Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Maris V Fonseca"'
Autor:
Maris V Fonseca, Michele S Swanson
Publikováno v:
Frontiers in Cellular and Infection Microbiology, Vol 4 (2014)
The Gram-negative bacterium Legionella pneumophila is ubiquitous in freshwater environments as a free-swimming organism, resident of biofilms, or parasite of protozoa. If the bacterium is aerosolized and inhaled by a susceptible human host, it can in
Externí odkaz:
https://doaj.org/article/85ba59fc17304cb099980266088089a9
Publikováno v:
Infection and Immunity. 82:720-730
The phagosomal transporter (Pht) family of the major facilitator superfamily (MFS) is encoded by phylogenetically related intracellular gammaproteobacteria, including the opportunistic pathogen Legionella pneumophila . The location of the pht genes b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4681ea43beef8d64b327d2082665145
https://doi.org/10.1128/iai.01043-13
https://doi.org/10.1128/iai.01043-13
Autor:
Maris V. Fonseca, Jorge C. Escalante-Semerena, Nicole R. Buan, Ivan Rayment, Alexander R. Horswill
Publikováno v:
Journal of Biological Chemistry. 277:33127-33131
The specificity of the ATP:corrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica serovar Typhimurium LT2 for its nucleotide substrate was tested using ATP analogs and alternative nucleotide donors. The enzyme showed broad specificity for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dfb3b0efa58fa253399c89250e3a31e
https://doi.org/10.1074/jbc.m203893200
https://doi.org/10.1074/jbc.m203893200
Publikováno v:
Journal of Biological Chemistry. 276:32101-32108
Homogeneous ferredoxin (flavodoxin):NADP(+) reductase and flavodoxin A proteins served as electron donors for the reduction of co(III)rrinoids to co(I)rrinoids in vitro. The resulting co(I)rrinoids served as substrates for the ATP:co(I)rrinoid adenos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f2597eebda689b5e777c9bf26fb27d1
https://doi.org/10.1074/jbc.m102510200
https://doi.org/10.1074/jbc.m102510200
Publikováno v:
Journal of Bacteriology. 182:4304-4309
Reduction of the cobalt ion of cobalamin from the Co(III) to the Co(I) oxidation state is essential for the synthesis of adenosylcobalamin, the coenzymic form of this cofactor. A cob(II)alamin reductase activity in Salmonella enterica serovar Typhimu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36a85b9f7085a0930ece5ea2a020829b
https://doi.org/10.1128/jb.182.15.4304-4309.2000
https://doi.org/10.1128/jb.182.15.4304-4309.2000
Autor:
Cary B. Bauer, James B. Thoden, Thomas B. Thompson, Maris V. Fonseca, Ivan Rayment, Hazel M. Holden, Jorge C. Escalante-Semerena
Publikováno v:
Biochemistry. 40(2)
In Salmonella typhimurium, formation of the cobalt-carbon bond in the biosynthetic pathway for adenosylcobalamin is catalyzed by the product of the cobA gene which encodes a protein of 196 amino acid residues. This enzyme is an ATP:co(I)rrinoid adeno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64e478d89b2f2f7f4055bceb6eb49aeb
https://pubmed.ncbi.nlm.nih.gov/11148030
https://pubmed.ncbi.nlm.nih.gov/11148030