|
type |
Journal Article |
authors |
Murakami, K.; Korbsrisate, S.; Asahara, N.; Hashimoto, Y.; Murooka, Y. |
title |
Cloning and characterization of the glutamate 1-semialdehyde aminomutase gene from Xanthomonas campestris pv. phaseoli |
journal |
Appl Microbiol Biotechnol |
Activity |
5.4.3.8 |
Family |
5.4.3.8 |
sel |
selected |
ui |
93159751 |
year |
(1993) |
volume |
38 |
number |
4 |
pages |
502-6. |
| |
keywords |
Amino Acid Sequence |
abstract |
The gene from Xanthomonas campestris pv. phaseoli for glutamate 1- semialdehyde (GSA) aminomutase, which is involved in the C5 pathway for synthesis of delta-aminolevulinic acid (ALA), was cloned onto a multicopy plasmid, pUC18, by the complementation of an ALA-deficient mutant (hemL) of Escherichia coli. Subcloning of deletion fragments from the initial 3.5-kb chromosomal fragment allowed the isolation of a 1.7-kb fragment which could complement the hemL mutation. Nucleotide sequence analysis of the 1.7-kb DNA fragment revealed an open reading frame (ORF) that is located downstream from a potential promoter sequence and a ribosome-binding site. The ORF encodes a polypeptide of 429 amino acid residues, and the deduced molecular mass of this polypeptide is 45,043 Da. The amino acid sequence shows a high degree of homology to the HemL proteins from other organisms, and a putative binding site for pyridoxal 5'-phosphate is conserved. |
last changed |
2008/05/21 16:26 |
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