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Gene Review:

proB - gamma-glutamyl kinase

Escherichia coli UTI89

Marco-Marín, C. et al., Lee, Y.J. et al., Pérez-Arellano, I. et al., Pérez-Arellano, I. et al.

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Disease relevance of proB

E. coli G5K presents a novel tetrameric (dimer of dimers) architecture [1].

High impact information on proB

Glutamate 5-kinase (G5K) makes the highly unstable product glutamyl 5-phosphate (G5P) in the initial, controlling step of proline/ornithine synthesis, being feedback-inhibited by proline or ornithine, and causing, when defective, clinical hyperammonaemia [1].
A Novel Two-domain Architecture Within the Amino Acid Kinase Enzyme Family Revealed by the Crystal Structure of Escherichia coli Glutamate 5-kinase [1].
Microbial G5K generally consists of one amino acid kinase (AAK) and one PUA (named after pseudo uridine synthases and archaeosine-specific transglycosylases) domain [2].
When speF (which encodes ornithine decarboxylase) and proB (which encodes gamma-glutamyl kinase) were inactivated to prevent the conversion of L: -ornithine to putrescine and to block the biosynthesis of a side branch of L: -ornithine, respectively, L: -ornithine production was further enhanced approxi [3].

Chemical compound and disease context of proB

We determined two crystal structures of G5K from Escherichia coli, at 2.9 A and 2.5 A resolution, complexed with glutamate and sulphate, or with G5P, sulphate and the proline analogue 5-oxoproline [1].

Associations of proB with chemical compounds

Glutamate-5-kinase (G5K) catalyzes the first step of proline (and, in mammals, ornithine) biosynthesis [4].

Analytical, diagnostic and therapeutic context of proB

Dissection of Escherichia coli glutamate 5-kinase: functional impact of the deletion of the PUA domain [2].
Glutamate-5-kinase from Escherichia coli: gene cloning, overexpression, purification and crystallization of the recombinant enzyme and preliminary X-ray studies [4].

References

A Novel Two-domain Architecture Within the Amino Acid Kinase Enzyme Family Revealed by the Crystal Structure of Escherichia coli Glutamate 5-kinase. Marco-Marín, C., Gil-Ortiz, F., Pérez-Arellano, I., Cervera, J., Fita, I., Rubio, V. J. Mol. Biol. (2007) [Pubmed]
Dissection of Escherichia coli glutamate 5-kinase: functional impact of the deletion of the PUA domain. Pérez-Arellano, I., Rubio, V., Cervera, J. FEBS Lett. (2005) [Pubmed]
Genetic manipulation of a primary metabolic pathway for L: -ornithine production in Escherichia coli. Lee, Y.J., Cho, J.Y. Biotechnol. Lett. (2006) [Pubmed]
Glutamate-5-kinase from Escherichia coli: gene cloning, overexpression, purification and crystallization of the recombinant enzyme and preliminary X-ray studies. Pérez-Arellano, I., Gil-Ortiz, F., Cervera, J., Rubio, V. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]

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