SPEA Protein, E.coli (His)

SPEA is a key enzyme in cellular metabolism responsible for the biosynthesis of agmatine from arginine. This catalytic process involves the conversion of arginine to agmatine, thereby forming a complex network of biochemical pathways within the cell. SPEA Protein, E.coli (His) is the recombinant E. coli-derived SPEA protein, expressed by E. coli , with N-His labeled tag. The total length of SPEA Protein, E.coli (His) is 654 a.a., with molecular weight of ~77.4 kDa.

SPEA, also known as agmatine ureohydrolase, is an enzyme that plays a central role in the biosynthesis of agmatine from arginine. Specifically, SPEA catalyzes the conversion of arginine into agmatine, a process crucial in the metabolism of nitrogen-containing compounds. This enzymatic activity is a key step in the arginine catabolic pathway, contributing to the generation of agmatine, a biogenic amine with diverse physiological functions. It has to underscore SPEA's role in the synthesis of agmatine, shedding light on its importance in cellular nitrogen metabolism and the broader implications of agmatine in various biological processes.

E.coli

E. coli

N-His

P21170 (3D-656E)

947432  [NCBI]

DDMSMGLPSSAGEHGVLRSMQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAQLVKTREAQGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALIGEKMGHKVYLVIEKMSEIAIVLDEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLREAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEENGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTVPTAPAEDAPRALQSMWETWQEMHEPGTRRSLREWLHDSQMDLHDIHIGYSSGIFSLQERAWAEQLYLSMCHEVQKQLDPQNRAHRPIIDELQERMADKMYVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTQFRDQVKKTDLDAELQQQFLEEFEAGLYGYTYLE

Approximately 77.4 kDa

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

<1 EU/μg, determined by LAL method.