CATH Classification

Domain Context

CATH Clusters

Superfamily Biosynthetic Threonine Deaminase; Domain 3
Functional Family L-threonine dehydratase

Enzyme Information

4.3.1.19
Threonine ammonia-lyase.
based on mapping to UniProt P04968
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)

P04968
ILVA_ECOLI
Escherichia coli K-12
L-threonine dehydratase biosynthetic IlvA

PDB Structure

PDB 1TDJ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase.
Gallagher, D.T., Gilliland, G.L., Xiao, G., Zondlo, J., Fisher, K.E., Chinchilla, D., Eisenstein, E.
Structure