Molecular cloning and complete primary sequence of human erythrocyte porphobilinogen deaminase.
We have cloned and sequenced a cDNA clone coding for human erythrocyte porphobilinogen deaminase. It encompasses the translated region, part of the 5' and the 3' untranslated regions. The deduced 344 amino acid sequence is consistent with the molecular weight and the partial amino-acid sequence of the NH2 terminal of the purified erythrocyte enzyme. Southern analysis of human genomic DNA shows that its gene is present as a single copy in the human genome and Northern analysis demonstrates the presence of a single size species of mRNA in erythroid and non-erythroid tissues and in several cultured cell lines. Quantitative determinations indicate that the amount of PBG-D mRNA is modulated both by the erythroid nature of the tissue and by cell proliferation, probably at the transcriptional level.
D000595:Amino Acid Sequence; D000642:Ammonia-Lyases / Q000235:genetics*; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis; D004912:Erythrocytes / Q000201:enzymology; D005796:Genes; D006801:Humans; D011163:Hydroxymethylbilane Synthase / Q000235:genetics*; D004915:Leukemia, Erythroblastic, Acute; D015470:Leukemia, Myeloid, Acute; D011061:Poly A / Q000032:analysis; D012333:RNA, Messenger / Q000032:analysis
D012333:RNA, Messenger; D011061:Poly A; D004247:DNA; D011163:Hydroxymethylbilane Synthase; D000642:Ammonia-Lyases