Crystallization (Comment) | Organism |
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molecular docking study on the orientations of substrates. Residue Arg301 has a dual function in a sequential reaction mechanism, i.e. substrate orientation in subsite 2 as well as stabilization of the transition state. With D-lactate a bifurcated H-bond from Arg301 to the R-OH of D-lactate may account for its orientation and nucleophile activation. This orientation is observed when the guanidino side chain of this residue is flexible. D-Ala adopts an orientation that utilizes H-bonding to water 2882 and the D-Ala phosphate in subsite 1. Both of these orientations provide mechanisms of deprotonation and place the nucleophile within 3.2 A of the electrophilic carbonyl of the D-Ala phosphate intermediate for formation of the transition state | Leuconostoc mesenteroides |
Organism | UniProt | Comment | Textmining |
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Leuconostoc mesenteroides | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 2 D-Ala | - |
Leuconostoc mesenteroides | ADP + phosphate + D-Ala-D-Ala | - |
? | |
ATP + D-Ala + D-lactate | - |
Leuconostoc mesenteroides | ADP + phosphate + D-Ala-D-lactate | depsipeptide D-Ala-D-lactate is responsible for the intrinsic resistance of Leuconostoc mesenteroides to vancomycin | ? |