GO:0036219 GTP diphosphatase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0036219 GTP diphosphatase activity is a molecular_function defined as catalysis of GTP + H2O = GMP + H+ + diphosphate, i.e. hydrolysis of GTP to GMP and pyrophosphate rather than to GDP and orthophosphate.
• The reaction is a pyrophosphohydrolase (diphosphatase) activity, mechanistically distinct from classical GTPase (GTP to GDP) and from nucleoside diphosphate kinase chemistry.
• Enzymes with this activity include Nudix-family hydrolases such as Ntdp from Staphylococcus aureus, whose structures reveal the basis for nucleoside tri- and diphosphate hydrolysis.
• Guanosine diphosphatase activities have been biochemically characterized in mammalian tissues, including calf liver microsomal salt-wash proteins and rodent brain and liver preparations [3,4].
• GTP diphosphatase chemistry is linked to membrane trafficking and fusion, because GTP-dependent targeting and fusion of ER-derived transport vesicles with yeast Golgi membranes requires hydrolyzable GTP and specific protein factors.
• The activity intersects with oxidative stress signaling, as the yeast GTP-binding protein Gtr1p is involved in the oxidative stress response.
Description
GTP diphosphatase activity (GO:0036219) is a molecular_function describing the catalysis of the reaction GTP + H2O = GMP + H+ + diphosphate. In contrast to canonical GTPases, which cleave GTP to GDP and inorganic phosphate, this activity removes pyrophosphate from GTP, releasing GMP and diphosphate. This distinction matters because the products and energetic consequences of the two routes differ, and because enzymes annotated with this activity participate in nucleotide homeostasis, membrane trafficking and stress responses [7,8]. The term is therefore of interest to researchers studying nucleotide metabolism, vesicle transport and cellular stress signaling [1,8]. Biochemical studies of guanosine diphosphatase and related activities have been reported in mammalian systems, including a purified guanosine diphosphatase from calf liver microsomal salt wash proteins and measurements of guanosine diphosphatase and guanosine triphosphatase activity in rat brain and liver under radiation injury. These early reports established that distinct enzyme activities can hydrolyze guanosine nucleotides at the diphosphate or triphosphate level, providing a foundation for later molecular and structural work [3,4]. More recent structural and mechanistic work on Nudix hydrolases, such as Ntdp from Staphylococcus aureus, has clarified how a single enzyme scaffold can accommodate both nucleoside triphosphate and nucleoside diphosphate substrates. In parallel, cell biological studies have shown that GTP hydrolysis is required for targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes, linking guanosine nucleotide chemistry to membrane traffic. Together, these findings make GO:0036219 a useful entry point for interrogating nucleotide hydrolase function in health and disease [7,8].
GTP diphosphatase activity At A Glance
| GO ID | GO:0036219 |
|---|---|
| GO term | GTP diphosphatase activity |
| Ontology | molecular_function |
| Definition | Catalysis of the reaction: GTP + H2O = GMP + H+ + diphosphate. |
| Synonym | GTP diphosphohydrolase activity; GTP diphosphohydrolase (diphosphate-forming); guanosine 5'-triphosphate pyrophosphohydrolase; GTP pyrophosphatase activity |
| Major function | Hydrolysis of GTP to GMP and diphosphate, contributing to guanosine nucleotide homeostasis and to GTP-dependent cellular processes. |
| Reaction direction | Hydrolytic; consumes water and GTP, releases GMP, H+ and diphosphate. |
| Representative enzyme family | Nudix hydrolases and related pyrophosphohydrolases, exemplified by Ntdp from Staphylococcus aureus. |
| Related biochemical activities | Guanosine diphosphatase and guanosine triphosphatase activities measured in mammalian tissues [3,4]. |
What Is GO:0036219?
GO:0036219 GTP diphosphatase activity is defined in QuickGO as catalysis of the reaction GTP + H2O = GMP + H+ + diphosphate. In other words, the enzyme uses water to split GTP into GMP and diphosphate (pyrophosphate), rather than producing GDP and orthophosphate. Synonyms include GTP diphosphohydrolase activity, GTP diphosphohydrolase (diphosphate-forming), guanosine 5'-triphosphate pyrophosphohydrolase and GTP pyrophosphatase activity. The term belongs to the molecular_function ontology aspect and describes a catalytic capability rather than a location or a pathway.
Why Is GTP diphosphatase activity Important in Cell Biology?
GTP diphosphatase activity matters because it defines a specific route of guanosine nucleotide breakdown that is mechanistically distinct from GTPase-mediated signaling. Enzymes with this activity can influence the balance of guanosine nucleotides available for translation, signaling and membrane trafficking, and structural work on Nudix hydrolases has shown how such enzymes recognize both triphosphate and diphosphate nucleoside substrates. Cell-free studies have demonstrated that GTP hydrolysis is required for targeting and fusion of ER-derived transport vesicles with yeast Golgi membranes, placing guanosine nucleotide chemistry at the heart of secretory pathway function. In addition, the yeast GTP-binding protein Gtr1p is involved in the oxidative stress response, indicating that guanosine nucleotide metabolism and signaling intersect with stress adaptation. For researchers, GO:0036219 provides a precise annotation target for distinguishing pyrophosphohydrolase chemistry from canonical GTPase chemistry in functional genomics and drug discovery.
• Defines a distinct nucleotide hydrolysis route (GTP to GMP plus diphosphate) that is often confused with GTPase activity.
• Provides a mechanistic framework for studying Nudix-family pyrophosphohydrolases and their substrate specificity.
• Connects guanosine nucleotide metabolism to membrane trafficking and vesicle fusion at the Golgi.
• Links guanosine nucleotide-binding proteins such as Gtr1p to oxidative stress responses in yeast.
• Supports interpretation of biochemical assays that measure guanosine diphosphatase and guanosine triphosphatase activities in tissues [3,4].
• Offers a functional annotation node for comparative genomics and enzyme classification.
• Helps distinguish pyrophosphate-forming hydrolysis from orthophosphate-forming hydrolysis in enzyme kinetics.
• Relevant to studies of nucleotide homeostasis in liver and brain, where guanosine nucleotide hydrolase activities have been measured [3,4].
• Provides a conceptual bridge between nucleotide biochemistry and secretory pathway cell biology.
• Useful for designing selective inhibitors or probes that target pyrophosphohydrolase chemistry rather than classical GTPases.
Molecular Mechanism of GTP diphosphatase activity
Substrate recognition and binding of GTP
In simple terms: The enzyme first grabs GTP and positions it so that water can attack the right bond.
GTP diphosphatase activity requires binding of the guanosine triphosphate substrate in a conformation that exposes the alpha-beta phosphoanhydride bond to nucleophilic attack by water. Structural analysis of Ntdp from Staphylococcus aureus revealed features that allow the enzyme to accommodate both nucleoside triphosphates and nucleoside diphosphates, providing a structural basis for the dual tri- and diphosphate hydrolysis activity observed in this Nudix enzyme. This substrate-binding step determines whether GTP is channeled toward GMP plus diphosphate rather than toward GDP plus orthophosphate.
Catalytic hydrolysis of GTP to GMP and diphosphate
In simple terms: Water splits GTP into GMP and a pyrophosphate group.
The defining chemical event of GO:0036219 is the hydrolytic cleavage of GTP to yield GMP, a proton and diphosphate. This pyrophosphate-forming reaction is chemically distinct from the orthophosphate-forming hydrolysis catalyzed by classical GTPases. The Ntdp structure and accompanying biochemical assays demonstrated that a single enzyme can catalyze hydrolysis of both nucleoside triphosphates and nucleoside diphosphates, consistent with a mechanism in which the scissile phosphoanhydride bond is positioned for water attack. The reaction consumes water and releases GMP and diphosphate as products.
Relationship to guanosine diphosphatase and GTPase activities
In simple terms: Related enzymes can cut GTP at different positions, so assays must distinguish them.
Biochemical studies have described guanosine diphosphatase activity purified from calf liver microsomal salt wash proteins, establishing that distinct enzyme preparations can hydrolyze guanosine nucleotides at the diphosphate level. Measurements of guanosine diphosphatase and guanosine triphosphatase activity in rat brain and liver under radiation injury further illustrate that these activities can be monitored separately in tissue extracts. These reports provide historical context for distinguishing GTP diphosphatase (pyrophosphate-forming) activity from GTPase (orthophosphate-forming) activity when interpreting enzyme assays [3,4].
Cofactors, ions and assay considerations
In simple terms: The reaction needs water and the right buffer conditions, and may depend on metal ions.
The QuickGO definition specifies water as a co-substrate, with GTP converted to GMP, a proton and diphosphate. Detailed cofactor requirements for individual enzymes annotated with GO:0036219 are enzyme-specific; structural and biochemical characterization of Ntdp from Staphylococcus aureus provides an experimentally validated example of nucleoside tri- and diphosphate hydrolysis by a Nudix enzyme. When designing assays, researchers should therefore verify product formation (GMP and diphosphate) rather than assuming GDP production, because the two product profiles reflect different catalytic mechanisms.
Integration with GTP-dependent cellular processes
In simple terms: GTP chemistry powers membrane traffic and stress responses in cells.
GTP hydrolysis is required for targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes, demonstrating that guanosine nucleotide chemistry is functionally coupled to membrane trafficking. In yeast, the GTP-binding protein Gtr1p is involved in the oxidative stress response, indicating that guanosine nucleotide-binding and hydrolyzing systems participate in stress signaling. These findings place GTP diphosphatase activity within a broader network of GTP-dependent cellular processes, even though the specific contribution of pyrophosphate-forming hydrolysis to these pathways remains an active area of investigation [1,8].
Key Genes Involved in GO:0036219 GTP diphosphatase activity
The following genes and proteins are experimentally linked to guanosine nucleotide hydrolysis, GTP-dependent trafficking or GTP-binding stress responses relevant to GO:0036219.
| Gene | Major Role | Research Relevance |
|---|---|---|
| Ntdp (Staphylococcus aureus) | Nudix hydrolase with nucleoside tri- and diphosphate hydrolysis activity | Structural model for dual tri-/diphosphate hydrolysis relevant to GO:0036219 |
| Gtr1p (Saccharomyces cerevisiae) | GTP-binding protein involved in oxidative stress response | Links guanosine nucleotide signaling to stress adaptation |
| RP2p (mouse) | Peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity | Example of a nudix hydrolase with diphosphatase chemistry in peroxisomes |
| Calf liver microsomal guanosine diphosphatase | Purified guanosine diphosphatase activity from microsomal salt wash proteins | Biochemical reference for guanosine nucleotide hydrolysis at the diphosphate level |
| Rat brain guanosine diphosphatase | Tissue activity measured under radiation injury | Demonstrates tissue-level regulation of guanosine nucleotide hydrolase activity |
| Rat liver guanosine diphosphatase | Tissue activity measured under radiation injury | Provides comparative tissue data for guanosine nucleotide hydrolysis |
| Yeast Golgi fusion machinery | GTP-dependent targeting and fusion of ER-derived vesicles | Connects GTP hydrolysis to secretory pathway function |
| Fetal pig glucogenic enzymes | Developmental regulation by cortisol | Context for developmental control of metabolic enzyme activities |
| Rat liver metabolic enzymes | Effects of progesterone on fat and carbohydrate metabolism | Illustrates hormonal modulation of hepatic enzyme activities |
| Nudix hydrolase family | Pyrophosphohydrolase chemistry on nucleoside substrates | Family context for enzymes annotated with GTP diphosphatase activity |
| Peroxisomal nudix hydrolases | Diphosphatase activity in peroxisomes | Subcellular example of diphosphatase function |
| GTP-binding proteins | GTP-dependent signaling and trafficking | Broad class linking GTP chemistry to cellular processes [1,8] |
How Is GTP diphosphatase activity Regulated?
Regulation of GTP diphosphatase activity is enzyme-specific and has been studied mainly at the level of tissue activity and developmental or hormonal context. Measurements of guanosine diphosphatase and guanosine triphosphatase activity in rat brain and liver under radiation injury indicate that these activities can change in response to stress conditions. In the fetal pig, the glucogenic capacity is developmentally regulated by cortisol, illustrating how metabolic enzyme activities can be under hormonal control during development. In rat liver, progesterone affects enzymes of fat and carbohydrate metabolism, showing that steroid hormones can modulate hepatic enzyme activities. At the protein level, the yeast GTP-binding protein Gtr1p is involved in the oxidative stress response, suggesting that guanosine nucleotide-binding and hydrolyzing systems are integrated into stress-responsive regulatory networks. For enzymes annotated with GO:0036219, researchers should determine regulation empirically for each candidate, because the available literature does not support a single universal regulatory mechanism [1,4,5,6].
GTP diphosphatase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| Gtr1p | Oxidative stress response | Yeast knockout and point-mutation models to test stress sensitivity |
| Ntdp | Bacterial nucleotide metabolism | Bacterial knockout and overexpression for biochemical assays |
| RP2p | Peroxisomal metabolism | Mouse knockout or tagged knock-in to study peroxisomal diphosphatase function |
| Guanosine diphosphatase (mammalian) | Tissue response to radiation injury | Rodent tissue activity assays under stress conditions |
| Golgi trafficking machinery | Secretory pathway function | In vitro vesicle fusion assays with purified Golgi membranes |
Nucleotide metabolism and stress-related pathology
Alterations in guanosine nucleotide hydrolase activities have been observed in animal tissues under stress conditions, as shown by measurements of guanosine diphosphatase and guanosine triphosphatase activity in rat brain and liver after radiation injury. These findings suggest that dysregulation of guanosine nucleotide hydrolysis could contribute to cellular stress responses, although direct causal links to human disease remain to be established.
Membrane trafficking and secretory pathway disorders
GTP hydrolysis is required for targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes, implicating guanosine nucleotide chemistry in the fidelity of the secretory pathway. Because defects in membrane trafficking underlie several human disorders, enzymes with GTP diphosphatase activity are plausible contributors to trafficking-related pathology, but specific disease associations require further experimental validation.
Oxidative stress and cellular defense
The yeast GTP-binding protein Gtr1p is involved in the oxidative stress response, linking guanosine nucleotide signaling to cellular defense against reactive oxygen species. This connection suggests that perturbations in guanosine nucleotide metabolism could influence oxidative stress susceptibility, although the relevance to human disease remains to be determined.
Peroxisomal and metabolic enzyme dysfunction
Proteomic analysis of mouse kidney peroxisomes identified RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity, demonstrating that diphosphatase enzymes can localize to peroxisomes and participate in metabolic pathways. This provides a model for understanding how diphosphatase dysfunction might affect peroxisomal metabolism, but direct links to human peroxisomal disease require further study.
From GTP diphosphatase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is a candidate gene required for GTP diphosphatase activity in cells? | CRISPR knockout cell line with biochemical activity assay |
| Does a specific residue mediate substrate recognition? | CRISPR point-mutation knock-in of the catalytic residue |
| Where does the enzyme localize in the cell? | Tagged knock-in with fluorescent or affinity tag |
| Does overexpression alter nucleotide pools? | CRISPR overexpression cell model with nucleotide profiling |
| Does the enzyme contribute to oxidative stress resistance? | Yeast knockout or point-mutation models with stress challenge |
| Does the activity affect membrane trafficking? | In vitro vesicle fusion assays with purified Golgi membranes |
How to Study the GTP diphosphatase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Biochemical activity assay | Conversion of GTP to GMP and diphosphate | Enzyme characterization and inhibitor testing |
| Structural biology (X-ray/cryo-EM) | Substrate binding and catalytic geometry | Mechanistic studies of Nudix hydrolases |
| In vitro vesicle fusion assay | GTP-dependent targeting and fusion of ER-derived vesicles with Golgi membranes | Testing trafficking roles of candidate enzymes |
| Yeast genetics and stress assays | Growth and survival under oxidative stress | Linking guanosine nucleotide proteins to stress responses |
| Tissue enzyme activity profiling | Guanosine diphosphatase and GTPase activities in extracts | Comparative tissue studies under stress conditions |
| Protein purification from tissue | Isolation of active guanosine diphosphatase | Biochemical characterization of native enzymes |
| Proteomic analysis of organelles | Identification of diphosphatase enzymes in peroxisomes | Subcellular localization and function discovery |
| Developmental and hormonal profiling | Changes in metabolic enzyme activities | Contextual regulation studies [5,6] |
Biochemical activity assays for GTP diphosphatase
Direct measurement of GTP diphosphatase activity requires detection of GMP and diphosphate products rather than GDP and orthophosphate. Historical studies purified guanosine diphosphatase activity from calf liver microsomal salt wash proteins and measured guanosine diphosphatase and guanosine triphosphatase activities in rat tissues, providing assay frameworks that can be adapted to modern chromatography or mass spectrometry readouts [3,4]. Structural and biochemical characterization of Ntdp from Staphylococcus aureus further illustrates how product analysis can distinguish tri- and diphosphate hydrolysis.
Structural and mechanistic analysis
Structural biology approaches such as X-ray crystallography or cryo-electron microscopy can reveal how enzymes annotated with GO:0036219 bind GTP and position the scissile bond. The structural mechanism for nucleoside tri- and diphosphate hydrolysis by Ntdp from Staphylococcus aureus provides a template for understanding how a single active site can accommodate both substrate types. Such studies help define catalytic residues for subsequent CRISPR point-mutation experiments.
Cell biological assays for GTP-dependent trafficking
Because GTP hydrolysis is required for targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes, in vitro vesicle fusion assays can be used to test whether candidate GTP diphosphatases influence membrane traffic. These assays complement biochemical activity measurements and can be combined with genetic perturbation of candidate genes.
Stress response and phenotypic profiling
Phenotypic profiling under oxidative stress can reveal whether guanosine nucleotide metabolism contributes to stress resistance. The involvement of Gtr1p in the oxidative stress response in Saccharomyces cerevisiae provides a validated example of how yeast genetics can be used to link guanosine nucleotide-binding proteins to stress phenotypes. Similar approaches can be applied to candidate GTP diphosphatases using knockout or point-mutation strains.
How CRISPR Can Be Used to Study GO:0036219 GTP diphosphatase activity
Knockout
CRISPR knockout of a candidate gene is the most direct way to test whether it is required for GTP diphosphatase activity in cells. By disrupting the coding sequence, researchers can measure loss of GMP and diphosphate production from GTP and compare with wild-type cells, using biochemical assays informed by structural and mechanistic studies of Nudix hydrolases. Knockout models are also useful for testing downstream phenotypes such as oxidative stress sensitivity or membrane trafficking defects.
Point Mutation
CRISPR point mutation allows precise substitution of catalytic or substrate-binding residues identified by structural analysis. For enzymes with nucleoside tri- and diphosphate hydrolysis activity, such as Ntdp from Staphylococcus aureus, point mutations can separate triphosphate from diphosphate hydrolysis and reveal which residues are essential for GTP diphosphatase activity. This approach provides causal evidence that a specific residue mediates the reaction rather than a pleiotropic effect.
Knock-in
CRISPR knock-in of epitope or fluorescent tags enables localization and interaction studies of endogenous GTP diphosphatase enzymes. Tagged knock-in models are particularly valuable for enzymes that localize to specific organelles, as illustrated by the peroxisomal nudix hydrolase RP2p identified by proteomic analysis of mouse kidney peroxisomes. Tagging preserves endogenous regulatory context while allowing imaging and affinity purification.
Overexpression
CRISPR-mediated overexpression or cDNA-based overexpression can test whether increased levels of a candidate enzyme alter guanosine nucleotide pools or cellular phenotypes. Overexpression studies are useful for detecting gain-of-function effects and for producing sufficient enzyme for biochemical and structural analysis, as demonstrated for Nudix hydrolases with nucleoside tri- and diphosphate hydrolysis activity. Overexpression can also be combined with stress challenges to test whether the enzyme modulates oxidative stress responses.
How EDITGENE Supports GTP diphosphatase activity Research
Researchers studying GTP diphosphatase activity-related genes often need to determine whether a candidate gene is causally involved in the reaction, where the enzyme localizes, and how its activity affects cellular phenotypes such as nucleotide homeostasis, membrane trafficking or stress resistance. Answering these questions requires precise genetic models that can isolate the contribution of a single gene or residue from background activities.
Contact EDITGENE today to design your custom CRISPR model for GTP diphosphatase activity research.
Frequently Asked Questions About GTP diphosphatase activity
What is GTP diphosphatase activity?
GTP diphosphatase activity (GO:0036219) is a molecular_function defined as catalysis of the reaction GTP + H2O = GMP + H+ + diphosphate, meaning GTP is hydrolyzed to GMP and pyrophosphate rather than to GDP and orthophosphate.
What is the GO ID for GTP diphosphatase activity?
The Gene Ontology ID for GTP diphosphatase activity is GO:0036219, and it belongs to the molecular_function ontology aspect.
What genes are involved in GTP diphosphatase activity?
Genes and proteins experimentally linked to this activity or related guanosine nucleotide hydrolysis include Ntdp from Staphylococcus aureus, a Nudix hydrolase with nucleoside tri- and diphosphate hydrolysis activity, and the yeast GTP-binding protein Gtr1p involved in oxidative stress response.
How is GTP diphosphatase activity different from GTPase activity?
GTP diphosphatase activity produces GMP and diphosphate from GTP, whereas classical GTPase activity produces GDP and orthophosphate. Structural and biochemical studies of Ntdp show that a single enzyme can hydrolyze both nucleoside tri- and diphosphates, highlighting the need to measure products carefully.
Which enzymes have GTP diphosphatase activity?
Enzymes with this activity include Nudix-family pyrophosphohydrolases such as Ntdp from Staphylococcus aureus, and related guanosine diphosphatase activities have been purified from mammalian tissues such as calf liver microsomal salt wash proteins.
Is GTP diphosphatase activity involved in membrane trafficking?
GTP hydrolysis is required for targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes, linking guanosine nucleotide chemistry to membrane trafficking.
How can I measure GTP diphosphatase activity?
Activity can be measured by detecting GMP and diphosphate products from GTP, as illustrated by biochemical and structural studies of Ntdp and by tissue assays of guanosine diphosphatase and guanosine triphosphatase activities.
What diseases are linked to GTP diphosphatase activity?
Direct human disease links are not firmly established, but guanosine nucleotide hydrolase activities change under stress conditions in rodent tissues, and GTP-dependent trafficking is essential for secretory pathway function.
Can CRISPR be used to study GTP diphosphatase activity?
Yes. CRISPR knockout, point mutation, knock-in and overexpression models can be used to test the requirement, catalytic residues, localization and gain-of-function effects of candidate GTP diphosphatase enzymes.
What model organisms are used to study GTP diphosphatase activity?
Saccharomyces cerevisiae is used to study GTP-binding proteins such as Gtr1p in oxidative stress, and mammalian tissues such as calf liver and rat brain and liver have been used for biochemical measurements of guanosine nucleotide hydrolase activities [3,4].
Conclusion
GO:0036219 GTP diphosphatase activity defines a specific pyrophosphate-forming hydrolysis of GTP to GMP and diphosphate, distinct from classical GTPase chemistry. Experimental work on Nudix hydrolases, guanosine diphosphatases and GTP-dependent membrane trafficking provides a foundation for understanding its biochemical and cellular roles [3,4,7,8]. The involvement of GTP-binding proteins such as Gtr1p in oxidative stress responses further connects guanosine nucleotide metabolism to stress signaling. For researchers, precise genetic models are essential to establish causality and to distinguish GTP diphosphatase activity from related nucleotide hydrolase activities. CRISPR knockout, point-mutation, knock-in and overexpression approaches, combined with biochemical and cell biological assays, offer a rigorous path to functional annotation and to identifying disease-relevant mechanisms [7,8].
References
- 1. Sekiguchi T et al.. 2022. Involvement of Gtr1p in the oxidative stress response in yeast Saccharomyces cerevisiae.. Biochem Biophys Res Commun 598:107-112 PMID: 35158208
- 2. Ofman R et al.. 2006. Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity.. Biochem J 393(Pt 2):537-43 PMID: 16185196
- 3. Raychaudhuri P et al.. 1985. Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins.. J Biol Chem 260(14):8306-11 PMID: 2989286
- 4. Savitskiĭ. 1985. [Activity of guanosine diphosphatase and guanosine triphosphatase in the rat brain and liver under radiation injury].. Ukr Biokhim Zh (1978) 57(2):73-6 PMID: 2988171
- 5. Fowden AL et al.. 1995. The glucogenic capacity of the fetal pig: developmental regulation by cortisol.. Exp Physiol 80(3):457-67 PMID: 7640010
- 6. Dahm CH Jr et al.. 1977. Effects of progesterone on some enzymes of fat and carbohydrate metabolism in rat liver.. Am J Obstet Gynecol 129(2):130-2 PMID: 197850
- 7. Wang Z et al.. 2021. The structural mechanism for the nucleoside tri- and diphosphate hydrolysis activity of Ntdp from Staphylococcus aureus.. FEBS J 288(20):6019-6034 PMID: 33955674
- 8. Lupashin VV et al.. 1996. Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes.. J Cell Biol 132(3):277-89 PMID: 8636207
