Structural basis of the selectivity of GenN, an Aminoglycoside N-Methyltransferase involved in gentamicin biosynthesis (2017)
- Authors:
- Autor USP: DIAS, MARCIO VINÍCIUS BERTACINE - ICB
- Unidade: ICB
- DOI: 10.1021/acschembio.7b00466
- Subjects: MICROBIOLOGIA; AMINOGLICOSÍDEOS; CATALISADORES; ATIVAÇÃO ENZIMÁTICA; ANTIBIÓTICOS; MUTAGÊNESE
- Language: Inglês
- Imprenta:
- Publisher place: Washington
- Date published: 2017
- Source:
- Título do periódico: ACS Chemical Biology
- ISSN: 1554-8937
- Volume/Número/Paginação/Ano: v. 12, n. 11, p. 2779-2787, 2017
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
BURY, Priscila dos Santos et al. Structural basis of the selectivity of GenN, an Aminoglycoside N-Methyltransferase involved in gentamicin biosynthesis. ACS Chemical Biology, v. 12, n. 11, p. 2779-2787, 2017Tradução . . Disponível em: https://doi.org/10.1021/acschembio.7b00466. Acesso em: 24 abr. 2024. -
APA
Bury, P. dos S., Huang, F., Li, S., Sun, Y., Leadlay, P. F., & Dias, M. V. B. (2017). Structural basis of the selectivity of GenN, an Aminoglycoside N-Methyltransferase involved in gentamicin biosynthesis. ACS Chemical Biology, 12( 11), 2779-2787. doi:10.1021/acschembio.7b00466 -
NLM
Bury P dos S, Huang F, Li S, Sun Y, Leadlay PF, Dias MVB. Structural basis of the selectivity of GenN, an Aminoglycoside N-Methyltransferase involved in gentamicin biosynthesis [Internet]. ACS Chemical Biology. 2017 ; 12( 11): 2779-2787.[citado 2024 abr. 24 ] Available from: https://doi.org/10.1021/acschembio.7b00466 -
Vancouver
Bury P dos S, Huang F, Li S, Sun Y, Leadlay PF, Dias MVB. Structural basis of the selectivity of GenN, an Aminoglycoside N-Methyltransferase involved in gentamicin biosynthesis [Internet]. ACS Chemical Biology. 2017 ; 12( 11): 2779-2787.[citado 2024 abr. 24 ] Available from: https://doi.org/10.1021/acschembio.7b00466 - Abordagem estrutural sobre biossínteses, alvos, estratégias de desenvolvimento e resistência a antimicrobianos
- Mycobacterial OtsA structures unveil substrate preference mechanism and allosteric regulation by 2-oxoglutarate and 2-phosphoglycerate
- Enzymology of pyran ring A formation in salinomycin biosynthesis
- Mechanistic insights into dideoxygenation in gentamicin biosynthesis
- Cloning, expression, purification and biophysical analysis of two putative halogenases from the glycopeptide A47,934 gene cluster of Streptomyces toyocaensis
- Fragment-Merging strategies with known pyrimidine scaffolds targeting dihydrofolate reductase from mycobacterium tuberculosis
- Using a fragment-based approach to identify alternative chemical scaffolds targeting dihydrofolate reductase from Mycobacterium tuberculosis
- 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
- Mutations and insights into the molecular mechanisms of resistance of Mycobacterium tuberculosis to first-line
Informações sobre o DOI: 10.1021/acschembio.7b00466 (Fonte: oaDOI API)
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
