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Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and Evolution

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Macromolecular Protein Complexes

Part of the book series: Subcellular Biochemistry ((SCBI,volume 83))

Abstract

Enzymes are usually comprised of multiple subunits and more often than not they are made up of identical subunits. In this review we examine lysine biosynthesis and focus on the enzyme dihydrodipicolinate synthase in terms of its structure, function and the evolution of its varied number of subunits (quaternary structure). Dihydrodipicolinate synthase is the first committed step in the biosynthesis of lysine, which occurs naturally in plants, bacteria, archaea and fungi, but is not synthesized in mammals. In bacteria, there have been four separate pathways identified from tetrahydrodipicolinate to meso-diaminopimelate, which is the immediate precursor to lysine. Dihydrodipicolinate synthases from many bacterial and plant species have been structurally characterised and the results show considerable variability with respect to their quaternary structure, hinting at their evolution. The oligomeric state of the enzyme plays a key role, both in catalysis and in the allosteric regulation of the enzyme by lysine. While most bacteria and plants have tetrameric enzymes, where the structure of the dimeric building blocks is conserved, the arrangement of the dimers differs. We also review a key development in the field, namely the discovery of a human dihydrodipicolinate synthase-like enzyme, now known as 4-hydroxy-2-oxoglutarate aldolase . This discovery complicates the rationale underpinning drug development against bacterial dihydrodipicolinate synthases, since genetic errors in 4-hydroxy-2-oxoglutarate aldolase cause the disease Primary Hyperoxaluria Type 3 and therefore compounds that are geared towards the inhibition of bacterial dihydrodipicolinate synthase may be toxic to mammalian cells.

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Acknowledgments

AOH acknowledges the College of Science and the Thomas H. Gosnell School of Life Sciences at the Rochester Institute of Technology for ongoing support. RCJD acknowledges the following for funding support, in part: (1) the Ministry of Business, Innovation and Employment (contract UOCX1208); (2) the New Zealand Royal Society Marsden Fund (contract UOC1013) and (3) the US Army Research Laboratory and US Army Research Office under contract/grant number W911NF-11-1-0481.

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Authors and Affiliations

  1. Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch, 8041, New Zealand

    F. Grant Pearce & Renwick C. J. Dobson

  2. Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, Rochester, NY, USA

    André O. Hudson

  3. School of Biological Sciences & Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand

    Kerry Loomes

  4. Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, 30 Flemington Road, Parkville, VIC, 3010, Australia

    Renwick C. J. Dobson

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  1. F. Grant Pearce
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  4. Renwick C. J. Dobson
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Correspondence to Renwick C. J. Dobson .

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  1. Institute of Zoology, University of Mainz, Mainz, Germany

    J. Robin Harris

  2. School of Biology, Newcastle University, Newcastle upon Tyne, United Kingdom

    Jon Marles-Wright

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Grant Pearce, F., Hudson, A.O., Loomes, K., Dobson, R.C.J. (2017). Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and Evolution. In: Harris, J., Marles-Wright, J. (eds) Macromolecular Protein Complexes. Subcellular Biochemistry, vol 83. Springer, Cham. https://doi.org/10.1007/978-3-319-46503-6_10

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