PMID:1900346
| Citation |
Grimm, B, Bull, A and Breu, V (1991) Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli. Mol. Gen. Genet. 225:1-10 |
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| Abstract |
In bacteria 5-aminolevulinate, the universal precursor in the biosynthesis of the porphyrin nucleus of hemes, chlorophylls and bilins is synthesised by two different pathways: in non-sulphur purple bacteria (Rhodobacter) or Rhizobium 5-aminolevulinate synthase condenses glycine and succinyl-CoA into 5-aminolevulinate as is the case in mammalian cells and yeast. In cyanobacteria, green and purple sulphur bacteria, as in chloroplasts of higher plants and algae a three step pathway converts glutamate into 5-aminolevulinate. The last step is the conversion of glutamate 1-semialdehyde into 5-aminolevulinate. Using a cDNA clone encoding glutamate 1-semialdehyde aminotransferase from barley, genes for this enzyme were cloned from Synechococcus PCC6301 and Escherichia coli and sequenced. The popC gene of E. coli, previously considered to encode 5-aminolevulinate synthase, appears to be a structural gene for glutamate 1-semialdehyde aminotransferase. Domains with identical amino acid sequences comprise 48% of the primary structure of the barley, cyanobacterial and putative E. coli glutamate 1-semialdehyde aminotransferases. The cyanobacterial and barley enzymes share 72% identical residues. The peptide containing a likely pyridoxamine phosphate binding lysine is conserved in all three protein sequences. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Blotting, Southern; Cyanobacteria/enzymology; Cyanobacteria/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Hordeum/enzymology; Hordeum/genetics; Intramolecular Transferases; Isomerases/genetics; Isomerases/metabolism; Molecular Sequence Data; Open Reading Frames; Porphyrins/biosynthesis; Sequence Homology, Nucleic Acid |
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