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dapB  -  dihydrodipicolinate reductase

Mycobacterium tuberculosis CDC1551

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Disease relevance of dapB

  • The Mycobacterium tuberculosis dapB-encoded DHPR has been cloned, expressed, purified, and crystallized in two ternary complexes with NADH or NADPH and the inhibitor 2,6-pyridinedicarboxylate (2,6-PDC) [1].
  • Dihydrodipicolinate reductase from Mycobacterium tuberculosis (DapB, DHDPR, Rv2773c) has been cloned and heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in three different crystal forms [2].

High impact information on dapB


Associations of dapB with chemical compounds

  • The M. tuberculosis DHPR uses NADH and NADPH with nearly equal efficiency based on V/K values [1].


  1. The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity. Cirilli, M., Zheng, R., Scapin, G., Blanchard, J.S. Biochemistry (2003) [Pubmed]
  2. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis. Kefala, G., Janowski, R., Panjikar, S., Mueller-Dieckmann, C., Weiss, M.S. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2005) [Pubmed]
  3. Inhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis. Paiva, A.M., Vanderwall, D.E., Blanchard, J.S., Kozarich, J.W., Williamson, J.M., Kelly, T.M. Biochim. Biophys. Acta (2001) [Pubmed]
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