CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

4.3.1.19
Threonine ammonia-lyase.
based on mapping to UniProt Q96GA7
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.
4.3.1.17
L-serine ammonia-lyase.
based on mapping to UniProt Q96GA7
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.

UniProtKB Entries (1)

Q96GA7
SDSL_HUMAN
Homo sapiens
Serine dehydratase-like

PDB Structure

PDB 2RKB
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: Crystal structure and site-directed mutagenesis studies.
Yamada, T., Komoto, J., Kasuya, T., Takata, Y., Ogawa, H., Mori, H., Takusagawa, F.
Biochim.Biophys.Acta