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	
2.2.1.9	685086	Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity	Biochemistry	46	10979-10989	2007	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=17760421&form=6&db=m	
2.2.1.9	705201	MenD as a versatile catalyst for asymmetric synthesis	J. Mol. Catal. B	61	56-66	2009	Escherichia coli K-12	-	
2.2.1.9	705130	Specificity and reactivity in menaquinone biosynthesis: the structure of Escherichia coli MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase)	J. Mol. Biol.	384	1353-1368	2008	Escherichia coli K-12	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18983854&form=6&db=m	
2.2.1.9	702035	Structural insights of the MenD from Escherichia coli reveal ThDP affinity	Biochem. Biophys. Res. Commun.	380	797-801	2009	Escherichia coli K-12	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19338755&form=6&db=m	
2.2.1.9	720243	Structure and reactivity of Bacillus subtilis MenD catalyzing the first committed step in menaquinone biosynthesis	J. Mol. Biol.	401	253-264	2010	Bacillus subtilis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=20600129&form=6&db=m	
2.2.1.9	718915	Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD	Biochemistry	50	8712-8721	2011	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21928762&form=6&db=m	
2.2.1.9	718915	Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD	Biochemistry	50	8712-8721	2011	Mycobacterium tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21928762&form=6&db=m