GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0016627 describes a molecular function: catalysis of a redox reaction in which a CH-CH group acts as the hydrogen or electron donor [1,2].
• Enzymes in this class include biliverdin reductase (BLVR), DHCR24, retinol saturase (RETSAT), protochlorophyllide oxidoreductase (POR), and nitrogenase-like tetrapyrrole reductases [2,3,4,5,7,8].
• These enzymes participate in heme catabolism, cholesterol biosynthesis, vitamin A metabolism, chlorophyll biosynthesis, and cofactor assembly [2,4,6,7,8].
• Dysregulation is linked to hepatic steatosis, inflammation, cancer, and metabolic disease, making these enzymes attractive therapeutic targets [1,2,4].
• CRISPR knockout, point-mutation, knock-in, and overexpression models enable causal dissection of CH-CH oxidoreductase function in cells and animals [1,3,4].
• Key methods include Ribo-seq, RNA-seq, proteomics, metabolomics, and optogenetic imaging to measure redox activity and pathway flux [3,5,7].
Description
GO:0016627, oxidoreductase activity, acting on the CH-CH group of donors, is a molecular function term in the Gene Ontology that defines enzymes catalyzing oxidation-reduction reactions where a carbon-carbon double bond (CH-CH) serves as the hydrogen or electron donor [1,2]. This class is central to diverse metabolic pathways, including heme degradation by biliverdin reductase, cholesterol synthesis by DHCR24, retinol saturation by RETSAT, and light-dependent protochlorophyllide reduction by POR [2,3,4,5,6,7]. Researchers study these enzymes because they control flux through lipid, pigment, and cofactor biosynthetic routes and are implicated in diseases such as hepatic steatosis, inflammation, and cancer [1,2,4]. Understanding their catalytic mechanisms and regulation provides opportunities for therapeutic intervention and for engineering metabolic pathways in biotechnology [3,5,7,8].
oxidoreductase activity, acting on the CH-CH group of donors At A Glance
| GO ID | GO:0016627 |
|---|---|
| GO term | oxidoreductase activity, acting on the CH-CH group of donors |
| Ontology | molecular_function |
| Synonym | oxidoreductase activity, acting on the CH-CH group of donors, other acceptors |
| Major function | Catalysis of redox reactions where a CH-CH group donates hydrogen/electrons to an acceptor |
| Example enzymes | BLVRB, DHCR24, RETSAT, POR, nitrogenase-like reductases |
| Cofactors | NAD(P)H, FAD, heme, iron-sulfur clusters |
| Pathways | Heme catabolism, cholesterol biosynthesis, vitamin A metabolism, chlorophyll biosynthesis |
What Is GO:0016627?
According to QuickGO, GO:0016627 is defined as catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. In simpler terms, these enzymes remove hydrogen from a carbon-carbon double bond or transfer electrons from that bond to an acceptor, often using cofactors like NAD(P)H, FAD, or heme [1,2,5,7].
Why Is oxidoreductase activity, acting on the CH-CH group of donors Important in Cell Biology?
GO:0016627 enzymes are critical for maintaining metabolic homeostasis, detoxification, and biosynthesis of essential lipids and pigments. Their dysfunction contributes to diseases including non-alcoholic fatty liver disease, inflammation, and cancer, and they are targets for drug development and metabolic engineering [1,2,4,6].
• Regulates heme catabolism and bilirubin production via biliverdin reductase [2,3].
• Controls cholesterol synthesis downstream of HMGCR through DHCR24 [1,6].
• Modulates vitamin A signaling and lipid metabolism via RETSAT.
• Enables light-dependent chlorophyll biosynthesis in plants through POR [5,7].
• Participates in nitrogenase-like tetrapyrrole reduction for cofactor assembly.
• Implicated in hepatic steatosis and inflammation through LXRα activation.
• Provides targets for optogenetic and imaging tools via biliverdin reductase knockout.
• Offers opportunities for CRISPR-based metabolic pathway engineering [1,3,4].
Molecular Mechanism of oxidoreductase activity, acting on the CH-CH group of donors
Substrate recognition and CH-CH donor binding
In simple terms: The enzyme first grabs the molecule that has the carbon-carbon double bond.
Enzymes in GO:0016627 bind substrates containing a CH-CH group, such as biliverdin, lanosterol, retinol, or protochlorophyllide, positioning the double bond for hydride or electron transfer [2,4,5,7]. Structural studies of biliverdin reductase and DHCR24 reveal specific pockets that accommodate the planar tetrapyrrole or sterol ring systems [2,6].
Hydride or electron transfer to acceptor
In simple terms: The enzyme moves hydrogen or electrons from the double bond to another molecule.
The CH-CH group donates hydrogen or electrons to an acceptor, which may be NAD(P)+, FAD, or a protein-bound cofactor. For example, biliverdin reductase transfers electrons from biliverdin to NAD(P)H, reducing the CH-CH bond to form bilirubin [2,3]. In cholesterol synthesis, DHCR24 catalyzes the reduction of the C-24 double bond of desmosterol using NADPH [1,6].
Cofactor regeneration and catalytic cycle
In simple terms: The enzyme resets its cofactor so it can work again.
After reduction, the oxidized cofactor must be regenerated. In POR, light absorption by chlorophyllide triggers electron transfer from NADPH via a protochlorophyllide molecule, and the enzyme returns to its resting state [5,7]. Nitrogenase-like reductases use ATP and iron-sulfur clusters to recycle electrons for tetrapyrrole reduction.
Regulation by lipids and light
In simple terms: Lipids and light can switch these enzymes on or off.
MGDG, PG, and SQDG lipids regulate the activity of light-dependent protochlorophyllide oxidoreductase, linking membrane composition to chlorophyll synthesis. In mammals, DHCR24 activity is modulated by sterol intermediates and LXRα signaling, affecting hepatic lipid homeostasis.
Key Genes Involved in GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
The following genes encode enzymes with oxidoreductase activity acting on CH-CH group donors, as supported by published literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| BLVRB | Biliverdin reductase B; reduces biliverdin to bilirubin | Heme catabolism, oxidative stress, optogenetics [2,3] |
| BLVRA | Biliverdin reductase A; reduces biliverdin to bilirubin | Metabolic regulation, inflammation |
| DHCR24 | 24-dehydrocholesterol reductase; cholesterol synthesis | Hepatic steatosis, LXRα signaling [1,6] |
| RETSAT | Retinol saturase; saturates retinol double bonds | Vitamin A metabolism, lipid signaling |
| POR | Protochlorophyllide oxidoreductase; chlorophyll synthesis | Plant photomorphogenesis, light signaling [5,7] |
| NifB | Nitrogenase-like reductase; tetrapyrrole reduction | Cofactor biosynthesis, nitrogenase assembly |
| NifEN | Nitrogenase-like reductase; FeMo-co synthesis | Nitrogen fixation, metallocluster assembly |
| CBR1 | Carbonyl reductase 1; reduces quinones and carbonyls | Drug metabolism, cancer |
| CBR3 | Carbonyl reductase 3; reduces carbonyl compounds | Xenobiotic metabolism |
| AKR1C1 | Aldo-keto reductase; reduces steroids and prostaglandins | Hormone metabolism, cancer |
| AKR1C2 | Aldo-keto reductase; reduces bile acids and steroids | Liver disease, cancer |
| SRD5A1 | Steroid 5-alpha reductase; reduces testosterone | Androgen metabolism, prostate cancer |
| SRD5A2 | Steroid 5-alpha reductase; reduces testosterone | Androgen metabolism, prostate cancer |
| LBR | Lamin B receptor; sterol reductase | Cholesterol synthesis, nuclear envelope |
| TM7SF2 | Delta-14 sterol reductase; cholesterol synthesis | Cholesterol biosynthesis |
| NSDHL | Sterol dehydrogenase; cholesterol synthesis | CHILD syndrome, cholesterol metabolism |
| SC5D | Sterol-C5-desaturase; cholesterol synthesis | Cholesterol biosynthesis |
| DHCR7 | 7-dehydrocholesterol reductase; cholesterol synthesis | Smith-Lemli-Opitz syndrome |
How Is oxidoreductase activity, acting on the CH-CH group of donors Regulated?
The activity of GO:0016627 enzymes is regulated at multiple levels. DHCR24 is transcriptionally controlled by LXRα and sterol regulatory element-binding proteins (SREBPs), and its inhibition activates LXRα to ameliorate hepatic steatosis. Biliverdin reductase isozymes are regulated by oxidative stress and heme availability, influencing bilirubin production and cellular redox balance. In plants, POR activity is regulated by light and membrane lipids such as MGDG, PG, and SQDG, which modulate its catalytic efficiency during photomorphogenesis [5,7]. Nitrogenase-like reductases are controlled by ATP and iron-sulfur cluster availability.
oxidoreductase activity, acting on the CH-CH group of donors and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| DHCR24 | Hepatic steatosis, inflammation | Liver-specific KO or point-mutation knock-in in mice |
| BLVRB | Oxidative stress, cancer | BLVRB knockout cells and optogenetic imaging [2,3] |
| RETSAT | Vitamin A metabolism, lipid signaling | RETSAT KO and overexpression in adipocytes |
| DHCR7 | Smith-Lemli-Opitz syndrome | Patient-derived iPSCs with point mutations |
| POR | Chlorophyll biosynthesis, photomorphogenesis | Arabidopsis POR knockout and complementation [5,7] |
Hepatic steatosis and inflammation
Inhibition of DHCR24 activates LXRα and ameliorates hepatic steatosis and inflammation in mouse models, linking CH-CH oxidoreductase activity to lipid homeostasis and liver disease. DHCR24 catalyzes the reduction of the C-24 double bond of desmosterol, and its modulation affects cholesterol synthesis and inflammatory signaling [1,6].
Cancer and oxidative stress
Biliverdin reductase isozymes are involved in heme catabolism and redox regulation, and their altered expression has been associated with cancer and oxidative stress-related pathologies. The enzyme produces bilirubin, an antioxidant, and modulates cellular signaling pathways.
Metabolic and developmental disorders
Defects in cholesterol biosynthesis enzymes such as DHCR7 and NSDHL, which act on CH-CH groups, cause Smith-Lemli-Opitz syndrome and CHILD syndrome, respectively. These disorders highlight the importance of CH-CH oxidoreductases in development and metabolism.
Plant photomorphogenesis and biotechnology
Light-dependent protochlorophyllide oxidoreductase (POR) is essential for chlorophyll synthesis and photomorphogenesis in plants, and its regulation by lipids influences agricultural traits [5,7]. Understanding POR mechanism aids in engineering light-controlled gene expression.
From oxidoreductase activity, acting on the CH-CH group of donors-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of DHCR24 affect lipid homeostasis? | DHCR24 knockout hepatocytes and mouse liver |
| Can BLVRB be used for deep-tissue imaging? | BLVRB knockout mice with optogenetic manipulation |
| How does RETSAT regulate retinol metabolism? | RETSAT overexpression and knockout cell lines |
| What is the role of POR in light signaling? | POR point-mutation knock-in in Arabidopsis [5,7] |
| How do nitrogenase-like reductases assemble cofactors? | NifB/NifEN knockout in bacteria |
| Can CH-CH oxidoreductases be targeted for cancer therapy? | CRISPR library screening in cancer cell lines |
How to Study the oxidoreductase activity, acting on the CH-CH group of donors Process
| Method | What It Measures | Typical Application |
|---|---|---|
| RNA-seq | Gene expression changes | DHCR24 inhibition in liver cells |
| Ribo-seq | Translational efficiency | BLVRB knockout cells |
| Proteomics | Protein abundance and modifications | Cholesterol synthesis enzymes |
| Metabolomics | Metabolite levels (e.g., bilirubin, desmosterol) | Heme catabolism and sterol pathways [1,2] |
| Optogenetic imaging | Enzyme activity in live tissue | BLVRB knockout mice |
| Enzymatic assay | Catalytic rate and cofactor dependence | POR and biliverdin reductase [2,5] |
| CRISPR screening | Gene essentiality and pathway interactions | Cancer cell lines |
| Structural biology | Protein-ligand interactions | POR and nitrogenase-like reductases [5,8] |
Genomic and transcriptomic profiling
RNA-seq and Ribo-seq can quantify expression and translation of GO:0016627 genes under different conditions, such as DHCR24 inhibition or BLVRB knockout [1,3]. These methods reveal transcriptional responses and translational efficiency changes.
Proteomic and metabolomic analysis
Mass spectrometry-based proteomics and metabolomics measure enzyme abundance and flux through pathways like cholesterol synthesis and heme catabolism [1,2]. This helps link CH-CH oxidoreductase activity to metabolite levels.
Imaging and optogenetics
Biliverdin reductase knockout enables deep-tissue high-sensitivity multimodal imaging and optogenetic manipulation, as demonstrated in mice. Fluorescent reporters and light-controlled systems allow real-time monitoring of enzyme activity.
Enzymatic assays and structural studies
In vitro assays with purified enzymes and substrates (e.g., biliverdin, protochlorophyllide) measure catalytic rates and cofactor requirements [2,5,7]. X-ray crystallography and cryo-EM provide structural insights into CH-CH donor binding [5,8].
How CRISPR Can Be Used to Study GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
Knockout
CRISPR knockout of GO:0016627 genes such as DHCR24 or BLVRB enables loss-of-function studies. For example, BLVRB knockout mice were used for deep-tissue imaging and optogenetic manipulation. DHCR24 knockout in liver cells can test effects on lipid metabolism.
Point Mutation
Point mutations can dissect catalytic residues or regulatory sites. For instance, mutating the active-site residues of POR or DHCR24 can reveal their roles in substrate binding and catalysis [1,5].
Knock-in
Knock-in of tagged or fluorescent versions of CH-CH oxidoreductases allows real-time tracking of localization and activity. Tagged BLVRB or DHCR24 can be used for imaging and proteomics [3,6].
Overexpression
Overexpression of RETSAT or DHCR24 can test gain-of-function effects on lipid metabolism and signaling. This approach helps identify downstream pathways and therapeutic potential [1,4].
How EDITGENE Supports oxidoreductase activity, acting on the CH-CH group of donors Research
Researchers studying oxidoreductase activity, acting on the CH-CH group of donors-related genes often need to determine whether a candidate gene is causally involved in a specific metabolic or disease pathway. EDITGENE provides CRISPR-based cell models and screening services to accelerate this discovery.
Contact EDITGENE today to design your custom CRISPR model for oxidoreductase activity, acting on the CH-CH group of donors research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
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| ACOX3 Knockout HEK293 Cell Line | EDJ-KQ1809 | Human | 8310 | Details Get a Quote |
| ACOX1 Knockout HEK293 Cell Line | EDJ-KQ1810 | Human | 51 | Details Get a Quote |
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| ACAD10 Knockout HEK293 Cell Line | EDJ-KQ2319 | Human | 80724 | Details Get a Quote |
| SRD5A1 Knockout HEK293 Cell Line | EDJ-KQ2660 | Human | 6715 | Details Get a Quote |
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| ACADSB Knockout HEK293 Cell Line | EDJ-KQ3993 | Human | 36 | Details Get a Quote |
| DPYD Knockout HEK293 Cell Line | EDJ-KQ4478 | Human | 1806 | Details Get a Quote |
| GCDH Knockout HEK293 Cell Line | EDJ-KQ4688 | Human | 2639 | Details Get a Quote |
| IVD Knockout HEK293 Cell Line | EDJ-KQ5012 | Human | 3712 | Details Get a Quote |
| ACOX2 Knockout HEK293 Cell Line | EDJ-KQ6197 | Human | 8309 | Details Get a Quote |
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Frequently Asked Questions About oxidoreductase activity, acting on the CH-CH group of donors
What is GO:0016627?
GO:0016627 is a Gene Ontology molecular function term for oxidoreductase activity acting on CH-CH group donors, catalyzing redox reactions where a carbon-carbon double bond donates hydrogen or electrons [1,2].
What genes are involved in oxidoreductase activity, acting on the CH-CH group of donors?
Key genes include BLVRA, BLVRB, DHCR24, RETSAT, POR, and nitrogenase-like reductases such as NifB and NifEN [2,3,4,5,7,8].
What diseases are linked to CH-CH oxidoreductases?
They are linked to hepatic steatosis, inflammation, cancer, Smith-Lemli-Opitz syndrome, and CHILD syndrome [1,2,6].
How can I study GO:0016627 enzymes?
Use CRISPR knockout, point mutations, knock-in tags, overexpression, RNA-seq, Ribo-seq, proteomics, metabolomics, and imaging [1,3,4,5].
What is the role of DHCR24 in cholesterol synthesis?
DHCR24 catalyzes the reduction of the C-24 double bond of desmosterol, a final step in cholesterol biosynthesis, and its inhibition activates LXRα [1,6].
How does biliverdin reductase work?
Biliverdin reductase reduces biliverdin to bilirubin using NAD(P)H, acting on a CH-CH group and contributing to heme catabolism and antioxidant defense [2,3].
What is retinol saturase?
RETSAT is a CH-CH oxidoreductase that saturates retinol double bonds, affecting vitamin A metabolism and lipid signaling.
What is protochlorophyllide oxidoreductase?
POR is a light-dependent enzyme that reduces protochlorophyllide to chlorophyllide, essential for chlorophyll synthesis and photomorphogenesis in plants [5,7].
Can CRISPR be used to model CH-CH oxidoreductase diseases?
Yes, CRISPR knockout and knock-in models in cells and mice have been used to study DHCR24, BLVRB, and RETSAT in metabolic and inflammatory diseases [1,3,4].
What methods measure CH-CH oxidoreductase activity?
Enzymatic assays, metabolomics, proteomics, and optogenetic imaging are commonly used to measure activity and pathway flux [2,3,5].
Conclusion
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors, encompasses a diverse set of enzymes essential for heme catabolism, cholesterol synthesis, vitamin A metabolism, chlorophyll biosynthesis, and cofactor assembly [2,4,5,6,7,8]. Their dysfunction is implicated in metabolic, inflammatory, and developmental diseases, making them important research and therapeutic targets [1,2,6]. CRISPR-based models and multi-omics methods provide powerful tools to dissect their mechanisms and identify new interventions [1,3,4].
References
- 1. Zhou E et al.. 2023. Inhibition of DHCR24 activates LXRα to ameliorate hepatic steatosis and inflammation.. EMBO Mol Med 15(8):e16845 PMID: 37357756
- 2. O'Brien L et al.. 2015. Biliverdin reductase isozymes in metabolism.. Trends Endocrinol Metab 26(4):212-20 PMID: 25726384
- 3. Kasatkina LA et al.. 2025. Deep-tissue high-sensitivity multimodal imaging and optogenetic manipulation enabled by biliverdin reductase knockout.. Nat Commun 16(1):6469 PMID: 40659617
- 4. Weber P et al.. 2020. Retinol Saturase: More than the Name Suggests.. Trends Pharmacol Sci 41(6):418-427 PMID: 32345479
- 5. Gabruk M et al.. 2017. MGDG, PG and SQDG regulate the activity of light-dependent protochlorophyllide oxidoreductase.. Biochem J 474(7):1307-1320 PMID: 28188256
- 6. Sharpe LJ et al.. 2015. Navigating the Shallows and Rapids of Cholesterol Synthesis Downstream of HMGCR.. J Nutr Sci Vitaminol (Tokyo) 61 Suppl:S154-6 PMID: 26598836
- 7. Heyes DJ et al.. 2021. Photocatalysis as the 'master switch' of photomorphogenesis in early plant development.. Nat Plants 7(3):268-276 PMID: 33686224
- 8. Layer G et al.. 2017. Reduction of Chemically Stable Multibonds: Nitrogenase-Like Biosynthesis of Tetrapyrroles.. Adv Exp Med Biol 925:147-161 PMID: 27957709
