Disease relevance of dihydrodipicolinate

• 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 [1].
• Regulation of cephamycin C synthesis, aspartokinase, dihydrodipicolinic acid synthetase, and homoserine dehydrogenase by aspartic acid family amino acids in Streptomyces clavuligerus [2].
• Bacterial sporulation and regulation of dihydrodipicolinate synthase in ribonucleic acid polymerase mutants of Bacillus subtilis [3].
• A four- to sixfold increase in specific activity of dihydrodipicolinic acid synthase was observed during sporulation of Bacillus cereus [4].
• The dapB gene, which encodes L-2,3-dihydrodipicolinate reductase, the second enzyme of the lysine branch of the aspartic amino acid family, was cloned and sequenced from a tabtoxin-producing bacterium, Pseudomonas syringae pv. tabaci BR2.024 [5].

High impact information on dihydrodipicolinate

• Dihydrodipicolinate reductase (DHPR) catalyzes the reduced pyridine nucleotide-dependent reduction of the alpha,beta-unsaturated cyclic imine, dihydrodipicolinate, to generate tetrahydrodipicolinate [1].
• Dihydrodipicolinate synthase (DHDPS) catalyzes the formation of dihydrodipicolinate from pyruvate and L-aspartate beta-semialdehyde (ASA) [6].
• Dihydrodipicolinate reductase catalyzes the NAD(P)H-dependent reduction of the carbon-carbon double bond of the alpha,beta-unsaturated cyclic imine dihydrodipicolinate to form the cyclic imine tetrahydrodipicolinate [7].
• A possible binding site for dihydrodipicolinate has been identified in this second domain, about 12 A away from the dinucleotide binding site [8].
• The DapA gene encoding the lysine biosynthetic enzyme dihydrodipicolinate synthase from Coix lacryma-jobi: cloning, characterization, and expression analysis [9].

Chemical compound and disease context of dihydrodipicolinate

• The E. coli gene products synthesized were isoleucyl tRNA synthetase, ribosomal protein S20, dihydrodipicolinic acid reductase and (possibly) the two subunits carbamoyl-phosphate synthetase [10].
• Threonine production by dihydrodipicolinate synthase-defective mutants of Brevibacterium flavum [11].
• A dihydrodipicolinate reductase containing flavin was purified from sporulating Bacillus subtilis PCI 219 [12].
• Dihydrodipicolinate reductase in Bacillus subtilis PCI 219 had FMN as a prosthetic group, and the hydrogen transfer pathway is considered to be NADPH yields FMN yields dihydrodipicolinate [13].

Associations of dihydrodipicolinate with other chemical compounds

• The enzyme catalyses the condensation of (S)-aspartate semialdehyde (ASA) and pyruvate to form dihydrodipicolinate [14].

Gene context of dihydrodipicolinate

• For all seven protein systems considered (HIV-1 protease, dihydrodipicolinate reductase, Rnase T1, streptavidin, pp60c-Src SH2 domain, Hsp90 molecular chaperone, and bovine beta-trypsin) the binding enthalpy of 25 small molecular weight peptide and nonpeptide ligands can be accounted for with a standard error of +/-0.3 kcal x mol(-1) [15].
• The L-lysine biosynthetic pathway of the gram-negative obligate methylotroph Methylophilus methylotrophus AS1 was examined through characterization of the enzymes aspartokinase (AK), aspartsemialdehyde dehydrogenase, dihydrodipicolinate synthase (DDPS), dihydrodipicolinate reductase, and diaminopimelate decarboxylase [16].

References