Gmprga

Gmprga represents a short peptide sequence containing mixed polar and hydrophobic residues that influence folding behavior. The motif supports investigations of charge distribution and solvent interactions. Researchers analyze its conformational transitions to clarify structure-function relationships. Applications include peptide-material design, motif exploration, and biochemical interaction studies.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Gmprga(CAS 2059978-58-2)

CAT No: R2514

CAS No:2059978-58-2

Synonyms/Alias:GMPRGA;HY-P6011;DA-73818;CS-0901458;2059978-58-2;

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M.F/Formula
C23H41N9O7S
M.W/Mr.
587.7
Sequence
One Letter Code:GMPRGA
Three Letter Code:H-Gly-Met-Pro-Arg-Gly-Ala-OH

Gmprga, also known as guanosine monophosphate reductase from Gallus gallus (chicken), is an essential enzyme in the purine nucleotide cycle, catalyzing the NADPH-dependent reduction of guanosine monophosphate (GMP) to inosine monophosphate (IMP). As a key player in cellular nucleotide metabolism, Gmprga helps regulate the balance between guanine and adenine nucleotides, which is fundamental to numerous biochemical processes including DNA and RNA synthesis, energy transfer, and signal transduction. Its biochemical significance extends to studies in enzymology, metabolic regulation, and comparative biochemistry, making it a valuable tool for researchers investigating purine metabolism and related cellular pathways.

Enzyme Kinetics Research: Gmprga serves as a robust model for detailed enzyme kinetics studies, enabling researchers to elucidate the catalytic mechanism and substrate specificity of GMP reductases. By providing a purified source of the enzyme, it facilitates the measurement of kinetic parameters, inhibitor profiling, and the exploration of allosteric regulation. These studies are crucial for understanding how cells fine-tune nucleotide pools and for identifying potential points of metabolic control in purine biosynthesis.

Metabolic Pathway Elucidation: The enzyme is frequently employed in in vitro assays to reconstruct and analyze the purine salvage and degradation pathways. By incorporating Gmprga into reconstituted metabolic systems, scientists can investigate flux control, substrate channeling, and the interplay between nucleotide synthesis and degradation. This approach is especially valuable for mapping metabolic networks in avian systems or for comparative analyses across species, offering insights into evolutionary adaptations in nucleotide metabolism.

Structural and Functional Characterization: Gmprga is a prime candidate for structural biology applications, including X-ray crystallography, cryo-electron microscopy, and NMR spectroscopy. Structural studies involving this enzyme provide a molecular-level understanding of its active site architecture, cofactor interactions, and conformational dynamics. Such insights are instrumental for rational drug design efforts targeting related enzymes in pathogenic organisms, as well as for engineering enzymes with altered substrate specificity or improved catalytic properties.

Protein Engineering and Mutagenesis: The availability of recombinant Gmprga enables targeted mutagenesis and protein engineering experiments aimed at dissecting structure-function relationships. By introducing specific amino acid substitutions, researchers can probe the roles of conserved residues, investigate the impact of mutations on enzyme activity, and develop variants with novel properties. These engineered forms are valuable for both basic research and potential biotechnological applications where custom nucleotide metabolism is desired.

Analytical Biochemistry and Assay Development: Gmprga is utilized as a standard or reagent in the development of quantitative assays for guanine nucleotides and related metabolites. Its specific catalytic activity allows for the sensitive detection and quantification of GMP and IMP in complex biological samples, supporting studies in metabolomics, diagnostics, and quality control. The enzyme's well-characterized reaction provides a reliable basis for the design of colorimetric, fluorometric, or chromatographic assays tailored to research and industrial needs.

In summary, Gmprga is a versatile biochemical tool with applications spanning enzyme kinetics, metabolic pathway analysis, structural biology, protein engineering, and analytical assay development. Its role in purine metabolism and its utility in diverse research contexts underscore its importance for advancing the understanding of nucleotide biochemistry and for supporting innovation in biochemical and biotechnological research.

InChI
InChI=1S/C23H41N9O7S/c1-13(22(38)39)29-18(34)12-28-19(35)14(5-3-8-27-23(25)26)31-20(36)16-6-4-9-32(16)21(37)15(7-10-40-2)30-17(33)11-24/h13-16H,3-12,24H2,1-2H3,(H,28,35)(H,29,34)(H,30,33)(H,31,36)(H,38,39)(H4,25,26,27)/t13-,14-,15-,16-/m0/s1
InChI Key
UEXOULUZVZYKES-VGWMRTNUSA-N

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