Threonine ammonia-lyase

In enzymology, a threonine ammonia-lyase (EC number|4.3.1.19) is an enzyme that catalyzes the chemical reaction

:L-threonine $ightleftharpoons$ 2-oxobutanoate + NH₃

Hence, this enzyme has one substrate, L-threonine, and two products, 2-oxobutanoate and NH₃.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-threonine ammonia-lyase (2-oxobutanoate-forming). Other names in common use include threonine deaminase, L-serine dehydratase, serine deaminase, L-threonine dehydratase, threonine dehydrase, L-threonine deaminase, threonine dehydratase, L-threonine hydro-lyase (deaminating), and L-threonine ammonia-lyase. This enzyme participates in glycine, serine and threonine metabolism and valine, leucine and isoleucine biosynthesis. It employs one cofactor, pyridoxal phosphate.

tructural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1VE5, PDB link|2GN0, PDB link|2GN1, and PDB link|2GN2.

References

*
*
*
*

External links

Gene Ontology (GO) codes