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Gene Review:

dapA - dihydrodipicolinate synthase

Escherichia coli CFT073

Tsujimoto, N. et al., Kefala, G. et al., Pearce, F.G. et al.

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Disease relevance of dapA

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 [1].
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 [1].
Dihydrodipicolinate synthase from Thermotoga maritima [2].
Dihydrodipicolinate synthase from Mycobacterium tuberculosis (DHDPS, DapA, Rv2753c) has been cloned, heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in a monoclinic crystal form [3].

Associations of dapA with chemical compounds

DHDPS (dihydrodipicolinate synthase) catalyses the branch point in lysine biosynthesis in bacteria and plants and is feedback inhibited by lysine [2].

References

L-Lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an L-lysine producer. Tsujimoto, N., Gunji, Y., Ogawa-Miyata, Y., Shimaoka, M., Yasueda, H. J. Biotechnol. (2006) [Pubmed]
Dihydrodipicolinate synthase from Thermotoga maritima. Pearce, F.G., Perugini, M.A., McKerchar, H.J., Gerrard, J.A. Biochem. J. (2006) [Pubmed]
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapA (Rv2753c) from Mycobacterium tuberculosis. Kefala, G., Weiss, M.S. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]

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