Journal article
Structure-function analyses of two plant mesodiaminopimelate decarboxylase isoforms reveal that active-site gating provides stereochemical control
JM Crowther, PJ Cross, MR Oliver, MM Leeman, AJ Bartl, AW Weatherhead, RA North, KA Donovan, MDW Griffin, H Suzuki, AO Hudson, M Kasanmascheff, RCJ Dobson
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2019
Abstract
meso-Diaminopimelate decarboxylase catalyzes the decarboxylation of meso-diaminopimelate, the final reaction in the diaminopimelate L-lysine biosynthetic pathway. It is the only known pyridoxal-5-phosphate-dependent decarboxylase that catalyzes the removal of a carboxyl group from a D-stereocenter. Currently, only prokaryotic orthologs have been kinetically and structurally characterized. Here, using complementation and kinetic analyses of enzymes recombinantly expressed in Escherichia coli, we have functionally tested two putative eukaryotic meso-diaminopimelate decarboxylase isoforms from the plant species Arabidopsis thaliana. We confirm they are both functional meso-diaminopimelate decar..
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Awarded by National Science Foundation
Funding Acknowledgements
[ "Recipient of an Australian Research Council Future Fellowship (Project no. FT140100544.", "Supported by National Science Foundation Grant MCB-1120541, National Institutes of Health Grant R15GM120653, and the College of Science and the Thomas H. Gosnell School of Life Sciences at the Rochester Institute of Technology. To whom correspondence may be addressed. Tel.: 585-475-4259; E-mail: aohsbi@rit.edu.", "Supported in part by the New Zealand Royal Society Marsden Fund (Contract UOC1506) and the United States Army Research Laboratory and Army Research Office under Contract/Grant W911NF-11-1-0481. To whom correspondence may be addressed. Tel.: 64-3-369-5145; E-mail:renwick.dobson@canterbury.ac.nz." ]