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Biochemical characterization of AtuD from Pseudomonas aeruginosa, the first member of a new subgroup of acyl-CoA dehydrogenases with specificity for citronellyl-CoA, by K. Förster-Fromme, A. Chattopadhyay and D. Jendrossek

Microbiology vol. 154, part 3, pp. 789 - 796

Fig. S1. Multiple sequence alignment of AtuD, the PA1535 gene product and Megasphera elsdenii butyryl-CoA dehydrogenase. CLUSTALX was used for alignment. Identical and similar amino acids are shaded in black and grey, respectively. Conserved sequences around putative FAD-binding sites and active sites (Djordjevic et al., 1994; Dym & Eisenberg, 2001) are boxed and marked by #, respectively. [PDF] (34 kb)

REFERENCES
Djordjevic, S., Dong, Y., Paschke, R., Frerman, F. E., Strauss, A. W. & Kim, J. J. (1994). Identification of the catalytic base in long chain acyl-CoA dehydrogenase. Biochemistry 33, 4258-4264.
Dym, O. & Eisenberg, D. (2001). Sequence-structure analysis of FAD-containing proteins. Protein Sci 10, 1712-1728.

This Article Abstract Full Text Services Email this article to a friend Alert me to new issues of the journal Citing Articles Citing Articles via CrossRef