UROD Protein, Human (His)

UROD proteins catalyze the sequential decarboxylation of the acetate side chain of uroporphyrinogen to form coproporphyrinogen and contribute to the fifth step of the heme biosynthetic pathway. UROD Protein, Human (His) is the recombinant human-derived UROD protein, expressed by E. coli , with N-6*His labeled tag. The total length of UROD Protein, Human (His) is 367 a.a., with molecular weight of ~40.0 kDa.

UROD protein plays a crucial role in the heme biosynthetic pathway by catalyzing the sequential decarboxylation of the four acetate side chains of uroporphyrinogen, resulting in the formation of coproporphyrinogen. Both isomer I and isomer III of uroporphyrinogen may serve as substrates, but only coproporphyrinogen III can be further converted to heme. This enzymatic process represents the fifth step in heme biosynthesis and is essential for the production of this critical component involved in various physiological functions. Additionally, in vitro experiments demonstrate UROD's capability to decarboxylate pentacarboxylate porphyrinogen I, underscoring its versatility in substrate specificity.

Human

E. coli

N-6*His

P06132 (M1-N367)

7389  [NCBI]

MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN

Approximately 40.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.