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Fig. 1 | BMC Biochemistry

Fig. 1

From: Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa

Fig. 1

a Multiple Sequence Alignment of PA0321, PA1409 and PA3774 from P. aeruginosa, acetylpolyamine amidohydrolase APAH from M. ramosa, histone deacetylase like amidohydrolase HDAH from Bordetella sp. and human HDAC6 (second deacetylase domain). The red triangles mark the amino acids that complex the catalytic Zn2+-ion and the magenta triangles the amino acids involved in the catalytic mechanism. The bars in light gray denote amino acids lining the binding pocket. b Average distance tree calculated from MSA in A) using the BLOSUM62 similarity matrix. c Percent identity matrix calculated using ClustalW2. Similarities between sequences are colored from non-identical high (green) to low (red)

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