Biomaterial Database

Interconversion of Tetrahymena pyriformis ornithine decarboxylase from inactive to active form by phosphorylation. 1989

C P Lougovoi, and D A Kyriakidis

Faculty of Chemistry, Aristotelian University of Thessaloniki, Greece.

A protein kinase and an acidic phosphoprotein phosphatase were purified from Tetrahymena pyriformis which phosphorylate and dephosphorylate the purified ornithine decarboxylase (ODC) of this microorganism. The protein kinase and the phosphoprotein phosphatase are copurified with ODC and can be separated in three distinct peaks only by a hydrophobic column of phenyl-Sepharose. The purified kinase is not dependent on cAMP, requires Mg2+ for its catalytic activity and has a molecule mass of 45 kDa. Incubation of [32P]ODC with the purified phosphoprotein phosphatase results in a complete loss of 32P and its catalytic activity. Phosphorylation of the inactive phosphatase-treated ODC by endogenous kinase or rat liver casein kinase-2 results in 100 or 40% reactivation of the initial untreated ODC activity, respectively.

UI	MeSH Term	Description	Entries
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D009955	Ornithine Decarboxylase	A pyridoxal-phosphate protein, believed to be the rate-limiting compound in the biosynthesis of polyamines. It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethionine to form spermidine.	Ornithine Carboxy-lyase,Carboxy-lyase, Ornithine,Decarboxylase, Ornithine,Ornithine Carboxy lyase
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D011494	Protein Kinases	A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.	Protein Kinase,Kinase, Protein,Kinases, Protein
D004789	Enzyme Activation	Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.	Activation, Enzyme,Activations, Enzyme,Enzyme Activations
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
D013769	Tetrahymena pyriformis	A species of ciliate protozoa used extensively in genetic research.	Tetrahymena pyriformi,pyriformi, Tetrahymena
D047388	Casein Kinases	A group of protein-serine-threonine kinases that was originally identified as being responsible for the PHOSPHORYLATION of CASEINS. They are ubiquitous enzymes that have a preference for acidic proteins. Casein kinases play a role in SIGNAL TRANSDUCTION by phosphorylating a variety of regulatory cytoplasmic and regulatory nuclear proteins.	Casein Kinase,Kinase, Casein,Kinases, Casein
D051381	Rats	The common name for the genus Rattus.	Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus