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

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
 
 
 
2D representation of the chemical structure of Q60998677.
(S)-pyroglutamic acid

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

  1. ↑ Baich A (December 1969). "Proline synthesis in Escherichia coli. A proline-inhibitable glutamic acid kinase". Biochimica et Biophysica Acta (BBA) - General Subjects. 192 (3): 462–7. doi:10.1016/0304-4165(69)90395-x. PMID 4904678.
  2. 1 2 Enzyme 2.7.2.11 at KEGG Pathway Database.


source: https://en.wikipedia.org/wiki/Glutamate_5-kinase