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. 2010 Jan 21;5(1):e8826. doi: 10.1371/journal.pone.0008826

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Han et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A, Superposition of drDDC structure onto pig DDC structure shows that T82 of drDDC is a putative substrate binding residue. Residues from pig DDC are colored in cyan and those from drDDC are colored in magenta. B, Alignment of drDDC, pig DDC, Drosophila tyrosine decarboxylase-1 (drTDC-1) and Drosophila tyrosine decarboxylase-2 (drTDC-2). The corresponding residues of T82 and H192 are labeled. C, Superposition of drDDC structure onto pig DDC structure shows the H192 of drDDC is a putative substrate and cofactor binding residue. Residues from pig DDC are colored in cyan and those from drDDC are colored in magenta.