Large-scale domain motions and pyridoxal-5'-phosphate assisted radical catalysis in coenzyme B12-dependent aminomutases

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'-phospha...

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Bibliographic Details
Published in:International journal of molecular sciences 2014-02, Vol.15 (2), p.3064-3087
Main Authors: Maity, Amarendra Nath, Chen, Yung-Han, Ke, Shyue-Chu
Format: Article
Language:English
Subjects:
Binding Sites
Biocatalysis
Catalysis
Cobamides - chemistry
Cobamides - metabolism
coenzyme B12 (5'-deoxyadenosylcobalamin
dAdoCbl
density functional theory (DFT)
Enzymes
Intramolecular Transferases - chemistry
Intramolecular Transferases - genetics
Intramolecular Transferases - metabolism
isotope-edited electron paramagnetic resonance (EPR) and electron-nuclear double resonance (ENDOR) spectroscopy
lysine 5,6-aminomutase
Molecular Docking Simulation
ornithine 4,5-aminomutase
Phosphates
Protein Structure, Tertiary
Pyridoxal Phosphate - chemistry
Pyridoxal Phosphate - metabolism
pyridoxal-5'-phosphate (PLP
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Review
vitamin B6
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Summary: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms15023064