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Literature summary for 4.6.1.1 extracted from

  • Scheib, U.; Broser, M.; Constantin, O.M.; Yang, S.; Gao, S.; Mukherjee, S.; Stehfest, K.; Nagel, G.; Gee, C.E.; Hegemann, P5
    Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 A structure of the adenylyl cyclase domain (2018), Nat. Commun., 9, 2046 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.6.1.1

Application

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(Commentary)

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 (Commentary)

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

Protein Variants Comment Organism
E497K/C566D mutations within the nucleotide binding site generates rhodopsin-adenylyl cyclases Catenaria anguillulae

Inhibitors

Inhibitors Comment Organism Structure
additional information the ATP analogs ATP-Sp-alphaS and ATP-Rp-alphaS are potent inhibitors Catenaria anguillulae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the N-terminus is positioned intracellularly Catenaria anguillulae 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21500
-
 SDS-PAGE Catenaria anguillulae

Organism

Organism UniProt Comment Textmining
Catenaria anguillulae A0A1Y2HEJ3
-
-
Catenaria anguillulae PL171 A0A1Y2HEJ3
-
-

Purification (Commentary)

Purification (Comment) Organism
truncated His-tagged guanylyl cyclase Catenaria anguillulae

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 21500, SDS-PAGE Catenaria anguillulae

Expression

Organism Comment Expression
Catenaria anguillulae addition of GTP/Mn2+ reveals the cyclase domain to be constitutively active additional information