Biomaterial Database

Inhibition of fructose-1,6-biphosphatase by the photoaffinity AMP analog, 8-azidoadenosine 5'-monophosphate. 1979

F Marcus, and B E Haley

Inhibition studies with the photoreactive AMP analog, 8-azidoadenosine 5'-monophosphate (8-azido-AMP), demonstrate that this compound is, like AMP, an allosteric inhibitor of pig kidney and muscle fructose-1,6-biphosphateses. Photolysis of a mixture of purified pig kidney fructose-1,6-biphosphate and 8-azido-[14C]AMP results in the loss of enzyme activity and the reagent is incorporated to the protein. The incorporation of reagent linearly correlates with the loss of enzyme activity. Extrapolation to zero activity correlates with the incorporation of 3.7 mol of reagent/mol of enzyme (i.e. 0.9 per subunit). Thus, 8-azido-AMP appears to be a photoaffinity label for the allosteric AMP binding site of fructose-1,6-biphosphatase.

UI	MeSH Term	Description	Entries
D007668	Kidney	Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.	Kidneys
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D010782	Photolysis	Chemical bond cleavage reactions resulting from absorption of radiant energy.	Photodegradation
D006597	Fructose-Bisphosphatase	An enzyme that catalyzes the conversion of D-fructose 1,6-bisphosphate and water to D-fructose 6-phosphate and orthophosphate. EC 3.1.3.11.	Fructose-1,6-Bisphosphatase,Fructose-1,6-Diphosphatase,Fructosediphosphatase,Hexosediphosphatase,D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase,FDPase,Fructose-1,6-Biphosphatase,1-Phosphohydrolase, D-Fructose-1,6-Bisphosphate,D Fructose 1,6 Bisphosphate 1 Phosphohydrolase,Fructose 1,6 Biphosphatase,Fructose 1,6 Bisphosphatase,Fructose 1,6 Diphosphatase,Fructose Bisphosphatase
D000249	Adenosine Monophosphate	Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.	AMP,Adenylic Acid,2'-AMP,2'-Adenosine Monophosphate,2'-Adenylic Acid,5'-Adenylic Acid,Adenosine 2'-Phosphate,Adenosine 3'-Phosphate,Adenosine 5'-Phosphate,Adenosine Phosphate Dipotassium,Adenosine Phosphate Disodium,Phosphaden,2' Adenosine Monophosphate,2' Adenylic Acid,5' Adenylic Acid,5'-Phosphate, Adenosine,Acid, 2'-Adenylic,Acid, 5'-Adenylic,Adenosine 2' Phosphate,Adenosine 3' Phosphate,Adenosine 5' Phosphate,Dipotassium, Adenosine Phosphate,Disodium, Adenosine Phosphate,Monophosphate, 2'-Adenosine,Phosphate Dipotassium, Adenosine,Phosphate Disodium, Adenosine
D000345	Affinity Labels	Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids.	Affinity Labeling Reagents,Labeling Reagents, Affinity,Labels, Affinity,Reagents, Affinity Labeling
D000494	Allosteric Regulation	The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.	Regulation, Allosteric,Allosteric Regulations,Regulations, Allosteric
D000495	Allosteric Site	A site on an enzyme which upon binding of a modulator, causes the enzyme to undergo a conformational change that may alter its catalytic or binding properties.	Allosteric Sites,Site, Allosteric,Sites, Allosteric
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013329	Structure-Activity Relationship	The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.	Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships