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Glutamine PRPP amidotransferase: snapshots of an enzyme in action
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scholarly article
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title
Glutamine PRPP amidotransferase: snapshots of an enzyme in action
(English)
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author name string
J L Smith
series ordinal
1
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language of work or name
English
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publication date
December 1998
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published in
Current Opinion in Structural Biology
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volume
8
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issue
6
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page(s)
686-94
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cites work
Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site
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7 January 2021
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A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
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Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism
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7 January 2021
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Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase
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Structure of the allosteric regulatory enzyme of purine biosynthesis
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Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides
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7 January 2021
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Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli
1 reference
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reference URL
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7 January 2021
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Characterization and chemical properties of phosphoribosylamine, an unstable intermediate in the de novo purine biosynthetic pathway
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7 January 2021
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Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
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Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product
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Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis
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Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex
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Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes
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Carbamoyl phosphate synthetase: a tunnel runs through it
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Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
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Identification of active sites in amidase: evolutionary relationship between amide bond- and peptide bond-cleaving enzymes
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The MTCY428.08 gene of Mycobacterium tuberculosis codes for NAD+ synthetase.
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The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
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Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase
1 reference
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Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain
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1 reference
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Identifiers
DOI
10.1016/S0959-440X(98)80087-0
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Fatcat ID
release_7k2bvlm3s5hdxp3nnaxbdosh2i
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24 November 2022
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PubMed publication ID
9914248
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