Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence.
The human erythrocyte 2,3-bisphosphoglycerate mutase (BPGM) is a multifunctional enzyme which controls the metabolism of 2,3-diphosphoglycerate (DPG), the main allosteric effector of haemoglobin. Several cDNA banks were constructed from reticulocyte mRNA either by conventional cloning methods in plasmid pBR322 and screening with specific mixed oligonucleotide probes, or in the expression vector lambda gt 11. The largest cDNA isolated was 1673 bases, and encodes for a protein of 258 amino acids; it contains a large 3' untranslated region (785 bases). It is slightly smaller than the size of the intact mRNA estimated by Northern blot (1800 bases). Our sequence data indicate differences with the previously published amino acid sequence involving 21% of the residues. They were entirely confirmed by the amino acid composition of the tryptic peptides derived from purified BPGM. The revised amino acid sequence of the human BPGM is presented.
D000595:Amino Acid Sequence; D001731:Bisphosphoglycerate Mutase / Q000097:blood / Q000235:genetics*; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics*; D006801:Humans; D010770:Phosphotransferases / Q000235:genetics*; D012333:RNA, Messenger / Q000097:blood / Q000235:genetics; D012156:Reticulocytes / Q000201:enzymology
D012333:RNA, Messenger; D004247:DNA; D010770:Phosphotransferases; D001731:Bisphosphoglycerate Mutase