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The coenzyme A disulphide reductase of Borrelia burgdorferi is important for rapid growth throughout the enzootic cycle and essential for infection of the mammalian host.
Eggers CH, Caimano MJ, Malizia RA, Kariu T, Cusack B, Desrosiers DC, Hazlett KR, Claiborne A, Pal U, Radolf JD. Eggers CH, et al. Among authors: claiborne a. Mol Microbiol. 2011 Nov;82(3):679-97. doi: 10.1111/j.1365-2958.2011.07845.x. Epub 2011 Oct 12. Mol Microbiol. 2011. PMID: 21923763 Free PMC article.
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity.
Wallen JR, Paige C, Mallett TC, Karplus PA, Claiborne A. Wallen JR, et al. Among authors: claiborne a. Biochemistry. 2008 May 6;47(18):5182-93. doi: 10.1021/bi8002204. Epub 2008 Apr 10. Biochemistry. 2008. PMID: 18399646 Free PMC article.
C., Leonardi, R., Jackowski, S., Mallett, T. C., and Claiborne, A. (2007) Biochemistry 46, 3234-3245], and we have now characterized the kinetic and redox properties of the B. anthracis coenzyme A-disulfide reductase (CoADR, BACoADR) and determined the crysta …
C., Leonardi, R., Jackowski, S., Mallett, T. C., and Claiborne, A. (2007) Biochemistry 46, 3234-3245], and we have now charact …
Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking.
Wallen JR, Mallett TC, Boles W, Parsonage D, Furdui CM, Karplus PA, Claiborne A. Wallen JR, et al. Among authors: claiborne a. Biochemistry. 2009 Oct 13;48(40):9650-67. doi: 10.1021/bi900887k. Biochemistry. 2009. PMID: 19725515 Free PMC article.
We have now determined the crystal structure at 2.10 A resolution for the Bacillus anthracis coenzyme A-disulfide reductase isoform (BaCoADR-RHD) containing a C-terminal RHD domain; this is the first structural representative of the multidomain proteins class …
We have now determined the crystal structure at 2.10 A resolution for the Bacillus anthracis coenzyme A-disulfide reductase is …
Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: implications for coenzyme A-dependent redox biology.
Nicely NI, Parsonage D, Paige C, Newton GL, Fahey RC, Leonardi R, Jackowski S, Mallett TC, Claiborne A. Nicely NI, et al. Among authors: claiborne a. Biochemistry. 2007 Mar 20;46(11):3234-45. doi: 10.1021/bi062299p. Epub 2007 Feb 27. Biochemistry. 2007. PMID: 17323930 Free PMC article.
Coenzyme A (CoASH) is the major low-molecular weight thiol in Staphylococcus aureus and a number of other bacteria; the crystal structure of the S. aureus coenzyme A-disulfide reductase (CoADR), which maintains the reduced intracellular state of CoASH, has re …
Coenzyme A (CoASH) is the major low-molecular weight thiol in Staphylococcus aureus and a number of other bacteria; the crysta …
122 results