The DAP pathway to lysine as a target for antimicrobial agents.
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For the record: The three-dimensional structure of the ternary complex ofCorynebacterium glutamicumdiaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelateMechanism of Substrate Recognition and Insight into Feedback Inhibition of Homocitrate Synthase from Thermus thermophilusL,L-Diaminopimelate Aminotransferase from Chlamydomonas reinhardtii: A Target for Algaecide DevelopmentSpecificity Determinants for Lysine Incorporation in Staphylococcus aureus Peptidoglycan as Revealed by the Structure of a MurE Enzyme Ternary ComplexBiochemical characterization of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate ligase (MurE) from Verrucomicrobium spinosum DSM 4136(T.)Metabolomics in premature labor: a novel approach to identify patients at risk for preterm delivery.Microarray analysis of toxicogenomic effects of ortho-phenylphenol in Staphylococcus aureus.Data Intensive Genome Level Analysis for Identifying Novel, Non-Toxic Drug Targets for Multi Drug Resistant Mycobacterium tuberculosisSynthesis and evaluation of conformationally restricted inhibitors of aspartate semialdehyde dehydrogenase.Design, synthesis, and conformational analysis of azacycloalkane amino acids as conformationally constrained probes for mimicry of peptide secondary structures.L,L-diaminopimelate aminotransferase (DapL): a putative target for the development of narrow-spectrum antibacterial compounds.Genomic and Biochemical Analysis of the Diaminopimelate and Lysine Biosynthesis Pathway in Verrucomicrobium spinosum: Identification and Partial Characterization of L,L-Diaminopimelate Aminotransferase and UDP-N-Acetylmuramoylalanyl-D-glutamyl-2,6-mCloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium Bartonella henselae strain Houston-1 at 2.1 Å resolution.Cytoplasmic steps of peptidoglycan biosynthesis.Structural basis for redox sensitivity in Corynebacterium glutamicum diaminopimelate epimerase: an enzyme involved in l-lysine biosynthesis.Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase.Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and Evolution.The lysine biosynthetic enzyme Lys4 influences iron metabolism, mitochondrial function and virulence in Cryptococcus neoformans.The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution.Synthesis of bis-α,α'-amino acids through diastereoselective bis-alkylations of chiral Ni(II)-complexes of glycine.Diaminopimelic acid (DAP) analogs bearing isoxazoline moiety as selective inhibitors against meso-diaminopimelate dehydrogenase (m-Ddh) from Porphyromonas gingivalis.Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly.
P2860
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P2860
The DAP pathway to lysine as a target for antimicrobial agents.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
The DAP pathway to lysine as a target for antimicrobial agents.
@en
type
label
The DAP pathway to lysine as a target for antimicrobial agents.
@en
prefLabel
The DAP pathway to lysine as a target for antimicrobial agents.
@en
P356
P1476
The DAP pathway to lysine as a target for antimicrobial agents.
@en
P2093
P356
10.1039/NP9961300029
P577
1996-02-01T00:00:00Z