protein

HMBS/Porphobilinogen deaminase Protein, Human (N-His)

HY-P70269A

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

63;107;300;510;1200;1700 USD

HMBS/Porphobilinogen deaminase Protein, Human (N-His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

63;107;300;510;1200;1700 USD

472439236

HMBS (porphobilinogen deaminase) is key to heme biosynthesis, catalyzing the sequential polymerization of four porphobilinogen molecules to form hydroxymethylbiphenyl. The process begins with dipyrromethane cofactor assembly derived from porphobilinogen or preuroporphyrinogen and promoted by apoenzymes. HMBS/Porphobilinogen deaminase Protein, Human (N-His) is the recombinant human-derived HMBS/Porphobilinogen deaminase protein, expressed by E. coli , with N-6*His labeled tag.

Human

HMBS, also known as Porphobilinogen deaminase, plays a crucial role in the heme biosynthetic pathway by catalyzing the sequential polymerization of four molecules of porphobilinogen, leading to the formation of hydroxymethylbilane, also referred to as preuroporphyrinogen. The catalytic process initiates with the assembly of the dipyrromethane cofactor, derived either from two molecules of porphobilinogen or from preuroporphyrinogen, by the apoenzyme. This covalently linked cofactor serves as a primer, facilitating the assembly of the tetrapyrrole product. In the final step of catalysis, the product preuroporphyrinogen is released, leaving the intact cofactor bound to the holodeaminase. This enzymatic activity is pivotal for the synthesis of heme, a crucial component with diverse biological functions.

Porphobilinogen deaminase; PBG-D; Hydroxymethylbilane synthase (HMBS); Pre-uroporphyrinogen synthase

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.