Crystal structure of dihydrodipicolinate synthase from Mycobacterium tuberculosis in complex with pyruvate and insights into allosteric regulation (2025)
- Authors:
- USP affiliated authors: DIAS, MARCIO VINÍCIUS BERTACINE - ICB ; ROSA, LUÍS VICTOR SANTANA - ICB
- Unidade: ICB
- DOI: 10.1016/j.ijbiomac.2025.147950
- Subjects: MICROBIOLOGIA; TUBERCULOSE; MYCOBACTERIUM TUBERCULOSIS; CRISTALOGRAFIA DE RAIOS X; REGULAÇÃO ALOSTÉRICA; ENZIMAS HIDROLÍTICAS
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Título: International Journal of Biological Macromolecules
- ISSN: 1879-0003
- Volume/Número/Paginação/Ano: v. 330, art. 147950, 9 p., 2025
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
ROSA, Luís Victor Santana et al. Crystal structure of dihydrodipicolinate synthase from Mycobacterium tuberculosis in complex with pyruvate and insights into allosteric regulation. International Journal of Biological Macromolecules, v. 330, p. 9 , 2025Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2025.147950. Acesso em: 27 jan. 2026. -
APA
Rosa, L. V. S., Blaszczyk, B., Blundell, T. L., & Dias, M. V. B. (2025). Crystal structure of dihydrodipicolinate synthase from Mycobacterium tuberculosis in complex with pyruvate and insights into allosteric regulation. International Journal of Biological Macromolecules, 330, 9 . doi:10.1016/j.ijbiomac.2025.147950 -
NLM
Rosa LVS, Blaszczyk B, Blundell TL, Dias MVB. Crystal structure of dihydrodipicolinate synthase from Mycobacterium tuberculosis in complex with pyruvate and insights into allosteric regulation [Internet]. International Journal of Biological Macromolecules. 2025 ; 330 9 .[citado 2026 jan. 27 ] Available from: https://doi.org/10.1016/j.ijbiomac.2025.147950 -
Vancouver
Rosa LVS, Blaszczyk B, Blundell TL, Dias MVB. Crystal structure of dihydrodipicolinate synthase from Mycobacterium tuberculosis in complex with pyruvate and insights into allosteric regulation [Internet]. International Journal of Biological Macromolecules. 2025 ; 330 9 .[citado 2026 jan. 27 ] Available from: https://doi.org/10.1016/j.ijbiomac.2025.147950 - Fragment-Merging strategies with known pyrimidine scaffolds targeting dihydrofolate reductase from mycobacterium tuberculosis
- Mechanistic insights into dideoxygenation in gentamicin biosynthesis
- Abordagem estrutural sobre biossínteses, alvos, estratégias de desenvolvimento e resistência a antimicrobianos
- Cloning, expression, purification and biophysical analysis of two putative halogenases from the glycopeptide A47,934 gene cluster of Streptomyces toyocaensis
- Enzymology of pyran ring A formation in salinomycin biosynthesis
- Structural basis of the selectivity of GenN, an Aminoglycoside N-Methyltransferase involved in gentamicin biosynthesis
- Mycobacterial OtsA structures unveil substrate preference mechanism and allosteric regulation by 2-oxoglutarate and 2-phosphoglycerate
- The crystal structure of AjiA1 reveals a novel structural motion mechanism in the adenylate-forming enzyme family
- Structure of a soluble epoxide hydrolase identified in Trichoderma reesei
- Using a fragment-based approach to identify alternative chemical scaffolds targeting dihydrofolate reductase from Mycobacterium tuberculosis
Informações sobre o DOI: 10.1016/j.ijbiomac.2025.147950 (Fonte: oaDOI API)
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
