5962-18-5

Usage

Uses

Used in Pharmaceutical Industry:
1-(2-Carboxyphenylamino)-1-deoxyribulose 5-phosphate is used as a pharmaceutical compound for its potential therapeutic applications. The presence of the 2-carboxyphenylamino group may allow for interactions with specific biological targets, making it a candidate for the development of new drugs or drug delivery systems.
Used in Chemical Research:
In the field of chemical research, 1-(2-Carboxyphenylamino)-1-deoxyribulose 5-phosphate can be used as a starting material or intermediate for the synthesis of more complex molecules. Its unique structure may provide new insights into the reactivity and properties of related compounds, contributing to the advancement of chemical knowledge.
Used in Biochemical Studies:
1-(2-Carboxyphenylamino)-1-deoxyribulose 5-phosphate may also be utilized in biochemical studies to investigate its interactions with enzymes, proteins, or other biomolecules. Understanding these interactions could lead to the discovery of new biological pathways or the development of targeted therapies for various diseases.

InChI:InChI=1/C12H16NO9P/c14-9(11(16)10(15)6-22-23(19,20)21)5-13-8-4-2-1-3-7(8)12(17)18/h1-4,10-11,13,15-16H,5-6H2,(H,17,18)(H2,19,20,21)/t10-,11+/m1/s1

Upstream product

• 27695-85-8 N'-(5'-phosphoribosyl)anthranilate 

Relevant academic research and scientific papers

Identification and analysis of residues contained on β → α loops of the dual-substrate (βα)8 phosphoribosyl isomerase a specific for its phosphoribosyl anthranilate isomerase activity

A good model to experimentally explore evolutionary hypothesis related to enzyme function is the ancient-like dual-substrate (βα)8 phosphoribosyl isomerase A (PriA), which takes part in both histidine and tryptophan biosynthesis in Streptomyces coelicolor and related organisms. In this study, we determined the Michaelis-Menten enzyme kinetics for both isomerase activities in wild-type PriA from S. coelicolor and in selected single-residue monofunctional mutants, identified after Escherichia coli in vivo complementation experiments. Structural and functional analyses of a hitherto unnoticed residue contained on the functionally important β → α loop 5, namely, Arg139, which was postulated on structural grounds to be important for the dual-substrate specificity of PriA, is presented for the first time. Indeed, enzyme kinetics analyses done on the mutant variants PriA-Ser81Thr and PriA-Arg139Asn showed that these residues, which are contained on β → α loops and in close proximity to the N-terminal phosphate-binding site, are essential solely for the phosphoribosyl anthranilate isomerase activity of PriA. Moreover, analysis of the X-ray crystallographic structure of PriA-Arg139Asn elucidated at 1.95 A herein strongly implicates the occurrence of conformational changes in this β → α loop as a major structural feature related to the evolution of the dual-substrate specificity of PriA. It is suggested that PriA has evolved by tuning a fine energetic balance that allows the sufficient degree of structural flexibility needed for accommodating two topologically dissimilar substrates-within a bifunctional and thus highly constrained active site-without compromising its structural stability. Published by Wiley-Blackwell.