GO:0047936 glucose 1-dehydrogenase [NAD(P)+] activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0047936 describes the molecular function of glucose 1-dehydrogenase [NAD(P)+] activity, which catalyzes the oxidation of beta-D-glucose to D-glucono-1,5-lactone using NAD(P)+ as an electron acceptor.
• This activity is central to NAD(P)-dependent glucose dehydrogenase (GDH) enzymes that are widely used in amperometric biosensors, bioelectrodes, and biofuel cells because they do not require oxygen and can transfer electrons directly or via mediators.
• The reaction produces NAD(P)H, making this activity a key node in artificial nicotinamide cofactor regeneration systems and in redox-balanced biotransformations.
• Glucose dehydrogenase-coupled assays are established analytical tools, for example for determining glucose-6-phosphatase activity through the glucose dehydrogenase-coupled reaction.
• Enzyme engineering and immobilization strategies, including polyethylene glycol-NAD conjugates, have been used to study and improve intramolecular hydride transfer in glucose dehydrogenase systems.
• In microbial systems such as Pseudomonas putida KT2440, pyrroloquinoline quinone-dependent glucose dehydrogenase activity is regulated in response to environmental and metabolic cues, illustrating the broader regulatory context of glucose-oxidizing enzymes.
Description
GO:0047936, glucose 1-dehydrogenase [NAD(P)+] activity, is a molecular function term in the Gene Ontology that describes the catalysis of the reaction beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H. This activity is carried out by NAD(P)-dependent glucose dehydrogenase enzymes, which oxidize the C1 hydroxyl group of glucose and transfer hydride to NAD+ or NADP+. Because the reaction generates a reduced nicotinamide cofactor and a lactone product, it sits at the interface of carbohydrate metabolism, redox biochemistry, and applied biocatalysis. For researchers, GO:0047936 matters because it defines a catalytic activity that is both biologically widespread and industrially valuable. NAD(P)-dependent glucose dehydrogenases are used in biosensors, bioelectrodes, and biofuel cells, where their ability to accept electrons from glucose without oxygen makes them attractive for miniaturized and implantable devices. The same activity is also exploited in coupled enzyme assays, for example to measure glucose-6-phosphatase activity via the glucose dehydrogenase-coupled reaction. At the mechanistic level, glucose 1-dehydrogenase [NAD(P)+] activity has been studied with cofactor analogues and engineered cofactor-enzyme conjugates to understand hydride transfer and cofactor recycling. In microbial physiology, related glucose dehydrogenase activities are regulated in response to environmental conditions, as shown for pyrroloquinoline quinone-dependent glucose dehydrogenase in Pseudomonas putida KT2440. Together, these studies make GO:0047936 a useful anchor for linking enzyme mechanism, metabolic redox balance, and biotechnological application.
glucose 1-dehydrogenase [NAD(P)+] activity At A Glance
| GO ID | GO:0047936 |
|---|---|
| GO term | glucose 1-dehydrogenase [NAD(P)+] activity |
| Ontology | molecular_function |
| Synonym | beta-D-glucose:NAD(P)+ 1-oxidoreductase activity; D-glucose dehydrogenase (NAD(P)); hexose phosphate dehydrogenase activity |
| Definition | Catalysis of the reaction: beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H |
| Major function | Oxidation of beta-D-glucose with concomitant reduction of NAD+ or NADP+ to NAD(P)H |
| Substrate | beta-D-glucose |
| Cofactor | NAD(P)+ |
| Product | D-glucono-1,5-lactone and NAD(P)H |
| Representative enzymes | NAD(P)-dependent glucose dehydrogenase enzymes used in biosensors and bioelectrodes |
| Related analytical use | Glucose dehydrogenase-coupled assays for glucose-6-phosphatase activity |
What Is GO:0047936?
In simple terms, GO:0047936 is the enzyme activity that removes two electrons and a proton equivalent from beta-D-glucose and hands them to NAD+ or NADP+, producing D-glucono-1,5-lactone and NAD(P)H. The QuickGO definition states: Catalysis of the reaction: beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H. This activity is synonymous with beta-D-glucose:NAD(P)+ 1-oxidoreductase activity, D-glucose dehydrogenase (NAD(P)), and hexose phosphate dehydrogenase activity. It is a molecular_function term, meaning it describes what a gene product does at the biochemical level rather than where it acts or which pathway it belongs to. The reaction is reversible in principle, but in cellular and biotechnological contexts it is often used in the oxidative direction to generate NAD(P)H or to consume glucose.
Why Is glucose 1-dehydrogenase [NAD(P)+] activity Important in Cell Biology?
GO:0047936 is important because it defines a catalytic activity that connects glucose oxidation to nicotinamide cofactor reduction, a reaction that is central to redox homeostasis, enzyme-coupled assays, and engineered biocatalysis. NAD(P)-dependent glucose dehydrogenases are among the most widely used enzymes in amperometric biosensors, bioelectrodes, and biofuel cells because they can oxidize glucose without oxygen and can be wired to electrodes through mediators or direct electron transfer. The same activity is used analytically, for example in glucose dehydrogenase-coupled reactions to determine glucose-6-phosphatase activity. Understanding its mechanism, regulation, and substrate specificity is therefore relevant to metabolic research, diagnostics, and synthetic biology.
• Provides a direct route from glucose oxidation to NAD(P)H generation, linking carbohydrate metabolism to cellular redox balance.
• Underpins NAD(P)-dependent glucose dehydrogenase enzymes used in amperometric biosensors and bioelectrodes for glucose monitoring.
• Enables biofuel cell designs that exploit glucose as a fuel and NAD(P)-dependent dehydrogenases as anodic catalysts.
• Supports artificial nicotinamide cofactor systems where NAD(P)H regeneration is required for continuous biotransformations.
• Is exploited in coupled enzyme assays, such as the glucose dehydrogenase-coupled determination of glucose-6-phosphatase activity.
• Serves as a model system for studying hydride transfer and cofactor-enzyme conjugation, including polyethylene glycol-NAD conjugates.
• Has microbial regulatory dimensions, as shown for pyrroloquinoline quinone-dependent glucose dehydrogenase in Pseudomonas putida KT2440.
• Is relevant to redox-related muscle biology through the broader family of glucose-6-phosphate dehydrogenase and related dehydrogenases.
• Provides a biochemical readout for glucose-6-phosphate dehydrogenase stability and activation studies.
• Offers a target for protein engineering to tune cofactor preference, thermostability, and electrode coupling.
Molecular Mechanism of glucose 1-dehydrogenase [NAD(P)+] activity
Substrate binding and recognition of beta-D-glucose
In simple terms: The enzyme first grabs beta-D-glucose and holds it in the right orientation for chemistry.
The reaction defined by GO:0047936 begins with binding of beta-D-glucose in the active site of a glucose dehydrogenase enzyme. The enzyme must discriminate the C1 hydroxyl group of the sugar and position it near the nicotinamide cofactor so that hydride transfer can occur. NAD(P)-dependent glucose dehydrogenases are known to accept beta-D-glucose as a substrate and to use either NAD+ or NADP+ as the electron acceptor, which is reflected in the [NAD(P)+] designation of the term. The specificity for the beta-anomer and the ability to use both cofactors are key features that distinguish this activity from other glucose-oxidizing enzymes.
Hydride transfer and cofactor reduction
In simple terms: The enzyme removes a hydride from glucose and places it onto NAD(P)+, making NAD(P)H.
Once beta-D-glucose is bound, the enzyme catalyzes hydride transfer from the C1 position of the sugar to the nicotinamide ring of NAD(P)+, yielding D-glucono-1,5-lactone and NAD(P)H. This step is the chemical heart of GO:0047936 and is responsible for the oxidoreductase classification. Studies with engineered cofactor-enzyme conjugates, such as glucose-dehydrogenase-polyethylene glycol NAD conjugates, have provided evidence for intramolecular hydride transfer and anchimeric assistance in this reaction. The reduced cofactor NAD(P)H produced in this step can then be used in downstream redox reactions or regenerated in artificial cofactor systems.
Cofactor preference and NAD(P)+ usage
In simple terms: Some versions of the enzyme prefer NAD+ and others prefer NADP+, and the term covers both.
The [NAD(P)+] notation in GO:0047936 indicates that the activity can use either NAD+ or NADP+ as the electron acceptor. This dual cofactor usage is important because NADH and NADPH serve different cellular roles, and enzymes with different cofactor preferences can be matched to specific biotechnological or analytical needs. Artificial nicotinamide cofactor systems have been developed to boost cofactor recycling and to support NAD(P)-dependent dehydrogenases in continuous operation. Understanding cofactor preference is therefore a major goal in enzyme engineering for biosensors and biofuel cells.
Product formation and reversibility
In simple terms: The reaction makes a lactone and NAD(P)H, and in principle it can run backward.
The immediate products of GO:0047936 are D-glucono-1,5-lactone and NAD(P)H. The lactone can spontaneously or enzymatically hydrolyze to gluconate, depending on the system, but the GO term itself describes the dehydrogenation step. Because the reaction is an oxidoreduction, it is thermodynamically reversible, and the direction observed in a given experiment depends on substrate and product concentrations, pH, and cofactor ratios. In biosensor and biofuel cell applications, the oxidative direction is typically favored to generate electrons from glucose.
Regulation and environmental control in microbes
In simple terms: In bacteria, the amount and activity of glucose dehydrogenases can change with growth conditions.
Glucose dehydrogenase activity is not always constitutive; in the model rhizosphere bacterium Pseudomonas putida KT2440, pyrroloquinoline quinone-dependent glucose dehydrogenase activity is regulated in response to environmental and metabolic signals. Although pyrroloquinoline quinone-dependent enzymes are distinct from NAD(P)-dependent glucose dehydrogenases, this example illustrates that glucose-oxidizing activities are subject to physiological control. In eukaryotic systems, related dehydrogenases such as glucose-6-phosphate dehydrogenase are regulated during exercise and muscle maintenance, highlighting the broader theme that glucose dehydrogenase family activities are integrated into metabolic and redox regulation.
Analytical coupling and assay design
In simple terms: The NAD(P)H produced by this activity can be measured to detect other reactions.
Because GO:0047936 produces NAD(P)H, it can be coupled to downstream detection systems. A classic example is the determination of glucose-6-phosphatase activity using the glucose dehydrogenase-coupled reaction, in which the glucose dehydrogenase step provides a measurable signal. This coupling strategy is widely used in clinical and research assays where NAD(P)H formation is monitored spectrophotometrically or electrochemically. The same principle underlies the use of NAD(P)-dependent glucose dehydrogenases in biosensor electrodes, where electron transfer from the enzyme to an electrode is transduced into a current.
Key Genes Involved in GO:0047936 glucose 1-dehydrogenase [NAD(P)+] activity
The following genes and proteins are representative of the enzymes, cofactor systems, and regulatory contexts associated with GO:0047936 and related glucose dehydrogenase activities.
| Gene | Major Role | Research Relevance |
|---|---|---|
| GDH (bacterial glucose dehydrogenase) | Catalyzes oxidation of beta-D-glucose with NAD(P)+ as acceptor | Model enzyme for GO:0047936 mechanism and biosensor development |
| PQQ-GDH (pyrroloquinoline quinone-dependent glucose dehydrogenase) | Oxidizes glucose using pyrroloquinoline quinone cofactor | Studied for regulation in Pseudomonas putida KT2440 |
| G6PD (glucose-6-phosphate dehydrogenase) | Generates NADPH in the pentose phosphate pathway | Related dehydrogenase studied in muscle frailty and exercise |
| NAD(P)+ cofactor pool (not a gene) | Provides the electron acceptor for the reaction | Engineered in artificial nicotinamide cofactor systems |
| NAD(P)H oxidase / recycling enzymes | Regenerate NAD(P)+ or consume NAD(P)H | Used in coupled assays and cofactor recycling |
| Glucose-6-phosphatase (G6PC) | Hydrolyzes glucose-6-phosphate | Measured using glucose dehydrogenase-coupled reactions |
| Polyethylene glycol-NAD conjugate systems | Engineered cofactor-enzyme conjugates | Used to study intramolecular hydride transfer |
| Glucose dehydrogenase from thermophilic sources | Thermostable glucose oxidation | Candidate for robust biosensors and biofuel cells |
| Glucose dehydrogenase from fungal sources | NAD(P)-dependent glucose oxidation | Potential source of enzymes with altered cofactor preference |
| Glucose dehydrogenase from insect sources | Glucose oxidation in specialized tissues | Comparative enzymology of GO:0047936 |
| Glucose dehydrogenase from mammalian sources | Glucose oxidation in metabolic tissues | Relevant to redox balance and glucose homeostasis |
| NAD kinase (NADK) | Phosphorylates NAD+ to NADP+ | Supplies NADP+ for NADP-dependent dehydrogenases |
| NADH/NADPH transhydrogenases | Interconvert NADH and NADPH | Modulate cofactor availability for GO:0047936 |
| Electron transfer mediators (e.g., ferrocene derivatives) | Shuttle electrons from enzyme to electrode | Used in amperometric glucose biosensors |
| Redox-sensitive transcription factors | Regulate expression of glucose-oxidizing enzymes | Link environmental signals to glucose dehydrogenase activity |
| Glucose-6-phosphate dehydrogenase regulatory proteins | Modulate G6PD stability and activity | Studied in muscle damage and frailty |
| Pentose phosphate pathway enzymes | Consume NADP+ and produce NADPH | Metabolic context for related dehydrogenases |
| Exercise-responsive metabolic regulators | Adapt muscle redox metabolism | Relevant to G6PD regulation during exercise |
How Is glucose 1-dehydrogenase [NAD(P)+] activity Regulated?
Regulation of glucose 1-dehydrogenase [NAD(P)+] activity occurs at several levels. In bacteria, the expression and activity of glucose dehydrogenases can be controlled by environmental conditions; for example, pyrroloquinoline quinone-dependent glucose dehydrogenase activity in Pseudomonas putida KT2440 is regulated in response to the rhizosphere environment. In eukaryotic systems, related dehydrogenases such as glucose-6-phosphate dehydrogenase are regulated during exercise and in muscle maintenance, with effects on redox balance and muscle damage. Cofactor availability also regulates flux through GO:0047936, because the reaction requires NAD(P)+ and produces NAD(P)H; artificial nicotinamide cofactor systems have been developed to manipulate this balance. Finally, enzyme stability and activation state can be modulated, as shown historically for glucose-6-phosphate dehydrogenase stability, activation, and inactivation.
glucose 1-dehydrogenase [NAD(P)+] activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| G6PD | Muscle frailty and damage | Knockout or overexpression in mouse muscle models |
| G6PD | Exercise-induced oxidative stress | Exercise-trained rodent models with G6PD modulation |
| G6PC | Glycogen storage disease type I | Glucose dehydrogenase-coupled enzyme assay in liver samples |
| GDH (bacterial) | Biofilm and rhizosphere colonization | Pseudomonas putida KT2440 mutants |
| NAD(P) cofactor systems | Redox imbalance in engineered cells | Artificial cofactor supplementation in cell culture |
Redox imbalance and muscle frailty
Glucose-6-phosphate dehydrogenase, a related dehydrogenase that shares the theme of glucose oxidation and NADPH production, has been linked to the onset of frailty and muscle damage. Studies in animal models show that glucose-6-phosphate dehydrogenase delays the onset of frailty by protecting against muscle damage. This suggests that dehydrogenases in the glucose oxidation family, including those related to GO:0047936, may influence age-related muscle decline through redox mechanisms.
Exercise and oxidative stress
Glucose-6-phosphate dehydrogenase is an antioxidant enzyme with regulatory functions in skeletal muscle during exercise. Its activity helps maintain NADPH pools that support antioxidant defenses. Although GO:0047936 specifically describes NAD(P)-dependent glucose 1-dehydrogenase activity, the broader principle that glucose-oxidizing dehydrogenases contribute to redox homeostasis is relevant to exercise physiology and oxidative stress research.
Diagnostic and metabolic disorders
Glucose dehydrogenase-coupled reactions are used to measure glucose-6-phosphatase activity, which is important in the diagnosis of metabolic disorders such as glycogen storage diseases. This analytical application links GO:0047936 to clinical biochemistry, because the activity provides a sensitive readout of upstream metabolic reactions. In addition, glucose dehydrogenase enzymes are used in biosensors for diabetes management, where accurate glucose measurement is essential.
Biotechnological and biofuel applications
NAD(P)-dependent glucose dehydrogenases are central to the development of bioelectrodes and biofuel cells, where they catalyze glucose oxidation at the anode. Deficiencies or alterations in enzyme activity can affect the performance of these devices, and engineering efforts aim to improve stability, cofactor preference, and electron transfer. Artificial nicotinamide cofactor systems further expand the biotechnological potential of this activity by enabling cofactor recycling.
From glucose 1-dehydrogenase [NAD(P)+] activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of a candidate glucose dehydrogenase gene alter glucose oxidation? | CRISPR knockout cell line or animal model |
| Does a specific point mutation change cofactor preference from NAD+ to NADP+? | CRISPR point-mutation knock-in |
| Can a tagged glucose dehydrogenase be used to monitor localization and interactions? | Tagged knock-in with fluorescent or affinity tag |
| Does overexpression of a glucose dehydrogenase increase NAD(P)H production? | CRISPR overexpression or stable transgenic line |
| Which genes regulate glucose dehydrogenase expression in bacteria? | Transposon or CRISPR interference library screening |
| Can engineered cofactor systems improve glucose dehydrogenase-coupled assays? | In vitro enzyme assays with artificial nicotinamide cofactors |
How to Study the glucose 1-dehydrogenase [NAD(P)+] activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| NAD(P)H absorbance assay | Increase in NAD(P)H at 340 nm | Kinetic characterization of glucose dehydrogenase |
| Coupled enzyme assay | NAD(P)H production linked to upstream reaction | Glucose-6-phosphatase activity determination |
| Amperometric biosensor | Electron transfer from enzyme to electrode | Glucose sensing and biofuel cell development |
| Site-directed mutagenesis | Effect of specific residues on catalysis | Mechanistic studies of hydride transfer |
| Cofactor conjugate chemistry | Intramolecular hydride transfer | Probing anchimeric assistance |
| Reporter gene fusion | Promoter activity of glucose dehydrogenase genes | Regulation studies in bacteria |
| CRISPR knockout screening | Gene requirement for glucose oxidation | Identifying novel regulators |
| Protein overexpression and purification | Enzyme yield and purity | Structural and biochemical studies |
Enzymatic activity assays
The most direct way to study GO:0047936 is to measure the formation of NAD(P)H spectrophotometrically at 340 nm or by fluorescence. Glucose dehydrogenase-coupled reactions are widely used, for example to determine glucose-6-phosphatase activity. These assays can be adapted to high-throughput formats for screening enzyme variants or inhibitors.
Electrochemical biosensor platforms
NAD(P)-dependent glucose dehydrogenases are commonly studied using amperometric electrodes, where electron transfer from the enzyme to the electrode is measured as current. Mediators such as ferrocene derivatives or direct electron transfer strategies can be used. These platforms are relevant for biosensor and biofuel cell development.
Protein engineering and cofactor conjugates
Site-directed mutagenesis and chemical conjugation can be used to probe the mechanism of hydride transfer. For example, glucose-dehydrogenase-polyethylene glycol NAD conjugates have been used to study intramolecular reactions and anchimeric assistance. Such approaches help identify residues involved in substrate binding and catalysis.
Microbial genetics and regulation studies
In bacteria such as Pseudomonas putida KT2440, reporter fusions, mutant libraries, and growth phenotyping can reveal how glucose dehydrogenase activity is regulated. These methods are useful for understanding the physiological role of glucose oxidation in environmental niches.
How CRISPR Can Be Used to Study GO:0047936 glucose 1-dehydrogenase [NAD(P)+] activity
Knockout
CRISPR knockout can be used to eliminate a candidate glucose dehydrogenase gene and measure the loss of GO:0047936 activity in cells or lysates. This approach helps determine whether a specific gene is responsible for glucose-dependent NAD(P)H production. Knockout models are also useful for studying the physiological consequences of losing glucose oxidation capacity.
Point Mutation
Point mutations can be introduced into the active site of a glucose dehydrogenase to test the role of specific residues in substrate binding or hydride transfer. For example, mutating a residue predicted to interact with the C1 hydroxyl of beta-D-glucose can reveal its contribution to catalysis. Such experiments provide mechanistic insight into GO:0047936.
Knock-in
Knock-in of a tagged version of a glucose dehydrogenase allows researchers to track its localization, interactions, and stability in living cells. This is particularly useful for enzymes that may be membrane-associated or secreted. Tagged knock-in models can also be used to purify the enzyme for biochemical assays.
Overexpression
Overexpression of a glucose dehydrogenase gene can increase flux through GO:0047936, leading to higher NAD(P)H levels. This is useful for biotechnological applications such as cofactor regeneration and for studying the downstream effects of redox imbalance. Overexpression models can also be used to produce sufficient enzyme for structural studies.
How EDITGENE Supports glucose 1-dehydrogenase [NAD(P)+] activity Research
Researchers studying glucose 1-dehydrogenase [NAD(P)+] activity-related genes often need to determine whether a candidate gene is causally involved in glucose oxidation, cofactor balance, or related disease phenotypes. EDITGENE provides CRISPR-based cell models and screening services to test these hypotheses directly, from knockout to precise point mutations and tagged knock-ins.
Contact EDITGENE today to design your custom CRISPR model for glucose 1-dehydrogenase [NAD(P)+] activity research.
Frequently Asked Questions About glucose 1-dehydrogenase [NAD(P)+] activity
What is glucose 1-dehydrogenase [NAD(P)+] activity?
It is the enzyme activity defined by GO:0047936 that catalyzes the oxidation of beta-D-glucose to D-glucono-1,5-lactone while reducing NAD+ or NADP+ to NAD(P)H.
What is the GO ID for glucose 1-dehydrogenase [NAD(P)+] activity?
The Gene Ontology ID is GO:0047936, and it belongs to the molecular_function ontology.
What reaction does GO:0047936 catalyze?
It catalyzes beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H.
What genes are involved in glucose 1-dehydrogenase [NAD(P)+] activity?
Genes encoding NAD(P)-dependent glucose dehydrogenases, as well as related dehydrogenases such as G6PD and bacterial PQQ-GDH, are relevant to this activity.
What are the synonyms for GO:0047936?
Synonyms include beta-D-glucose:NAD(P)+ 1-oxidoreductase activity, D-glucose dehydrogenase (NAD(P)), and hexose phosphate dehydrogenase activity.
How is glucose 1-dehydrogenase activity measured?
It is commonly measured by monitoring NAD(P)H formation at 340 nm, by coupled enzyme assays, or by amperometric biosensors.
Why are NAD(P)-dependent glucose dehydrogenases important in biosensors?
They can oxidize glucose without oxygen and transfer electrons to electrodes, making them ideal for amperometric glucose sensors and biofuel cells.
Can glucose dehydrogenase be used to measure other enzyme activities?
Yes, glucose dehydrogenase-coupled reactions are used, for example, to determine glucose-6-phosphatase activity.
How is glucose dehydrogenase activity regulated in bacteria?
In Pseudomonas putida KT2440, pyrroloquinoline quinone-dependent glucose dehydrogenase activity is regulated in response to environmental conditions.
What CRISPR models are available to study GO:0047936?
Knockout, point-mutation, knock-in, tagged knock-in, and overexpression models can be generated to study glucose dehydrogenase genes and their functions.
Conclusion
GO:0047936, glucose 1-dehydrogenase [NAD(P)+] activity, defines a fundamental oxidoreductase reaction that links glucose oxidation to NAD(P)H production. Its importance spans basic enzymology, microbial physiology, clinical assays, and biotechnological devices such as biosensors and biofuel cells. Continued research into its mechanism, regulation, and engineering potential will benefit from precise CRISPR models and rigorous biochemical assays.
References
- 1. Stolarczyk K et al.. 2020. NAD(P)-dependent glucose dehydrogenase: Applications for biosensors, bioelectrodes, and biofuel cells.. Bioelectrochemistry 135:107574 PMID: 32498025
- 2. Zachos I et al.. 2022. Boosting artificial nicotinamide cofactor systems.. Chem Commun (Camb) 58(85):11945-11948 PMID: 36200889
- 3. Arc-Chagnaud C et al.. 2021. Glucose 6-P dehydrogenase delays the onset of frailty by protecting against muscle damage.. J Cachexia Sarcopenia Muscle 12(6):1879-1896 PMID: 34704386
- 4. García-Domínguez E et al.. 2022. Glucose 6-P Dehydrogenase-An Antioxidant Enzyme with Regulatory Functions in Skeletal Muscle during Exercise.. Cells 11(19) PMID: 36231003
- 5. An R et al.. 2016. Regulation of Pyrroloquinoline Quinone-Dependent Glucose Dehydrogenase Activity in the Model Rhizosphere-Dwelling Bacterium Pseudomonas putida KT2440.. Appl Environ Microbiol 82(16):4955-64 PMID: 27287323
- 6. MARKS PA. 1961. Glucose-6-P dehydrogenase stability, activation, and inactivation.. Cold Spring Harb Symp Quant Biol 26:343-5 PMID: 14470063
- 7. Nakamura A et al.. 1986. Anchimeric assistance in the intramolecular reaction of glucose-dehydrogenase-polyethylene glycol NAD conjugate.. J Biol Chem 261(36):16792-4 PMID: 3097012
- 8. Alegre M et al.. 1988. Determination of glucose-6-phosphatase activity using the glucose dehydrogenase-coupled reaction.. Anal Biochem 173(1):185-9 PMID: 2847588
