Toolkit/engineered soluble photoactivated guanylate cyclases
engineered soluble photoactivated guanylate cyclases
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Engineered soluble photoactivated guanylate cyclases are microbe-derived engineered protein-domain optogenetic tools that couple light activation to guanylate cyclase activity. A 2018 study reported their biochemical characterization and presented them as an expansion of the optogenetic toolkit.
Usefulness & Problems
Why this is useful
These tools are useful as light-responsive guanylate cyclases that broaden the available optogenetic repertoire. The supplied evidence supports their relevance as optogenetic components but does not provide specific application data or performance benchmarks.
Source:
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Problem solved
They address the need for additional optogenetic actuators based on soluble microbial proteins with light-activated guanylate cyclase function. The evidence indicates toolkit expansion, but it does not specify a particular biological system or experimental bottleneck that was solved.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The available evidence identifies these tools as engineered soluble microbial photoactivated guanylate cyclases and indicates biochemical characterization. No further practical details are provided on construct design, cofactors, expression systems, or delivery strategies.
The provided evidence does not report quantitative activity, spectral properties, dynamic range, kinetics, or validation in cells or organisms. It also does not specify the protein architecture, chromophore requirements, or comparative performance against other optogenetic cyclases.
Validation
Supporting Sources
Ranked Claims
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Approval Evidence
Biochemical Characterization of the Engineered Soluble Photoactivated Guanylate Cyclases from Microbes Expands Optogenetic Tools
Source:
The paper reports biochemical characterization of engineered soluble photoactivated guanylate cyclases from microbes.
Source:
Engineered soluble photoactivated guanylate cyclases from microbes expand optogenetic tools.
Source:
Comparisons
Source-backed strengths
The main supported strength is that these engineered microbial proteins were biochemically characterized, providing direct experimental assessment of their light-activated guanylate cyclase properties. The source also explicitly frames them as expanding optogenetic tools.
Ranked Citations
- 1.