gucD Protein, Bacillus subtilis (His, Strep)

The gucD protein is an important enzyme that catalyzes the irreversible ammonia removal of L-kynurenine to generate kynurenic acid (KA). This process is part of the tryptophan catabolic pathway and produces KA, known for its broad-spectrum antagonistic activity at excitatory amino acid receptors. gucD Protein, Bacillus subtilis (His, Strep) is the recombinant gucD protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of gucD Protein, Bacillus subtilis (His, Strep) is 487 a.a., .

KYAT1 protein orchestrates the irreversible transamination of the L-tryptophan metabolite L-kynurenine, culminating in the formation of kynurenic acid (KA). This process holds significance within the tryptophan catabolic pathway and yields KA, known for its broad-spectrum antagonistic activity against the three ionotropic excitatory amino acid receptors, among others. Beyond its role in tryptophan metabolism, KYAT1 is involved in the transformation of cysteine conjugates from specific halogenated alkenes and alkanes into reactive metabolites. Furthermore, KYAT1 catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, leading to the cleavage of the C-S or C-Se bond. The diverse enzymatic activities of KYAT1 underscore its involvement in key metabolic pathways and xenobiotic processing.

Others

E. coli

N-Strep;N-6*His

P42236 (S2-P488)

938406

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

<1 EU/μg, determined by LAL method.