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Literature summary for 4.6.1.2 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 4.6.1.2

Application

Application Comment Organism
molecular biology the enzyme is a favorable optogenetic tool 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
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 Blastocladiella emersonii
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 Blastocladiella emersonii
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 Blastocladiella emersonii
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 cyclase Catenaria anguillulae

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.16
-
 GTP pH 7.5, 22°C, wild-type enzyme, wild-type enzyme Blastocladiella emersonii
5.78
-
 GTP pH 7.5, 22°C, wild-type enzyme, wild-type enzyme Catenaria anguillulae
6.09
-
 GTP pH 7.5, 22°C, wild-type enzyme, mutant enzyme E497K/C566D Catenaria anguillulae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Blastocladiella emersonii 16020
-
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 Blastocladiella emersonii
21500
-
 SDS-PAGE Catenaria anguillulae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP Blastocladiella emersonii converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark 3',5'-cyclic GMP + diphosphate
-
 ?
GTP Catenaria anguillulae the enzyme produces cGMP in response to green light with a light to dark activity ratio above 1000. After light excitation the putative signaling state forms. The membrane embedded protein converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark 3',5'-cyclic GMP + diphosphate
-
 ?
GTP Catenaria anguillulae PL171 the enzyme produces cGMP in response to green light with a light to dark activity ratio above 1000. After light excitation the putative signaling state forms. The membrane embedded protein converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark 3',5'-cyclic GMP + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Blastocladiella emersonii
-
-
-
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.
GTP converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark Blastocladiella emersonii 3',5'-cyclic GMP + diphosphate
-
 ?
GTP the enzyme produces cGMP in response to green light with a light to dark activity ratio above 1000. After light excitation the putative signaling state forms. The membrane embedded protein converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark Catenaria anguillulae 3',5'-cyclic GMP + diphosphate
-
 ?
GTP membrane embedded protein converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark. In contrast to membrane embedded protein, for both purified enzyme a significant dark activity is detected and the cGMP production increases linearly with substrate concentration Blastocladiella emersonii 3',5'-cyclic GMP + diphosphate
-
 ?
GTP the membrane embedded protein converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark. In contrast to membrane embedded protein, for both purified enzyme a significant dark activity is detected and the cGMP production increases linearly with substrate concentration Catenaria anguillulae 3',5'-cyclic GMP + diphosphate
-
 ?
GTP the enzyme produces cGMP in response to green light with a light to dark activity ratio above 1000. After light excitation the putative signaling state forms. The membrane embedded protein converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark Catenaria anguillulae PL171 3',5'-cyclic GMP + diphosphate
-
 ?
GTP the membrane embedded protein converts GTP into cGMP in many cell types upon green light stimulation whereas it is totally inactive in the dark. In contrast to membrane embedded protein, for both purified enzyme a significant dark activity is detected and the cGMP production increases linearly with substrate concentration Catenaria anguillulae PL171 3',5'-cyclic GMP + diphosphate
-
 ?

Subunits

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

Synonyms

Synonyms Comment Organism
BERhGC
-
 Blastocladiella emersonii
CaRhGC
-
 Catenaria anguillulae
rhodopsin-guanylyl cyclase
-
 Blastocladiella emersonii
rhodopsin-guanylyl cyclase
-
 Catenaria anguillulae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Blastocladiella emersonii
22
-
 assay at Catenaria anguillulae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.34
-
 GTP pH 7.5, 22°C, wild-type enzyme, wild-type enzyme Blastocladiella emersonii
1.01
-
 GTP pH 7.5, 22°C, wild-type enzyme, mutant enzyme E497K/C566D Catenaria anguillulae
1.13
-
 GTP pH 7.5, 22°C, wild-type enzyme, wild-type enzyme Catenaria anguillulae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Catenaria anguillulae

Expression

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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.16
-
 GTP pH 7.5, 22°C, wild-type enzyme, wild-type enzyme Blastocladiella emersonii
0.17
-
 GTP pH 7.5, 22°C, wild-type enzyme, mutant enzyme E497K/C566D Catenaria anguillulae
0.2
-
 GTP pH 7.5, 22°C, wild-type enzyme, wild-type enzyme Catenaria anguillulae