If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-glutamine Degradation|
Wild-type E. coli K-12 grows only poorly on glutamine as the sole source of carbon, although mutants that gain the ability to utilize glutamine can be isolated easily [Masters81]. In contrast, glutamine supports rapid growth as the sole source of nitrogen, although growth is biphasic with a transition in mid-log phase [Atkinson02a]. No mutants unable to utilize glutamine as the sole source of nitrogen have been identified.
Two enzymes able to degrade glutamine, glutaminase and glutaminase B, were purified from E. coli B; no mutants were identified at the time, and thus the identity of the genes encoding them has not been established. Recently, two genes encoding glutaminases with properties resembling those of glutaminase A and B have been identified in E. coli K-12 [Brown08].
Review: Reitzer, L., Catabolism of Amino Acids and Related Compounds, Module 3.4.7 [ECOSAL]
Atkinson02a: Atkinson MR, Blauwkamp TA, Bondarenko V, Studitsky V, Ninfa AJ (2002). "Activation of the glnA, glnK, and nac promoters as Escherichia coli undergoes the transition from nitrogen excess growth to nitrogen starvation." J Bacteriol 184(19);5358-63. PMID: 12218022
Brown08: Brown G, Singer A, Proudfoot M, Skarina T, Kim Y, Chang C, Dementieva I, Kuznetsova E, Gonzalez CF, Joachimiak A, Savchenko A, Yakunin AF (2008). "Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis." Biochemistry 47(21);5724-35. PMID: 18459799
Abbott06: Abbott JL, Newell JM, Lightcap CM, Olanich ME, Loughlin DT, Weller MA, Lam G, Pollack S, Patton WA (2006). "The Effects of Removing the GAT Domain from E. coli GMP Synthetase." Protein J 25;483-491. PMID: 17103135
Anderson83: Anderson PM (1983). "CTP synthetase from Escherichia coli: an improved purification procedure and characterization of hysteretic and enzyme concentration effects on kinetic properties." Biochemistry 22(13);3285-92. PMID: 6349684
Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699
Bearne01: Bearne SL, Hekmat O, Macdonnell JE (2001). "Inhibition of Escherichia coli CTP synthase by glutamate gamma-semialdehyde and the role of the allosteric effector GTP in glutamine hydrolysis." Biochem J 356(Pt 1);223-32. PMID: 11336655
Boehlein94: Boehlein SK, Richards NG, Schuster SM (1994). "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad." J Biol Chem 269(10);7450-7. PMID: 7907328
Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043
Cedar69: Cedar H, Schwartz JH (1969). "The asparagine synthetase of Escherhic coli. I. Biosynthetic role of the enzyme, purification, and characterization of the reaction products." J Biol Chem 1969;244(15);4112-21. PMID: 4895361
Delannay99: Delannay S, Charlier D, Tricot C, Villeret V, Pierard A, Stalon V (1999). "Serine 948 and threonine 1042 are crucial residues for allosteric regulation of Escherichia coli carbamoylphosphate synthetase and illustrate coupling effects of activation and inhibition pathways." J Mol Biol 286(4);1217-28. PMID: 10047492
Deras99: Deras ML, Chittur SV, Davisson VJ (1999). "N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of Escherichia coli guanosine monophosphate synthetase." Biochemistry 38(1);303-10. PMID: 9890911
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Endrizzi04: Endrizzi JA, Kim H, Anderson PM, Baldwin EP (2004). "Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets." Biochemistry 43(21);6447-63. PMID: 15157079
Endrizzi05: Endrizzi JA, Kim H, Anderson PM, Baldwin EP (2005). "Mechanisms of product feedback regulation and drug resistance in cytidine triphosphate synthetases from the structure of a CTP-inhibited complex." Biochemistry 44(41);13491-9. PMID: 16216072
Fan09: Fan Y, Lund L, Shao Q, Gao YQ, Raushel FM (2009). "A combined theoretical and experimental study of the ammonia tunnel in carbamoyl phosphate synthetase." J Am Chem Soc 131(29);10211-9. PMID: 19569682
Fresquet00: Fresquet V, Mora P, Rochera L, Ramon-Maiques S, Rubio V, Cervera J (2000). "Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals." J Mol Biol 299(4);979-91. PMID: 10843852
Showing only 20 references. To show more, press the button "Show all references".
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493