2.2.1.9 745170 A thiamine-dependent enzyme utilizes an active tetrahedral intermediate in vitamin K biosynthesis J. Am. Chem. Soc. 138 7244-7247 2016 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27213829&form=6&db=m 2.2.1.9 757239 Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogen Mycobacterium tuberculosis J. Biol. Chem. 295 3759-3770 2020 Mycobacterium tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32029475&form=6&db=m 2.2.1.9 757239 Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogen Mycobacterium tuberculosis J. Biol. Chem. 295 3759-3770 2020 Mycobacterium tuberculosis H37Rv http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32029475&form=6&db=m 2.2.1.9 756458 Alteration of the route to menaquinone towards isochorismate-derived metabolites ChemBioChem 20 1672-1677 2019 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30866142&form=6&db=m 2.2.1.9 758338 Enhancing menaquinone-7 production in recombinant Bacillus amyloliquefaciens by metabolic pathway engineering RSC Adv. 7 28527-28534 2017 Bacillus amyloliquefaciens - 2.2.1.9 758338 Enhancing menaquinone-7 production in recombinant Bacillus amyloliquefaciens by metabolic pathway engineering RSC Adv. 7 28527-28534 2017 Bacillus amyloliquefaciens W-21 - 2.2.1.9 758483 Structural views along the Mycobacterium tuberculosis MenD reaction pathway illuminate key aspects of thiamin diphosphate-dependent enzyme mechanisms Structure 24 1167-1177 2016 Mycobacterium tuberculosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27291649&form=6&db=m 2.2.1.9 758483 Structural views along the Mycobacterium tuberculosis MenD reaction pathway illuminate key aspects of thiamin diphosphate-dependent enzyme mechanisms Structure 24 1167-1177 2016 Mycobacterium tuberculosis H37Rv http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27291649&form=6&db=m 2.2.1.9 756007 Two active site arginines are critical determinants of substrate binding and catalysis in MenD a thiamine-dependent enzyme in menaquinone biosynthesis Biochem. J. 475 3651-3667 2018 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30341164&form=6&db=m 2.2.1.9 684159 Crystallization and preliminary X-ray analysis of (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase (MenD) from Escherichia coli Acta Crystallogr. Sect. F 61 489-492 2005 Escherichia coli http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16511076&form=6&db=m