Application | Comment | Organism |
---|---|---|
molecular biology | the enzyme is a favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light. The rhodopsin domain from Catenaria is more photostable than that from Blastocladiella, and the signaling state persists longer, both of which are highly desirable traits for optogenetic applications | Catenaria anguillulae |
pharmacology | pharmacological approaches do not allow cell specific manipulation of cyclic nucleotides in tissue and lack precision in space and time, limitations that can be overcome using the light-activated enzyme | Catenaria anguillulae |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged truncated cyclase domain in Escherichia coli C41. The mutant enzyme E497K/C566D is expressed the N-terminal YFP-tagged constructs in oocytes | Catenaria anguillulae |
Crystallization (Comment) | Organism |
---|---|
crystal structure of the ligand-bound adenylyl cyclase (resulting from the point mutations E497K/C566D) domain at 2.25 A reveals the mechanistic basis for the change from cGMP to cAMP production | Catenaria anguillulae |
Protein Variants | Comment | Organism |
---|---|---|
E497K/C566D | mutations within the nucleotide binding site generates rhodopsin-adenylyl cyclases | Catenaria anguillulae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the ATP analogs ATP-Sp-alphaS and ATP-Rp-alphaS are potent inhibitors | Catenaria anguillulae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | the N-terminus is positioned intracellularly | Catenaria anguillulae | 16020 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
21500 | - |
SDS-PAGE | Catenaria anguillulae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Catenaria anguillulae | A0A1Y2HEJ3 | - |
- |
Catenaria anguillulae PL171 | A0A1Y2HEJ3 | - |
- |
Purification (Comment) | Organism |
---|---|
truncated His-tagged guanylyl cyclase | Catenaria anguillulae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP | adenylyl cyclase activity results from the point mutations E497K/C566D in guanylyl cyclase | Catenaria anguillulae | 3',5'-cyclic AMP + diphosphate | - |
? | |
ATP | adenylyl cyclase activity results from the point mutations E497K/C566D in guanylyl cyclase | Catenaria anguillulae PL171 | 3',5'-cyclic AMP + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 21500, SDS-PAGE | Catenaria anguillulae |
Organism | Comment | Expression |
---|---|---|
Catenaria anguillulae | addition of GTP/Mn2+ reveals the cyclase domain to be constitutively active | additional information |