scholarly journals 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-meso-Diaminopimelate Ligase

2012 ◽  
Vol 3 ◽  
Author(s):  
Victoria R. Nachar ◽  
Francisco C. Savka ◽  
Sean E. McGroty ◽  
Katherine A. Donovan ◽  
Rachel A. North ◽  
...  
1992 ◽  
Vol 34 (6) ◽  
pp. 511-516 ◽  
Author(s):  
Júnia Soares Hamdan ◽  
Maria Aparecida de Resende ◽  
Sarah Piancastelli Franzot ◽  
Eduardo Osório Cisalpino

Yeast forms of five strains of Paracoccidioides brasiliensis (SN, 2, 18, 192 and JT- 1) were cultured in a synthetic medium for obtaining methylic antigens. These antigens were lyophilized and studied for each strain, to determine their partial biochemical composition, through measurements of total lipid, protein and carbohydrate contents. Lipids of methylic antigens were purified and analysed for sterols, phospholipids, glycolipids, li-poproteins, and partial characterization of sterols. Significant differences were found among antigenic preparations derived from distinct P. brasiliensis strains, in relation to the quantitative determinations. On the other hand, sterol analysis revealed the presence of ergosterol, lanosterol and squalene in all samples. The diversity verified in the biochemical characteristics of antigens derived from different P. brasiliensis strains, confirm the need of using a pool of fungal samples in order to produce antigen preparations for serological procedures without hampering their sensitivity.


2008 ◽  
Vol 190 (9) ◽  
pp. 3256-3263 ◽  
Author(s):  
André O. Hudson ◽  
Charles Gilvarg ◽  
Thomas Leustek

ABSTRACT A variant of the diaminopimelate (DAP)-lysine biosynthesis pathway uses an ll-DAP aminotransferase (DapL, EC 2.6.1.83) to catalyze the direct conversion of l-2,3,4,5-tetrahydrodipicolinate to ll-DAP. Comparative genomic analysis and experimental verification of DapL candidates revealed the existence of two diverged forms of DapL (DapL1 and DapL2). DapL orthologs were identified in eubacteria and archaea. In some species the corresponding dapL gene was found to lie in genomic contiguity with other dap genes, suggestive of a polycistronic structure. The DapL candidate enzymes were found to cluster into two classes sharing approximately 30% amino acid identity. The function of selected enzymes from each class was studied. Both classes were able to functionally complement Escherichia coli dapD and dapE mutants and to catalyze ll-DAP transamination, providing functional evidence for a role in DAP/lysine biosynthesis. In all cases the occurrence of dapL in a species correlated with the absence of genes for dapD and dapE representing the acyl DAP pathway variants, and only in a few cases was dapL coincident with ddh encoding meso-DAP dehydrogenase. The results indicate that the DapL pathway is restricted to specific lineages of eubacteria including the Cyanobacteria, Desulfuromonadales, Firmicutes, Bacteroidetes, Chlamydiae, Spirochaeta, and Chloroflexi and two archaeal groups, the Methanobacteriaceae and Archaeoglobaceae.


2010 ◽  
Vol 108 (10) ◽  
pp. 323-329 ◽  
Author(s):  
Marti F. A. Bierhuizen ◽  
Moniek de Wit ◽  
Carin A. R. L. Govers ◽  
Willem van Dijk

1966 ◽  
Vol 241 (7) ◽  
pp. 1530-1536
Author(s):  
Marcos Rojkind ◽  
Olga O. Blumenfeld ◽  
Paul M. Gallop

1980 ◽  
Vol 255 (11) ◽  
pp. 5468-5474 ◽  
Author(s):  
R.J. Kirschner ◽  
C.S. Federiuk ◽  
J.P. Ford ◽  
J.A. Shafer

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