DPYS Protein, Human (sf9, His-GST)

The DPYS protein plays a key role in the reductive pyrimidine degradation pathway by catalyzing the second step involving the reversible hydrolysis of dihydropyrimidines. Its enzymatic activity extends to the ring opening of 5,6-dihydrouracil, leading to the formation of N-carbamoyl-alanine, and the conversion of 5,6-dihydrothymine to N-carbamoyl-aminoisobutylene acid ester. DPYS Protein, Human (sf9, His-GST) is the recombinant human-derived DPYS protein, expressed by Sf9 insect cells , with N-GST, N-His labeled tag. The total length of DPYS Protein, Human (sf9, His-GST) is 519 a.a., with molecular weight of ~69 kDa.

Dihydropyrimidinase (DPYS) is an enzyme that plays a crucial role in the reductive pyrimidine degradation pathway, catalyzing the reversible hydrolytic ring opening of dihydropyrimidines. Specifically, DPYS can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. This enzymatic activity is a key step in the catabolism of pyrimidine derivatives, contributing to the breakdown of nucleotide and nucleic acid metabolites. The versatility of DPYS in the hydrolytic ring opening of dihydropyrimidines highlights its significance in maintaining pyrimidine homeostasis and the recycling of pyrimidine-related compounds within the cell. Understanding the functions of DPYS provides insights into the regulation of pyrimidine metabolism and its implications for cellular processes.

Human

Sf9 insect cells

N-GST;N-His

Q14117 (M1-P519)

1807  [NCBI]

Approximately 69 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.