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{{enzyme
| Name = glutamate 5-kinase
| EC_number = 2.7.2.11
| CAS_number = 54596-30-4
| IUBMB_EC_number = 2/7/2/11
| GO_code = 0004349
| image =
| width =
| caption =
}}
In [[enzymology]], a '''glutamate 5-kinase''' ({{EC number|2.7.2.11}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:ATP + L-glutamate <math>\rightleftharpoons</math> ADP + L-glutamate 5-phosphate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[L-glutamate]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[L-glutamate 5-phosphate]].

This enzyme belongs to the family of [[transferase]]s, specifically those transferring phosphorus-containing groups ([[phosphotransferase]]s) 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'''. This enzyme participates in [[urea cycle and metabolism of amino groups]].

==Structural studies==

As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|2AKO}}, {{PDB link|2J5T}}, and {{PDB link|2J5V}}.

==References==
{{reflist|1}}
* {{cite journal | author = Baich A | year = 1969 | title = Proline synthesis in Escherichia coli. A proline-inhibitable glutamic acid kinase | journal = Biochim. Biophys. Acta. | volume = 192 | pages = 462–7 | pmid = 4904678 | issue = 3 }}

[[Category:EC 2.7.2]]
[[Category:Enzymes of known structure]]

{{enzyme-stub}}

Gluconokinase - Revision history

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