tautomycin and microcystin

tautomycin has been researched along with microcystin* in 4 studies

Reviews

3 review(s) available for tautomycin and microcystin

Article	Year
[Tumor promotion by inhibitors of protein phosphatase 1 and 2A]. Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1998, Volume: 43, Issue:8 Suppl Topics: Animals; Antifungal Agents; Marine Toxins; Microcystins; Neoplasms, Experimental; Okadaic Acid; Oxazoles; Peptides, Cyclic; Phosphoprotein Phosphatases; Protein Phosphatase 1; Pyrans; Spiro Compounds	1998
[Naturally occurring toxins with specific inhibitory activity against protein serine/threonine phosphatases 1 and 2A]. Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1998, Volume: 43, Issue:8 Suppl Topics: Alkenes; Animals; Antifungal Agents; Cantharidin; Marine Toxins; Microcystins; Okadaic Acid; Oxazoles; Peptides, Cyclic; Phosphoprotein Phosphatases; Polyenes; Pyrans; Pyrones; Spiro Compounds	1998
Tumor promotion by inhibitors of protein phosphatases 1 and 2A: the okadaic acid class of compounds. Advances in cancer research, 1993, Volume: 61 Topics: Animals; Antifungal Agents; Carcinogens; Ethers, Cyclic; Humans; Microcystins; Neoplasms; Okadaic Acid; Peptides, Cyclic; Phosphoprotein Phosphatases; Pyrans; Spiro Compounds; Structure-Activity Relationship	1993

Other Studies

1 other study(ies) available for tautomycin and microcystin

Article	Year
Importance of the beta12-beta13 loop in protein phosphatase-1 catalytic subunit for inhibition by toxins and mammalian protein inhibitors. The Journal of biological chemistry, 1999, Aug-06, Volume: 274, Issue:32 Type-1 protein serine/threonine phosphatases (PP1) are uniquely inhibited by the mammalian proteins, inhibitor-1 (I-1), inhibitor-2 (I-2), and nuclear inhibitor of PP1 (NIPP-1). In addition, several natural compounds inhibit both PP1 and the type-2 phosphatase, PP2A. Deletion of C-terminal sequences that included the beta12-beta13 loop attenuated the inhibition of the resulting PP1alpha catalytic core by I-1, I-2, NIPP-1, and several toxins, including tautomycin, microcystin-LR, calyculin A, and okadaic acid. Substitution of C-terminal sequences from the PP2A catalytic subunit produced a chimeric enzyme, CRHM2, that was inhibited by toxins with dose-response characteristics of PP1 and not PP2A. However, CRHM2 was insensitive to the PP1-specific inhibitors, I-1, I-2, and NIPP-1. The anticancer compound, fostriecin, differed from other phosphatase inhibitors in that it inhibited wild-type PP1alpha, the PP1alpha catalytic core, and CRHM2 with identical IC(50). Binding of wild-type and mutant phosphatases to immobilized microcystin-LR, NIPP-1, and I-2 established that the beta12-beta13 loop was essential for the association of PP1 with toxins and the protein inhibitors. These studies point to the importance of the beta12-beta13 loop structure and conformation for the control of PP1 functions by toxins and endogenous proteins. Topics: Alkenes; Amino Acid Sequence; Antifungal Agents; Enzyme Activation; Enzyme Inhibitors; Humans; Microcystins; Models, Molecular; Molecular Sequence Data; Peptides, Cyclic; Phosphoprotein Phosphatases; Polyenes; Protein Binding; Protein Phosphatase 1; Protein Structure, Secondary; Proteins; Pyrans; Pyrones; Sequence Homology, Amino Acid; Spiro Compounds	1999

Article

Year

Importance of the beta12-beta13 loop in protein phosphatase-1 catalytic subunit for inhibition by toxins and mammalian protein inhibitors.

The Journal of biological chemistry, 1999, Aug-06, Volume: 274, Issue:32

Type-1 protein serine/threonine phosphatases (PP1) are uniquely inhibited by the mammalian proteins, inhibitor-1 (I-1), inhibitor-2 (I-2), and nuclear inhibitor of PP1 (NIPP-1). In addition, several natural compounds inhibit both PP1 and the type-2 phosphatase, PP2A. Deletion of C-terminal sequences that included the beta12-beta13 loop attenuated the inhibition of the resulting PP1alpha catalytic core by I-1, I-2, NIPP-1, and several toxins, including tautomycin, microcystin-LR, calyculin A, and okadaic acid. Substitution of C-terminal sequences from the PP2A catalytic subunit produced a chimeric enzyme, CRHM2, that was inhibited by toxins with dose-response characteristics of PP1 and not PP2A. However, CRHM2 was insensitive to the PP1-specific inhibitors, I-1, I-2, and NIPP-1. The anticancer compound, fostriecin, differed from other phosphatase inhibitors in that it inhibited wild-type PP1alpha, the PP1alpha catalytic core, and CRHM2 with identical IC(50). Binding of wild-type and mutant phosphatases to immobilized microcystin-LR, NIPP-1, and I-2 established that the beta12-beta13 loop was essential for the association of PP1 with toxins and the protein inhibitors. These studies point to the importance of the beta12-beta13 loop structure and conformation for the control of PP1 functions by toxins and endogenous proteins.

Topics: Alkenes; Amino Acid Sequence; Antifungal Agents; Enzyme Activation; Enzyme Inhibitors; Humans; Microcystins; Models, Molecular; Molecular Sequence Data; Peptides, Cyclic; Phosphoprotein Phosphatases; Polyenes; Protein Binding; Protein Phosphatase 1; Protein Structure, Secondary; Proteins; Pyrans; Pyrones; Sequence Homology, Amino Acid; Spiro Compounds

1999