112893 Results for: "2,5-dioxopyrrolidin-1-yldodecanoate&amp"

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FUNCTION: Membrane-bound, calcium-inhibitable adenylyl cyclase (By similarity).
CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
SIMILARITY: Contains 2 guanylate cyclase domains.
COFACTOR: Binds 2 magnesium ions per subunit (By similarity).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

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CANT1 belongs to the apyrase family.It is a calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. The enzyme has very low activity towards ADP and even lower activity towards ATP. And it does not hydrolyze AMP and GMP.

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The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca (2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca (2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD (Zhang et al., 2003 [PubMed 12574164]).

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Adenine phosphoribosyltransferase (APRT) belongs to the purine/pyrimidine phosphoribosyltransferase family. A conserved feature of this gene is the distribution of CpG dinucleotides. This enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). It also produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in this enzyme causes 2,8-dihydroxyadenine urolithiasis. Two transcript variants encoding different isoforms have been found for this gene.Adenine phosphoribosyltransferase belongs to the purine/pyrimidine phosphoribosyltransferase family. A conserved feature of this gene is the distribution of CpG dinucleotides. This enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). It also produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in this enzyme causes 2,8-dihydroxyadenine urolithiasis. Two transcript variants encoding different isoforms have been found for this gene.

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Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.

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NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalyzing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It was shown to be induced by heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation and is involved in biological processes like stress response and sporulation resulting in formation of a cellular spore. Catalytic activity: ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+

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NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalysing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It can use both glutamine or ammonia as a nitrogen source. Catalytic activity: ATP + deamido-NAD+ + L-glutamine + H₂O = AMP + diphosphate + NAD+ + L-glutamate.

Supplier: MP Biomedicals

1,1-Dimethylbiguanide hydrochloride (Metformin) is an antidiabetic agent that reduces blood glucose levels and improves insulin sensitivity. Its metabolic effects, including the inhibition of hepatic gluconeogenesis, are mediated at least in part by activation of the LKB1-AMPK (AMP-activated protein kinase) pathway. Activation of this pathway also appears to be involved in the antiproliferative and proapoptotic actions of metformin in cancer cell lines.

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L-glutamate is the major excitatory neurotransmitter in the central nervous system and activates both ionotropic and metabotropic glutamate receptors. The metabotropic glutamate receptors are a family of G protein-coupled receptors, that have been divided into 3 groups on the basis of sequence homology, putative signal transduction mechanisms, and pharmacologic properties. GRM6 is part of Group III which is linked to the inhibition of the cyclic AMP cascade.

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Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterised by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumours (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterized by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumors (2).

Supplier: ProSci Inc.

CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. Defects in C1QTNF5 are a cause of late-onset retinal degeneration (LORD).

Supplier: Bioss

Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response.

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CTRP5 (C1qTNF-related protein 5; C1QTNF5) belongs to a highly conserved family of adiponectin paralogs. CTRP5 mediates activation of AMP-activated protein kinase (AMPK) in muscle and liver cells, thereby regulating glucose and lipid metabolism. Serum levels of CTRP5 are significantly higher in obese/diabetic animal models compared to normal controls. Furthermore, CTRP5 may be a putative biomarker for mitochondrial dysfunction. Defects in C1QTNF5 are a cause of late-onset retinal degeneration (LORD).

Supplier: Bioss

Vasopressin (AVP), the antidiuretic hormone, is a cyclic nonpeptide that is involved in the regulation of body fluid osmolality (1-3). AVP mediates its effects through a family of G-protein coupled receptors, the vasopressin receptors type V1a, V2 and V3 (also designated V1b) (1,2). The AVP receptor V1a is responsible for several functions, including blood vessel constriction, liver glycogenolysis and platelet adhesion (3). It is detected as a full length protein and a shorter protein, which results from proteolytic cleavage of its amino terminus (4). The V1a receptor is coupled to Gq/11 protein, which increases the intracellular calcium concentration (3). The human AVP receptor V2 gene maps to chromosome Xq28 and is expressed in lung and kidney (5,6). Mutations in the V2 receptor result in nephrogenic diabetes insipidus (NDI), a rare X-linked disorder characterised by the inability of the kidney to concentrate urine in response to AVP (5,7). The AVP Receptor V2 activates the Gs protein and the cyclic AMP second messenger system (7). The AVP receptor V3 is preferentially expressed in the pituitary and stimulates the release of adrenocorticotropic hormone (ACTH) in response to AVP by mobilizing intracellular calcium stores (8). AVP receptor antagonists may have potential therapeutic effects in hypertension, congestive heart failure, nephrotic syndrome and ACTH-secreting tumours (2).

Supplier: Bioss

CECR1 is a member of the adenosine and AMP deaminases family. It may act as a growth factor and have adenosine deaminase activity. It is a candidate gene for cat eye syndrome. Two transcript variants encoding distinct isoforms have been identified for this gene.Adenosine deaminase is an enzyme that is present in most tissues and exists predominantly as a monomer, although in some tissues it is associated with adenosine deaminase-binding protein. Adenosine deaminase degrades extracellular adenosine, which is toxic for lymphocytes. A novel family of growth factors that share sequence similarity to adenosine deaminase has been identified. The cat eye syndrome critical region protein (CECR) family includes CECR1, CECR2, CECR3, CECR4, CECR5, CECR6, CECR7, CECR8 and CECR9. The genes encoding CECR proteins are candidates for Cat Eye Syndrome (CES), a developmental disorder associated with the duplication of a 2 Mb region of 22q11.2. CES is characterized by the combination of coloboma of the iris and anal atresia with fistula, downslanting palpebral fissures, preauricular tags and/or pits, frequent occurrence of heart and renal malformations, and normal or near-normal mental development. CECR family members are widely expressed. Specifically, CECR1 has the highest expression in adult heart, lung, lymphoblasts and placenta. CECR2 is also involved in neurulation and chromatin remodeling. Mutations in the CECR2 gene result in neural tube defects.

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Inositol monophosphatase 2, also known as Inositol-1(or 4)-monophosphatase 2, Myo-inositol monophosphatase A2 and IMPA2, is an enzyme which belongs to the inositol monophosphatase family. IMPA2 catalyses the dephosphoylration of inositol monophosphate with cofactor Magnesium and Inhibited by high Li+ and restricted Mg2+ concentrations. IMPA2 plays an important role in phosphatidylinositol signaling. IMPA2 can use the myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. IMPA2 is a pharmacological target for lithium Li(+) action in brain, it is considered to have a role in schizophrenia and bipolar disorder.

Supplier: MP Biomedicals

IBMX has been shown to be a potent, non-specific inhibitor of adenosine 3',5'-cyclic monophosphate phosphodiesterase (cAMP PDE)4, significantly more effective than theophylline. Also inhibits cGMP phosphodiesterases. IBMX inhibits cyclic nucleotide PDE with subsequent inhibition of cyclic nucleotide hydrolysis, resulting in accumulation of cyclic AMP and guanosine 3',5'-cyclic monophosphate.

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Inositol Monophosphatase 1 (IMPA1) belongs to the inositol monophosphatase family. IMPA1 is responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides, IMPA1 can use myo-inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2-AMP as substrates. IMPA1 has been implicated as the pharmacological target for lithium action in brain. IMPA1 shows magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. In addition, IMPA1 plays a improtant role in intracellular signal transduction.

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ACSBG2 belongs to the ATP-dependent AMP-binding enzyme family, bubblegum subfamily.ACSBG2 mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. It is able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. ACSBG2 has increased ability to activate oleic and linoleic acid. It may play a role in spermatogenesis.

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Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.