Structure–function analyses of two plant meso-diaminopimelate decarboxylase isoforms reveal that active-site gating provides stereochemical control

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....

Полное описание

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Библиографические подробности
Опубликовано в: :J Biol Chem
Главные авторы: Crowther, Jennifer M., Cross, Penelope J., Oliver, Michael R., Leeman, Mary M., Bartl, Austin J., Weatherhead, Anthony W., North, Rachel A., Donovan, Katherine A., Griffin, Michael D. W., Suzuki, Hironori, Hudson, André O., Kasanmascheff, Müge, Dobson, Renwick C. J.
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Biochemistry and Molecular Biology 2019
Предметы:
Enzymology
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC6544842/
https://ncbi.nlm.nih.gov/pubmed/30962284
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA118.006825
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