Structural highlights
Publication Abstract from PubMed
The structure of the title aminomutase was solved. The steric bulk of Phe 455 (green CPK structure) twists the phenylpropanoate ligand (green stick) by approximately 15 degrees about the C(beta) axis, which precludes a stronger bidentate salt bridge with Arg 323 (magenta structure). Instead, a weaker monodentate bridge may partially explain the different configuration of the product, relative to that obtained with an isoenzyme that forms a bidentate intermediate.
Insights into the Mechanistic Pathway of the Pantoea agglomerans Phenylalanine Aminomutase.,Strom S, Wanninayake U, Ratnayake ND, Walker KD, Geiger JH Angew Chem Int Ed Engl. 2012 Feb 8. doi: 10.1002/anie.201108525. PMID:22319000[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Strom S, Wanninayake U, Ratnayake ND, Walker KD, Geiger JH. Insights into the Mechanistic Pathway of the Pantoea agglomerans Phenylalanine Aminomutase. Angew Chem Int Ed Engl. 2012 Feb 8. doi: 10.1002/anie.201108525. PMID:22319000 doi:http://dx.doi.org/10.1002/anie.201108525
