Glutamine PRPP amidotransferase: snapshots of an enzyme in action
References (47)
- et al.
Regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase activity by end products
J Biol Chem
(1979) - et al.
Identification of sites for feedback regulation of glutamine 5-phosphoribosylpyrophosphate amidotransferase by nucleotides and relationship to residues important for catalysis
J Biol Chem
(1993) - et al.
Binding of purine nucleotides to two regulatory sites results in synergistic feedback inhibition of glutamine 5-phosphoribosylpyrophosphate amidotransferase
J Biol Chem
(1994) - et al.
Structure of the allosteric regulatory enzyme of purine biosynthesis
Science
(1994) - et al.
Synthesis of (+)-(1S)—1-pyrophosphoryl-(2R,3R)-2,3-dihydroxy-(4S)-4-phosphoryloxymethyl)cyclopentane, a stable, optically-active carbocyclic analog of 5-phosphoribosyl-1-pyrophosphate (PRPP)
Tetrahedron
(1997) - et al.
Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
J Biol Chem
(1996) - et al.
Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis
Biochemistry
(1998) - et al.
Exchange of K+ or CS+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase α2β2 complex
Biochemistry
(1996) - et al.
Glu-tRNAGin amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
Proc Natl Acad Sci USA
(1997) - et al.
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
Nat Struct Biol
(1996)
Penicillin acylase has a single-amino-acid catalytic centre
Nature
Three-dimensional structure of human lysosomal aspartylglucosaminidase
Nat Struct Biol
The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP
Cell
Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding
EMBO J
molscript: a program to produce both detailed and schematic plots of protein structures
J Appl Crystallogr
Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site
Biochemistry
A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
Nature
Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism
Crit Rev Biochem
Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase
Biochemistry
Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli: purification and properties
J Biol Chem
Mechanism of the synergistic endproduct regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides
Biochemistry
Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli
Protein Sci
5-Phosphorylribose 1-methylenebisphosphonate: properties of a substrate analog of 5-phosphorylribose 1-diphosphate
Bioorg Chem
Cited by (56)
The 3D Modules of Enzyme Catalysis: Deconstructing Active Sites into Distinct Functional Entities
2023, Journal of Molecular BiologyMicrobiota-Sourced Purines Support Wound Healing and Mucous Barrier Function
2020, iScienceCitation Excerpt :The purine ring is then sequentially built using small molecule donors, a process that consumes five ATP molecules to eventually form IMP (Figure S1). The preference for nucleotide genesis via the salvage pathway is likely the result of HGPRT having a higher specific activity than ATase, increased affinity for PRPP than ATase, and the allosteric inhibition of ATase by purine nucleotides produced by salvage (Natsumeda et al., 1984; Smith, 1998; Weber et al., 1983, 1987; Yamaoka et al., 1997). Indeed, purine salvage suppresses the de novo pathway (Yamaoka et al., 1997).
A New View into the Regulation of Purine Metabolism: The Purinosome
2017, Trends in Biochemical SciencesConformational changes involving ammonia tunnel formation and allosteric control in GMP synthetase
2014, Archives of Biochemistry and BiophysicsCitation Excerpt :With the Release model, the random loop was defined using density from the human isoform of GMPS, which crystallized in an open form, and since no intramolecular contacts were defined for the loop, the homodimer binding region appears slightly open and more solvent exposed than the Catalytic model. The Catalytic model for the closed form of GMPS reinforces the idea proposed earlier [64] regarding the apparent dichotomy in amidotransferase ammonia tunneling. The enzymes that generate a channel during each cycle with a conformational change require a lining of hydrophobic and nonpolar residues to minimize the presence of water in the ammonia tunnel, which could lead to inefficient hydrolysis of substrates.
Glutathione degradation by the alternative pathway (DUG pathway) in Saccharomyces cerevisiae is initiated by (Dug2p-Dug3p)2 complex, a novel glutamine amidotransferase (GATase) enzyme acting on glutathione
2012, Journal of Biological ChemistryCitation Excerpt :The GATaseII domain of different amidotransferases shares weak homology; for example, the GATaseII domain of glutamine phosphoribosyl amidotransferase of Bacillus subtilis and asparagine synthetase of E. coli share an identity of only 25% and a similarity of 41%. However, the residues important for catalysis and substrate binding as identified from the crystal structures of these enzymes are fully conserved among all the class II family members (26–31). Multiple sequence alignments revealed that these residues were also conserved in Dug3p (Fig. 2A) despite an otherwise weak similarity with known GATaseII domains.