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Chemical Compound Review:

L-glutamyl-5-P (2S)-2-amino-5-oxo-5- phosphonooxy...

Synonyms: AG-K-65901, CHEBI:17798, HMDB01228, AC1L4WCB, CTK4B7976, ...

Liaw, S.H. et al., Clark, D.D. et al., Hu, C.A. et al., Terao, Y. et al., Wedler, F.C. et al., et al.

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Disease relevance of L-gamma-glutamyl phosphate

Use of the sodium borohydride reduction technique to identify a gamma-glutamyl phosphate intermediary in the Escherichia coli glutamine synthetase reaction [1].
IS1230C was located next to attB, the bacteriophage P22 attachment site, and proB, encoding gamma-glutamyl phosphate reductase [2].

High impact information on L-gamma-glutamyl phosphate

To confirm the identity of the putative P5CS cDNAs, we expressed both human forms in gamma-glutamyl kinase- and gamma-glutamyl phosphate reductase-deficient strains of Saccharomyces cerevisiae and showed that they conferred the proline prototrophy [3].
The reactions catalyzed by gamma-glutamylcysteine synthetase and glutamine synthetase are thought to proceed via enzyme-bound gamma-glutamyl phosphate intermediates [4].
Interestingly, this mutation enhanced the activities of gamma-glutamyl kinase and gamma-glutamyl phosphate reductase, both of which catalyze the first two steps of L-proline synthesis and which together may form a complex in vivo [5].
This observation supports a two-step mechanism with ordered substrate binding: ATP first binds to GS, then Glu binds and attacks ATP to form gamma-glutamyl phosphate and ADP, which complete the ammonium binding site [6].
(5) Because the products (Glu or Gln) of the reactions catalyzed by GS are determined by the molecule (water or ammonium) attacking the intermediate gamma-glutamyl phosphate, this negatively charged ammonium binding pocket has been designed naturally for high affinity of ammonium to GS, permitting glutamine synthesis to proceed in aqueous solution [6].

Chemical compound and disease context of L-gamma-glutamyl phosphate

Interaction of a new gamma-glutamyl-phosphate analog, 4-(phosphonoacetyl)-L-alpha-aminobutyrate, with glutamine synthetase enzymes from Escherichia coli, plant, and mammalian sources [7].

Gene context of L-gamma-glutamyl phosphate

Strong homology is also found at the N-terminus to bacterial and yeast gamma-glutamyl kinase and at the C-terminus to bacterial gamma-glutamyl phosphate reductase [8].
Isotope-exchange enhancement studies, a variation on positional isotope-exchange enhancement as described by Raushel and Garrard [Raushel, F. M., & Garrard, L. J. (1984) Biochemistry 23, 1791-1795], are used to establish the point in the biosynthetic reaction of Escherichia coli glutamine synthetase at which gamma-glutamyl phosphate is formed [9].

References

Use of the sodium borohydride reduction technique to identify a gamma-glutamyl phosphate intermediary in the Escherichia coli glutamine synthetase reaction. Todhunter, J.A., Purich, D.L. J. Biol. Chem. (1975) [Pubmed]
Sequence analysis and distribution in Salmonella enterica serovars of IS3-like elements. Collighan, R.J., Walker, S.L., Woodward, M.J. Int. J. Med. Microbiol. (2000) [Pubmed]
Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. Hu, C.A., Lin, W.W., Obie, C., Valle, D. J. Biol. Chem. (1999) [Pubmed]
Inactivation of gamma-glutamylcysteine synthetase, but not of glutamine synthetase, by S-sulfocysteine and S-sulfohomocysteine. Moore, W., Wiener, H.L., Meister, A. J. Biol. Chem. (1987) [Pubmed]
Gene dosage effect of L-proline biosynthetic enzymes on L-proline accumulation and freeze tolerance in Saccharomyces cerevisiae. Terao, Y., Nakamori, S., Takagi, H. Appl. Environ. Microbiol. (2003) [Pubmed]
Discovery of the ammonium substrate site on glutamine synthetase, a third cation binding site. Liaw, S.H., Kuo, I., Eisenberg, D. Protein Sci. (1995) [Pubmed]
Interaction of a new gamma-glutamyl-phosphate analog, 4-(phosphonoacetyl)-L-alpha-aminobutyrate, with glutamine synthetase enzymes from Escherichia coli, plant, and mammalian sources. Wedler, F.C., Horn, B.R., Roby, W.G. Arch. Biochem. Biophys. (1980) [Pubmed]
Isolation, characterization, and chromosomal location of a gene encoding the delta 1-pyrroline-5-carboxylate synthetase in Arabidopsis thaliana. Savouré, A., Jaoua, S., Hua, X.J., Ardiles, W., Van Montagu, M., Verbruggen, N. FEBS Lett. (1995) [Pubmed]
Isotope-exchange enhancement studies of Escherichia coli glutamine synthetase. Clark, D.D., Villafranca, J.J. Biochemistry (1985) [Pubmed]

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