|
type |
Journal Article |
authors |
Tsujimoto N, Gunji Y, Ogawa-Miyata Y, Shimaoka M, Yasueda H.
|
title |
L-Lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an L-lysine producer |
journal |
J Biotechnol |
Activity |
4.1.1.20 |
Family |
4.1.1.20 |
sel |
selected |
ui |
16483680 |
year |
(2006) |
volume |
124 |
number |
2 |
pages |
327-37 |
| |
abstract |
Previously, we showed that the enzymes aspartokinase (AK) and dihydrodipicolinate synthase (DDPS), which are involved in L-lysine biosynthesis in the Gram-negative obligate methylotroph Methylophilus methylotrophus AS1, were inhibited by allosteric effectors, including L-lysine. To elucidate further the regulation of L-lysine biosynthesis in M. methylotrophus, we cloned the genes encoding three other enzymes involved in this pathway, L-aspartate-beta-semialdehyde dehydrogenase, dihydrodipicolinate reductase (DDPR) and diaminopimelate decarboxylase, and examined their properties. DDPR was markedly inhibited by L-lysine. Based on this and our previous results, we constructed an L-lysine-producing strain of M. methylotrophus by introducing well-characterized genes encoding desensitized forms of AK and DDPS, as well as dapB (encoding DDPR) from Escherichia coli, using a broad host range plasmid. L-Lysine production was significantly increased by employing an S-(2-aminoethyl)-L-cysteine (L-lysine analog)-resistant mutant as the host. This derivative accumulated L-lysine at a concentration of 1 g l(-1) of medium using methanol as a carbon source. |
last changed |
2008/01/22 13:27 |
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