

CSAD proteins play a crucial role in the metabolism of sulfur-containing amino acids, catalyzing L-aspartate, 3-sulfinyl-L-alanine (cysteine sulfenic acid) and L-cysteine The acid is decarboxylated to produce β-alanine, hypotaurine and taurine respectively. Among these substrates, 3-sulfinyl-L-alanine is the preferred substrate for CSAD. CSAD Protein, Mouse (His-SUMO) is the recombinant mouse-derived CSAD protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of CSAD Protein, Mouse (His-SUMO) is 493 a.a., with molecular weight of ~71.1 kDa.

Cysteine sulfinic acid decarboxylase (CSAD) is an enzyme that catalyzes the decarboxylation of three substrates: L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate, resulting in the production of beta-alanine, hypotaurine, and taurine, respectively. Among these substrates, CSAD shows a preference for 3-sulfino-L-alanine. Notably, the enzyme does not exhibit any decarboxylation activity toward glutamate. The diverse substrate specificity of CSAD suggests its involvement in the biosynthesis of important metabolites, such as taurine and beta-alanine, which play roles in various physiological processes, including bile salt formation and neurotransmission. It has to highlight CSAD's ability to selectively decarboxylate specific substrates, shedding light on its significance in the cellular metabolism of sulfur-containing amino acids.

Mouse

E. coli

N-6*His;N-SUMO

Q9DBE0 (M1-L493)

246277  [NCBI]

MADSKPLRTLDGDPVAVEALLQDVFGIVVDEAILKGTSASEKVCEWKEPEELKQLLDLELQSQGESREQILERCRTVIHYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLKKLRALVGWNSGDGVFCPGGSISNMYAMNLARFQRYPDCKQRGLRALPPLALFTSKECHYSITKGAAFLGLGTDSVRVVKADERGRMIPEDLERQIILAEAEGSVPFLVSATSGTTVLGAFDPLDAIADVCQRHGLWFHVDAAWGGSVLLSRTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLRDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRVDCLKLWLMWKAQGGQGLERRIDQAFALTRYLVEEIKKREGFELVMEPEFVNVCFWFVPPSLRGKKESPDYSQRLSQVAPVLKERMVKKGTMMIGYQPHGTRANFFRMVVANPILAQADIDFLLGELELLGQDL

Approximately 71.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.