Aspartate aminotransferase catalytic intermediates, models

Aspartate aminotransferase 57s, 135s, 753 absorption spectra 749 active site structure 744 atomic structure 750 catalytic intermediates, models 752 NMR spectra 149 quinonoid intermediate 750 Ramachandran plot 61 sequence 57 transamination 742 Aspartate ammonia-lyase 685 Aspartate carbamoyltransferase 348s active sites 348 regulation 540... 

Figure 14-10 Models of catalytic intermediates for aspartate aminotransferase in a half-transamination reaction from aspartate to oxalocetate. For clarity, only a selection of the active site groups are shown. (A) Michaelis complex of PLP enzyme with aspartate. (B) Geminal diamine. (C) Ketimine intermediate. The circle indicates a bound water molecule. See Jansonius and Vincent in Jurnak and McPherson.163 Courtesy of J.N. Jansonius.

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