| Description: | HMBS, or Porphobilinogen deaminase, is pivotal in heme biosynthesis, catalyzing the sequential polymerization of four porphobilinogen molecules to form hydroxymethylbilane. This process begins with dipyrromethane cofactor assembly, derived from porphobilinogen or preuroporphyrinogen, facilitated by the apoenzyme. The covalently linked cofactor serves as a primer for tetrapyrrole assembly, and in the final step, preuroporphyrinogen is released, leaving the intact cofactor bound to the holodeaminase. This enzymatic activity is crucial for heme synthesis, vital for diverse biological functions. HMBS/Porphobilinogen deaminase Protein, Human (HEK293, His) is the recombinant human-derived HMBS/Porphobilinogen deaminase protein, expressed by HEK293, with C-6*His labeled tag. The total length of HMBS/Porphobilinogen deaminase Protein, Human (HEK293, His) is 360 a.a., with molecular weight of ~47.0 kDa. |
