Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Reference

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Show additional data
do not include text mining results
include AMENDA results (Automatic Mining of Enzyme Data)
include FRENDA results (AMENDA + additional results, but less precise)

Search term:

Results 1 - 10 of 17 > >>
download as CSV
download all results as CSV
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9684159 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 16511076
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9685086 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 17760421
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9702035 Structural insights of the MenD from Escherichia coli reveal ThDP affinity Biochem. Biophys. Res. Commun. 380 797-801 2009 Escherichia coli K-12 19338755
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9705130 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 18983854
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9705201 MenD as a versatile catalyst for asymmetric synthesis J. Mol. Catal. B 61 56-66 2009 Escherichia coli K-12 -
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9718915 Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD Biochemistry 50 8712-8721 2011 Escherichia coli 21928762
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9718915 Using substrate analogues to probe the kinetic mechanism and active site of Escherichia coli MenD Biochemistry 50 8712-8721 2011 Mycobacterium tuberculosis 21928762
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9720243 Structure and reactivity of Bacillus subtilis MenD catalyzing the first committed step in menaquinone biosynthesis J. Mol. Biol. 401 253-264 2010 Bacillus subtilis 20600129
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9745170 A thiamine-dependent enzyme utilizes an active tetrahedral intermediate in vitamin K biosynthesis J. Am. Chem. Soc. 138 7244-7247 2016 Escherichia coli 27213829
Show all pathways known for 2.2.1.9Display the word mapDisplay the reaction diagram Show all sequences 2.2.1.9756007 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 30341164
Results 1 - 10 of 17 > >>
download as CSV
download all results as CSV