| Types | DnaRegion
|
| Roles | CDS
Coding
|
| Sequences | BBa_I718004_sequence (Version 1)
|
Description
Dihydrodipicolinate synthase is the first enzyme unique to lysine biosynthesis, catalyzing the condensation of pyruvate and aspartate β-semialdehyde by a ping-pong mechanism. It also catalyzes the rate-limiting step in E.coli lysine biosynthesis after aspartate kinase III. The condensing enzyme-pyruvate complex, prior to reduction and hydrolysis, exists as the Schiff base formed between the carbonyl of pyruvate and an ε-amino group of a lysine residue on the enzyme. This property classifies the enzyme as a Class I aldolase with respect to carbon-carbon bond formation. The enzyme is inhibited by lysine, a feedback inhibitor. (source: Ecocyc)
Notes
none
Source
E. Coli MG1655
