4.1.1.20 Lung Diseases https://pubmed.ncbi.nlm.nih.gov/7847892/ Molecular genetics of Aspergillus pathogenicity. causal interaction 3 4.1.1.20 Lung Diseases https://pubmed.ncbi.nlm.nih.gov/7847892/ Molecular genetics of Aspergillus pathogenicity. unassigned - 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/12637582/ Crystal structure of Mycobacterium tuberculosis diaminopimelate decarboxylase, an essential enzyme in bacterial lysine biosynthesis. therapeutic application 1 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/16511157/ Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis. therapeutic application 1 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/25986217/ An optimized coupled assay for quantifying diaminopimelate decarboxylase activity. therapeutic application 2 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/26921318/ Dimerization of Bacterial Diaminopimelate Decarboxylase is Essential for Catalysis. therapeutic application 1 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/12637582/ Crystal structure of Mycobacterium tuberculosis diaminopimelate decarboxylase, an essential enzyme in bacterial lysine biosynthesis. ongoing research 1 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/13601806/ Inhibition of diaminopimelic acid decarboxylase activity in Mycobacterium tuberculosis by isonicotinic acid hydrazide. ongoing research 2 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/19543810/ The three-dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation. ongoing research 2 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/24820872/ Cell-specific labeling enzymes for analysis of cell-cell communication in continuous co-culture. ongoing research 1 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/25986217/ An optimized coupled assay for quantifying diaminopimelate decarboxylase activity. ongoing research 1 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/26921318/ Dimerization of Bacterial Diaminopimelate Decarboxylase is Essential for Catalysis. ongoing research 3 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/12637582/ Crystal structure of Mycobacterium tuberculosis diaminopimelate decarboxylase, an essential enzyme in bacterial lysine biosynthesis. unassigned - 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/13601806/ Inhibition of diaminopimelic acid decarboxylase activity in Mycobacterium tuberculosis by isonicotinic acid hydrazide. unassigned - 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/19543810/ The three-dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation. unassigned - 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/16511157/ Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis. unassigned - 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/24820872/ Cell-specific labeling enzymes for analysis of cell-cell communication in continuous co-culture. unassigned - 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/25986217/ An optimized coupled assay for quantifying diaminopimelate decarboxylase activity. unassigned - 4.1.1.20 Tuberculosis https://pubmed.ncbi.nlm.nih.gov/26921318/ Dimerization of Bacterial Diaminopimelate Decarboxylase is Essential for Catalysis. unassigned -