|
type |
Journal Article |
authors |
Inoue, H.; Inagaki, K.; Sugimoto, M.; Esaki, N.; Soda, K.; Tanaka, H. |
title |
Structural analysis of the L-methionine gamma-lyase gene from Pseudomonas putida |
journal |
J Biochem (Tokyo) |
Activity |
4.4.1.11 |
Family |
4.4.1.11 |
ui |
96172583 |
year |
(1995) |
volume |
117 |
number |
5 |
pages |
1120-5. |
| |
keywords |
Amino Acid Sequence |
abstract |
The gene encoding L-methionine gamma-lyase from Pseudomonas putida was cloned and the primary structure of the enzyme was deduced from its nucleotide sequence. The L-methionine gamma-lyase gene was expressed in Escherichia coli. The amino acid sequences of BrCN-digested peptides agreed with the corresponding parts of the L-methionine gamma-lyase sequence determined from the gene structure. The polypeptide is composed of 398 amino acid residues with a calculated molecular weight of 42,626, corresponding to the subunit of the homotetrameric enzyme. The deduced amino acid sequence of L-methionine gamma-lyase only showed extensive homology with other well known alpha,gamma-elimination and/or gamma-replacement pyridoxal 5'-phosphate-dependent enzymes, such as cystathionine gamma-lyase, cystathionine gamma-synthase, and O- acetylhomoserine O-acetylserine sulfhydrylase, that participate in the biosynthesis of sulfur amino acids. However, the deduced essential cysteine residue of L-methionine gamma-lyase was not conserved in these enzymes. We confirmed the presence of a part of an open reading frame in the 3'-flanking region of the L-methionine gamma-lyase gene, which showed high homology with the N-terminal region of pyruvate dehydrogenase (lipoamide) from E. coli, suggesting that it participates in the degradative pathway for L-methionine together with L-methionine gamma-lyase. |
last changed |
2008/06/09 17:52 |
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