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Kinetics of Binding of Multisubstrate Analogue Inhibitor (2-Amino-9-[2-(Phosphonomethoxy)Ethyl]-6-Sulfanylpurine) with Trimeric Purine Nucleoside Phosphorylase
- Source :
- Nucleosides, Nucleotides & Nucleic Acids. 26:969-974
- Publication Year :
- 2007
- Publisher :
- Informa UK Limited, 2007.
-
Abstract
- Complex formation of multisubstrate analogue inhibitor--2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine (PME-6-thio-Gua) with trimeric purine nucleoside phosphorylase from Cellulomonas sp. was investigated using a stopped-flow spectrofluorimetric approach. Results obtained indicate that, in contrast to binding of guanine, i.e., the transition-state conformation trapping ligand, for which binding at each active site is followed by the enzyme conformational change, association of the ground-state analogue PME-6-thio-Gua is a one-step process.
- Subjects :
- Conformational change
Guanine
Stereochemistry
Kinetics
Purine nucleoside phosphorylase
Models, Biological
Biochemistry
Fluorescence
chemistry.chemical_compound
Cellulomonas sp
Genetics
Enzyme Inhibitors
Protein Structure, Quaternary
Cellulomonas
chemistry.chemical_classification
biology
Active site
General Medicine
Ligand (biochemistry)
Enzyme
Purine-Nucleoside Phosphorylase
chemistry
biology.protein
Molecular Medicine
Subjects
Details
- ISSN :
- 15322335 and 15257770
- Volume :
- 26
- Database :
- OpenAIRE
- Journal :
- Nucleosides, Nucleotides & Nucleic Acids
- Accession number :
- edsair.doi.dedup.....0d829ce502131a7709dbf74dd9674ea7