Glutamine PRPP amidotransferase: snapshots of an enzyme in action (Q28294777)

Current Opinion in Structural Biology

Europe PubMed Central

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

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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

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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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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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Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli

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Characterization and chemical properties of phosphoribosylamine, an unstable intermediate in the de novo purine biosynthetic pathway

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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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Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation

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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

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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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Penicillin acylase has a single-amino-acid catalytic centre

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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

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A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase

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Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop

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Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding.

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Identifiers

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Fatcat ID

release_7k2bvlm3s5hdxp3nnaxbdosh2i

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Fatcat

https://api.fatcat.wiki/v0/release/7k2bvlm3s5hdxp3nnaxbdosh2i

24 November 2022