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Int. J. Mol. Sci. 2014, 15(2), 3064-3087; doi:10.3390/ijms15023064
Review

Large-Scale Domain Motions and Pyridoxal-5'-Phosphate Assisted Radical Catalysis in Coenzyme B12-Dependent Aminomutases

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Received: 27 November 2013; in revised form: 25 December 2013 / Accepted: 22 January 2014 / Published: 20 February 2014
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Abstract: Lysine 5,6-aminomutase (5,6-LAM) and ornithine 4,5-aminomutase (4,5-OAM) are two of the rare enzymes that use assistance of two vitamins as cofactors. These enzymes employ radical generating capability of coenzyme B12 (5'-deoxyadenosylcobalamin, dAdoCbl) and ability of pyridoxal-5'-phosphate (PLP, vitamin B6) to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons. A large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form. In spite of all the similarities, these enzymes differ in substrate specificities. 4,5-OAM is highly specific for D-ornithine as a substrate while 5,6-LAM can accept D-lysine and L-β-lysine. This review focuses on recent computational, spectroscopic and structural studies of these enzymes and their implications on the related enzymes. Additionally, we also discuss the potential biosynthetic application of 5,6-LAM.
Keywords: coenzyme B12 (5'-deoxyadenosylcobalamin; dAdoCbl); pyridoxal-5'-phosphate (PLP; vitamin B6); lysine 5,6-aminomutase; ornithine 4,5-aminomutase; isotope-edited electron paramagnetic resonance (EPR) and electron-nuclear double resonance (ENDOR) spectroscopy; density functional theory (DFT) coenzyme B12 (5'-deoxyadenosylcobalamin; dAdoCbl); pyridoxal-5'-phosphate (PLP; vitamin B6); lysine 5,6-aminomutase; ornithine 4,5-aminomutase; isotope-edited electron paramagnetic resonance (EPR) and electron-nuclear double resonance (ENDOR) spectroscopy; density functional theory (DFT)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Maity, A.N.; Chen, Y.-H.; Ke, S.-C. Large-Scale Domain Motions and Pyridoxal-5'-Phosphate Assisted Radical Catalysis in Coenzyme B12-Dependent Aminomutases. Int. J. Mol. Sci. 2014, 15, 3064-3087.

AMA Style

Maity AN, Chen Y-H, Ke S-C. Large-Scale Domain Motions and Pyridoxal-5'-Phosphate Assisted Radical Catalysis in Coenzyme B12-Dependent Aminomutases. International Journal of Molecular Sciences. 2014; 15(2):3064-3087.

Chicago/Turabian Style

Maity, Amarendra N.; Chen, Yung-Han; Ke, Shyue-Chu. 2014. "Large-Scale Domain Motions and Pyridoxal-5'-Phosphate Assisted Radical Catalysis in Coenzyme B12-Dependent Aminomutases." Int. J. Mol. Sci. 15, no. 2: 3064-3087.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert