CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1100
Functional Family L-serine dehydratase/L-threonine deaminase

Enzyme Information

4.3.1.17
L-serine ammonia-lyase.
based on mapping to UniProt P09367
L-serine = pyruvate + NH(3).
-!- The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13) followed by tautomerization to an imine form and hydrolysis of the C-N bond. -!- The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10. -!- This reaction is also carried out by EC 4.3.1.19 from a number of sources. -!- Formerly EC 4.2.1.13.
4.3.1.19
Threonine ammonia-lyase.
based on mapping to UniProt P09367
L-threonine = 2-oxobutanoate + NH(3).
-!- The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond. -!- The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10. -!- The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17. -!- Formerly EC 4.2.1.16.

UniProtKB Entries (1)

P09367
SDHL_RAT
Rattus norvegicus
L-serine dehydratase/L-threonine deaminase

PDB Structure

PDB 1PWE
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of serine dehydratase from rat liver.
Yamada, T., Komoto, J., Takata, Y., Ogawa, H., Pitot, H.C., Takusagawa, F.
Biochemistry