Skip to main content
. Author manuscript; available in PMC: 2012 Sep 23.
Published in final edited form as: J Mol Biol. 2011 Jul 22;412(3):412–422. doi: 10.1016/j.jmb.2011.07.034

TABLE 1. Amino acid differences between mitochondrial and cytoplasmic aspartate aminotransferase in the putative fatty acid binding region of chicken heart mAsp-AT.

Throughout the binding site region as a whole, there are 15 hydrophobic amino acids in mAsp-AT compared with 10 in cAsp-AT. In the helices defining the RIGHT and LEFT boundaries of the binding site cleft, the 7 amino acids depicted in bold italic type have a difference in hydrophobicity or charge in cAsp-AT compared to their mAsp-AT counterpart. In 5 of these 7 instances, the change resulted in a relative decrease in hydrophobicity in cAsp-AT compared with mAsp-AT.

mAsp-AT cAsp-AT

Pos. # AA Type AA Type Site
166 CYS H ARG B
178 SER P GLU A
180 ILE H ALA H
198 VAL H THR P Buried graphic file with name nihms-314379-t0008.jpg R
I
G
H
T
201 ARG B THR P Exposed
207 GLU A GLN P Exposed
212 VAL H MET H Buried
214 LYS B ARG B Exposed
216 ASN P PHE H Exposed
219 ALA H PRO H Buried
223 MET H SER P Buried
242 HIS B TYR P Exposed graphic file with name nihms-314379-t0009.jpg L
E
F
T
244 ILE H VAL H Buried
245 GLU A SER P Exposed
246 GLN P GLU A Exposed
248 ILE H PHE H Buried
250 VAL H LEU H Buried
252 LEU H CYS H
256 TYR H PHE H
257 ALA H SER P
260 MET H PHE H
264 GLY H ASN P
269 ALA H ASN P

Type: H = hydrophobic; P = uncharged polar; A = Acidic; B = basic