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

• Dihydrodipicolinate reductase (DHPR) catalyzes the reduced pyridine nucleotide-dependent reduction of the alpha,beta-unsaturated cyclic imine, dihydrodipicolinate, to generate tetrahydrodipicolinate [1].
• Specifically, dihydrodipicolinate reductase, the essential gene product of dapB, was screened for novel inhibitors [3].
• Inhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis [3].

Associations of dapB with chemical compounds

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

References