Literature summary for 4.3.1.18 extracted from

Tanaka, H.; Senda, M.; Venugopalan, N.; Yamamoto, A.; Senda, T.; Ishida, T.; Horiike, K.
Crystal structure of a zinc-dependent D-serine dehydratase from chicken kidney (2011), J. Biol. Chem., 286, 27548-27558.

Crystallization (Commentary)

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

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

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

Metals/Ions	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Gallus gallus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Gallus gallus

Renatured (Commentary)

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

Source Tissue	Comment	Organism	Textmining
kidney	-	Gallus gallus	-

Substrates and Products (Substrate)

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	-	?