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- Fellner, Matthias; Rankin, Joel A.; Desguin, Benoît; Hu, Jian; Hausinger, Robert P.
- Biochemistry 2018 v.57 no.38 pp. 5513-5523
- Lactobacillus plantarum; Thermoanaerobacterium thermosaccharolyticum; active sites; adenosine triphosphate; apoproteins; biosynthesis; chemical bonding; coenzyme A; crystal structure; cysteine; lactic acid; models; sulfur; transferases
- ... LarE from Lactobacillus plantarum is an ATP-dependent sulfur transferase that sacrifices its Cys176 sulfur atom to form a dehydroalanine (Dha) side chain during biosynthesis of the covalently linked nickel-pincer nucleotide (NPN) cofactor (pyridinium 3-thioamide-5-thiocarboxylic acid mononucleotide) of lactate racemase. Coenzyme A (CoA) stabilizes LarE and forms a CoA-Cys176 mixed disulfide with t ...
- Rohde, Michael; Sippel, Daniel; Trncik, Christian; Andrade, Susana L. A.; Einsle, Oliver
- Biochemistry 2018 v.57 no.38 pp. 5497-5504
- active sites; catalytic activity; chemical bonding; hydrides; hydrogen; nitrogen; nitrogenase
- ... The reaction catalyzed by the nitrogenase enzyme involves breaking the stable triple bond of the dinitrogen molecule and is consequently considered among the most challenging reactions in biology. While many aspects regarding its atomic mechanism remain to be elucidated, a kinetic scheme established by David Lowe and Roger Thorneley has remained a gold standard for functional studies of the enzyme ...