Enzymes of nucleotide synthesis
References (37)
- et al.
Crystal structure of adenylosuccinate synthetase from Escherichia coli
J Biol Chem
(1993) Aspartate transcarbamylase from Escherichia coli: activity and regulation
Adv Enzymol Relat Areas Mol Biol
(1994)- et al.
The α/β hydrolase fold
Protein Eng
(1992) - et al.
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
Science
(1995) - et al.
A protein catalytic framework with an N-terminal nucleophile and capable of self-activation
Nature
(1995) The amidotransferases
Adv Enzymol Relat Areas Mol Biol
(1993)- et al.
Three-dimensional structure of the free radical protein of ribonucleotide reductase
Nature
(1990) - et al.
Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase
Proc Natl Acad Sci USA
(1992) - et al.
Refined crystal structure of unligated adenylosuccinate synthetase from Escherichia coli
J Mol Biol
(1995) - et al.
Stereochemical mechanism of action for thymidylate synthase based on the x-ray structure of the covalent inhibitory ternary complex with 5-fluoro-2'-deoxyuridylate and 5,10-methylenetetrahydrofolate
J Mol Biol
(1990)
Relation between structure and function of α/β proteins
Q Rev Biophys
Structure of the allosteric regulatory enzyme of purine biosynthesis
Science
Towards structure-based drug design: crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 Å resolution
J Mol Biol
The crystal structure of GMP synthetase: a paradigm for two enzyme families and a novel catalytic triad
Nature Struct Biol
Crystal structure of orotate phosphoribosyltransferase
Biochemistry
Structure of ribonucleotide reductase protein R1
Nature
Structure of and kinetic channelling in bifunctional dihydrofolate reductase—thymidylate synthase
Nature Struct Biol
Crystal structure of thymidylate synthase from T4 phage: component of a deoxynucleoside triphosphate—synthesizing complex
Biochemistry
Cited by (33)
Enzyme-driven oxygen-fuelled pathway selectivity of tyrosine-containing peptide oxidation evolution
2022, Chemical Engineering JournalCitation Excerpt :Enzymatic oxidation reactions happen in living systems all time [1–4]. Many significant living processes such as ATP production [5], nucleotides synthesis [6] and post-translational modification [7], signal transduction [8], substances exchange and functional metabolic compounds biosynthesis [9,10] can be achieved relying on the orderly progression on enzymatic cascade reactions [11,12]. As typical enzymatic oxidation reactions, the pigmentation plays an important role in living organisms [13–16].
Comprehensive genomic identification and expression analysis of the nucleobase-ascorbate transporter (NAT) gene family in apple
2016, Scientia HorticulturaeCitation Excerpt :However, AsA is not a likely substrate for those proteins (Niopek-Witz et al., 2014). Nucleobases have crucial functions in the metabolism of DNA and RNA (Senecoff et al., 1996; Smith, 1995), and are direct precursors for the synthesis of essential cofactors (e.g., flavine coenzymes, nicotinamide, and coenzyme A), vitamins (e.g., thiamine), and signaling molecules (cAMP). They are also essential constituents of cytokinins and precursors of purine alkaloids (D’Agostino and Kieber, 1999).
Phosphoribosyltransferase Mechanisms and Roles in Nucleic Acid Metabolism
2004, Progress in Nucleic Acid Research and Molecular BiologyCitation Excerpt :The enzyme nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase uses β-nicotinate mononucleotide as a ribose 5-phosphate donor in the formation of the vitamin B12 precursor α-5,6-dimethylbenzimidazolyl ribose 5-phosphate (65). The fundamental structures of Type 1 phosphoribosyltransferases have been reviewed by Smith (2, 4), and we concentrate here on the domains that receive special attention in the following sections. The structures each contain a core of conserved three-dimensional structure, a hood, enclosing the strands forming the top of the carboxyl portion of the core, whose primary and higher-level structure varies between enzymes of different specificities and a flexible loop that can move to cover the tops of the strands that form the more amino-terminal portion of the core.