|
type |
Journal Article |
authors |
Foglino, M.; Borne, F.; Bally, M.; Ball, G.; Patte, J. C. |
title |
A direct sulfhydrylation pathway is used for methionine biosynthesis in Pseudomonas aeruginosa |
journal |
Microbiology |
Activity |
o.succinylhomoserine.sulfhydrylase |
Family |
o.succinylhomoserine.sulfhydrylase |
sel |
selected |
ui |
7704274 |
year |
(1995) |
volume |
141 |
number |
Pt 2 |
pages |
431-9 |
| |
keywords |
Amino Acid Sequence |
abstract |
The relationship between genes and enzymes in the methionine biosynthetic pathway has been studied in Pseudomonas aeruginosa. The first step is catalysed by an O-succinylhomoserine synthase, the product of the metA gene mapped at 20 min on the chromosome. The second step is achieved by direct sulfhydrylation, involving the enzyme encoded by a metZ gene that we have identified and sequenced, located at 40 min. Thus Pseudomonas appears to be the only organism so far described that uses O-succinylhomoserine as substrate for a direct sulfhydrylation. As in yeast, the two transsulfuration pathways between cysteine and homocysteine, with cystathionine as an intermediate, probably exist in parallel in this organism. |
last changed |
2009/07/10 16:38 |
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