CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1100
Functional Family D-serine dehydratase

Enzyme Information

4.3.1.18
D-serine ammonia-lyase.
based on mapping to UniProt P00926
D-serine = pyruvate + NH(3).
-!- The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- Also acts, slowly, on D-threonine. -!- Formerly EC 4.2.1.14.

UniProtKB Entries (1)

P00926
SDHD_ECOLI
Escherichia coli K-12
D-serine dehydratase

PDB Structure

PDB 3SS7
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of D-serine dehydratase from Escherichia coli.
Urusova, D.V., Isupov, M.N., Antonyuk, S., Kachalova, G.S., Oblomova, G., Vagin, A.A., Lebedev, A.A., Bourenko, G.P., Dauter, Z., Bartunik, H.D., Lamzin, V.S., Melik-Adamyan, W.R., Mueller, T.D., Schnackerz, K.D.
Biochim.Biophys.Acta