Crystallization (Comment) | Organism |
---|---|
to 1.9 A resolution. In the active site pocket, a zinc ion that coordinates His347 and Cys349 is located near the PLP-Lys45 Schiff base. A theoretical model of the enzyme-D-serine complex suggests that the hydroxyl group of D-serine directly coordinates the zinc ion, and that the epsilon-NH2 group of Lys45 is a short distance from the substrate C-atom. The alpha-proton abstraction from D-serine by Lys45 and the elimination of the hydroxyl group seem to occur with the assistance of the zinc ion, resulting in the strict reaction specificity | Gallus gallus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | the enzyme activity on D-serine decreases 20fold by EDTA treatment and recovers nearly completely by the addition of Zn2+ | Gallus gallus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | the addition of Mn2+ induces a maximal recovery of 20% of the original activity in the EDTA-treated enzyme | Gallus gallus | |
additional information | no activation of the EDTA-treated enzyme is obtained after the addition of other divalent cations such as Mg2+, Ca2+, Cu2+ and Ni2+ | Gallus gallus | |
Zn2+ | the enzyme activity on D-serine decreases 20fold by EDTA treatment and recovers nearly completely by the addition of Zn2+. The hydroxyl group of D-serine directly coordinates the zinc ion, and the epsilon-NH2 group of Lys45 is a short distance from the substrate C-atom. The alpha-proton abstraction from D-serine by Lys45 and the elimination of the hydroxyl group seem to occur with the assistance of the zinc ion, resulting in the strict reaction specificity | Gallus gallus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Gallus gallus |
Renatured (Comment) | Organism |
---|---|
the enzyme activity on D-serine decreases 20fold by EDTA treatment and recovers nearly completely by the addition of Zn2+ | Gallus gallus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | - |
Gallus gallus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-serine | none of the reaction products that would be expected from side reactions of the PLP-D-serine Schiff base are detected during the more than 6000 catalytic cycles of dehydration, indicating high reaction specificity. Neither transamination product 3-hydroxypyruvate, retro-aldol cleavage product glycine, decarboxylation product 2-aminoethanol, or racemization product L-serine are detected | Gallus gallus | pyruvate + NH3 | - |
? |