Wikiwand AI

Glutamate 5-kinase

Enzyme From Wikipedia, the free encyclopedia

Glutamate 5-kinase (EC 2.7.2.11) is an enzyme that catalyzes the chemical reaction

 
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
ATP
ADP
 
2D representation of the chemical structure of Q27102623.
L-γ-glutamyl phosphate

The enzyme characterised from Escherichia coli, converts L-glutamic acid, to L-γ-glutamyl phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of the biosynthesis of the amino acid, proline.[1]

The product can spontaneously cyclise to (S)-pyroglutamic acid by loss of the phosphate group (Pi):[2]

L-γ-glutamyl phosphate
 
 
 
Rightward reaction arrow with minor product(s) to top right
 
 
 

This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:L-glutamate 5-phosphotransferase. Other names in common use include ATP-L-glutamate 5-phosphotransferase, ATP:gamma-L-glutamate phosphotransferase, gamma-glutamate kinase, gamma-glutamyl kinase, and glutamate kinase.[2]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 2AKO, PDB: 2J5T, and PDB: 2J5V.

References

Related Articles

Timelines

Top Qs

Fact Checks