Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system

Benoît Desguin, Philippe Goffin, Eric Viaene, Michiel Kleerebezem, Vlad Martin-Diaconescu, Michael J. Maroney, Jean-Paul Declercq, Patrice Soumillion and Pascal Hols ()
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Benoît Desguin: Institute of Life Sciences, Université catholique de Louvain
Philippe Goffin: Institute of Life Sciences, Université catholique de Louvain
Eric Viaene: Institute of Life Sciences, Université catholique de Louvain
Michiel Kleerebezem: NIZO Food Research
Vlad Martin-Diaconescu: University of Massachusetts
Michael J. Maroney: University of Massachusetts
Jean-Paul Declercq: Institute of Life Sciences, Université catholique de Louvain
Patrice Soumillion: Institute of Life Sciences, Université catholique de Louvain
Pascal Hols: Institute of Life Sciences, Université catholique de Louvain

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract Racemases catalyse the inversion of stereochemistry in biological molecules, giving the organism the ability to use both isomers. Among them, lactate racemase remains unexplored due to its intrinsic instability and lack of molecular characterization. Here we determine the genetic basis of lactate racemization in Lactobacillus plantarum. We show that, unexpectedly, the racemase is a nickel-dependent enzyme with a novel α/β fold. In addition, we decipher the process leading to an active enzyme, which involves the activation of the apo-enzyme by a single nickel-containing maturation protein that requires preactivation by two other accessory proteins. Genomic investigations reveal the wide distribution of the lactate racemase system among prokaryotes, showing the high significance of both lactate enantiomers in carbon metabolism. The even broader distribution of the nickel-based maturation system suggests a function beyond activation of the lactate racemase and possibly linked with other undiscovered nickel-dependent enzymes.

Date: 2014
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DOI: 10.1038/ncomms4615

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