EC Number   |
General Information |
Reference |
|---|
    2.2.1.9 | evolution |
the enzyme Men D is not significantly different from other ThDP-dependent enzymes in active-site architecture, cofactor binding, or overall three-dimensional structure, suggesting the use of the canonical enamine intermediate in its catalysis |
745170 |
| 2.2.1.9 | metabolism |
MenD is a thiamine diphosphate-dependent enzyme that catalyzes a distinctive Stetterlike 1,4-addition reaction in bacterial biosynthesis of vitamin K2 |
745170 |
| 2.2.1.9 | metabolism |
the enzyme catalyzes an essential Stetter reaction in menaquinone (vitamin K2) biosynthesis via thiamine diphosphate (ThDP)-bound tetrahedral postdecarboxylation intermediates |
756007 |
| 2.2.1.9 | more |
in the covalent tetrahedral enamine intermediate, all of the bond lengths and angles of its planar thiazolium ring are comparable to those of a similar enzyme-free thiamine diphosphate adduct, complex crystal structure determination and analysis, NMR structure analysis and modeling, overview |
745170 |
| 2.2.1.9 | physiological function |
enzyme is essential for menaquinone biosynthesis |
718915 |
| 2.2.1.9 | physiological function |
first enzyme in biosynthesis of menaquinone or vitamin K2, influence on electron transport in bacteria |
705130 |
