Glycine Dehydrogenase
Glycine Dehydrogenase (Decarboxylating)
Glycine
Malate Dehydrogenase
Decarboxylation
Selenomonas
Isocitrate Dehydrogenase
Phosphogluconate Dehydrogenase
Glycine dehydrogenase, also known as glycine cleavage system protein P or glycine synthase, is a mitochondrial enzyme complex that plays a crucial role in the catabolism of glycine, an amino acid. This enzyme complex is composed of four separate proteins (P-protein, H-protein, T-protein, and L-protein) that work together to catalyze the reversible conversion of glycine into ammonia, carbon dioxide, and a molecule of 5,10-methylenetetrahydrofolate.
The reaction can be summarized as follows:
Glycine + Tetrahydrofolate + NAD+ ↔ Ammonia + Carbon Dioxide + Methylenetetrahydrofolate + NADH
This pathway is essential for the metabolism of glycine, and its dysfunction has been linked to several genetic disorders, such as non-ketotic hyperglycinemia, which can result in neurological impairments and other health issues.
Glycine is a simple amino acid that plays a crucial role in the body. According to the medical definition, glycine is an essential component for the synthesis of proteins, peptides, and other biologically important compounds. It is also involved in various metabolic processes, such as the production of creatine, which supports muscle function, and the regulation of neurotransmitters, affecting nerve impulse transmission and brain function. Glycine can be found as a free form in the body and is also present in many dietary proteins.
Malate Dehydrogenase (MDH) is an enzyme that plays a crucial role in the Krebs cycle, also known as the citric acid cycle or tricarboxylic acid (TCA) cycle. It catalyzes the reversible oxidation of malate to oxaloacetate, while simultaneously reducing NAD+ to NADH. This reaction is essential for energy production in the form of ATP and NADH within the cell.
There are two main types of Malate Dehydrogenase:
1. NAD-dependent Malate Dehydrogenase (MDH1): Found primarily in the cytoplasm, this isoform plays a role in the malate-aspartate shuttle, which helps transfer reducing equivalents between the cytoplasm and mitochondria.
2. FAD-dependent Malate Dehydrogenase (MDH2): Located within the mitochondrial matrix, this isoform is involved in the Krebs cycle for energy production.
Abnormal levels of Malate Dehydrogenase enzyme can be indicative of certain medical conditions or diseases, such as myocardial infarction (heart attack), muscle damage, or various types of cancer. Therefore, MDH enzyme activity is often assessed in diagnostic tests to help identify and monitor these health issues.
Decarboxylation is a chemical reaction that removes a carboxyl group from a molecule and releases carbon dioxide (CO2) as a result. In the context of medical chemistry, decarboxylation is a crucial process in the activation of certain acidic precursor compounds into their biologically active forms.
For instance, when discussing phytocannabinoids found in cannabis plants, decarboxylation converts non-psychoactive tetrahydrocannabinolic acid (THCA) into psychoactive delta-9-tetrahydrocannabinol (Δ9-THC) through the removal of a carboxyl group. This reaction typically occurs when the plant material is exposed to heat, such as during smoking or vaporization, or when it undergoes aging.
In summary, decarboxylation refers to the chemical process that removes a carboxyl group from a molecule and releases CO2, which can activate certain acidic precursor compounds into their biologically active forms in medical chemistry.
Selenomonas is a genus of gram-negative, anaerobic bacteria that are commonly found in the oral cavity and gastrointestinal tract of humans and animals. These bacteria have a unique characteristic of having curved or spiral-shaped morphology and a polar flagellum for motility. They are named after their ability to reduce selenite to elemental selenium, which gives them a characteristic red color.
Selenomonas species are often associated with dental caries and periodontal disease due to their production of acid and other virulence factors that can contribute to tissue destruction. However, they also play important roles in the breakdown of complex carbohydrates and the production of volatile sulfur compounds in the gut.
It's worth noting that while Selenomonas species are generally considered to be commensal organisms, they have been implicated in various opportunistic infections, particularly in immunocompromised individuals or those with underlying medical conditions.
Isocitrate Dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate in the presence of NAD+ or NADP+, producing NADH or NADPH respectively. This reaction occurs in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a crucial metabolic pathway in the cell's energy production and biosynthesis of various molecules. There are three isoforms of IDH found in humans: IDH1 located in the cytosol, IDH2 in the mitochondrial matrix, and IDH3 within the mitochondria. Mutations in IDH1 and IDH2 have been associated with several types of cancer, such as gliomas and acute myeloid leukemia (AML), leading to abnormal accumulation of 2-hydroxyglutarate, which can contribute to tumorigenesis.
Phosphogluconate dehydrogenase (PGD) is an enzyme that plays a crucial role in the pentose phosphate pathway, which is a metabolic pathway that supplies reducing energy to cells by converting glucose into ribose-5-phosphate and NADPH.
PGD catalyzes the third step of this pathway, in which 6-phosphogluconate is converted into ribulose-5-phosphate, with the concurrent reduction of NADP+ to NADPH. This reaction is essential for the generation of NADPH, which serves as a reducing agent in various cellular processes, including fatty acid synthesis and antioxidant defense.
Deficiencies in PGD can lead to several metabolic disorders, such as congenital nonspherocytic hemolytic anemia, which is characterized by the premature destruction of red blood cells due to a defect in the pentose phosphate pathway.
Glycine dehydrogenase (decarboxylating) - Wikipedia
Structure of the homodimeric glycine decarboxylase P-protein from Synechocystis sp. PCC 6803 suggests a mechanism for redox...
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GLDC gene: MedlinePlus Genetics
RCSB PDB - 6I35: Crystal structure of human glycine decarboxylase (P-protein) bound with pyridoxyl-glycine-5'-monophosphate
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Cleavage system P protein1
- Glycine decarboxylase also known as glycine cleavage system P protein or glycine dehydrogenase is an enzyme that in humans is encoded by the GLDC gene. (wikipedia.org)
Enzyme10
- Glycine decarboxylase (EC 1.4.4.2) is an enzyme that catalyzes the following chemical reaction: glycine + H-protein-lipoyllysine ⇌ {\displaystyle \rightleftharpoons } H-protein-S-aminomethyldihydrolipoyllysine + CO2 Thus, the two substrates of this enzyme are glycine and H-protein-lipoyllysine, whereas its two products are H-protein-S-aminomethyldihydrolipoyllysine and CO2. (wikipedia.org)
- This enzyme participates in glycine, serine and threonine metabolism. (wikipedia.org)
- Degradation of glycine is brought about by the glycine cleavage system, which is composed of four mitochondrial protein components: P protein (a pyridoxal phosphate-dependent glycine decarboxylase), H protein (a lipoic acid-containing protein), T protein (a tetrahydrofolate-requiring enzyme), and L protein (a lipoamide dehydrogenase). (wikipedia.org)
- Glycine decarboxylase, or P-protein, is a pyridoxal 5'-phosphate (PLP)-dependent enzyme in one-carbon metabolism of all organisms, in the glycine and serine catabolism of vertebrates, and in the photorespiratory pathway of oxygenic phototrophs. (nih.gov)
- PLP and the substrate glycine bind in the active site of this reduced enzyme and appear to cause further conformational changes involving a flexible surface loop. (nih.gov)
- The GLDC gene provides instructions for making an enzyme called glycine dehydrogenase. (medlineplus.gov)
- When an altered version of this enzyme is incorporated into the glycine cleavage system, it impairs the system's ability to break down glycine. (medlineplus.gov)
- 3. Pahlich, E. and Joy, K.W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. (qmul.ac.uk)
- What enzyme decarboxylates the α-keto acids of branched-chain amino acids? (flashcardmachine.com)
- OMP is then decarboxylated by the enzyme OMP decarboxylase to yield uridine monophosphate (UMP). (biologyonline.com)
GLDC4
- Glycine encephalopathy is due to defects in GLDC or AMT of the glycine cleavage system. (wikipedia.org)
- Other mutations insert or delete genetic material in the GLDC gene, or disrupt how genetic information from the gene is spliced together to make a blueprint for producing glycine dehydrogenase. (medlineplus.gov)
- Some GLDC gene mutations lead to the production of a nonfunctional version of glycine dehydrogenase, while other mutations reduce but do not eliminate the enzyme's activity. (medlineplus.gov)
- Conter C, Rolland MO, Cheillan D, Bonnet V, Maire I, Froissart R. Genetic heterogeneity of the GLDC gene in 28 unrelated patients with glycine encephalopathy. (medlineplus.gov)
Encephalopathy1
- Applegarth DA, Toone JR. Glycine encephalopathy (nonketotic hyperglycinemia): comments and speculations. (medlineplus.gov)
Decarboxylase Complex1
- It is one of four components of the glycine decarboxylase complex. (ucdenver.edu)
Glutamate dehydrogenase3
- 1. Frieden, C. L -Glutamate dehydrogenase. (qmul.ac.uk)
- Ammonia incorporation in animals occurs through the actions of glutamate dehydrogenase and glutamine synthase. (medmuv.com)
- A pair of principal enzymes, glutamate dehydrogenase and glutamine synthatase, are found in all organisms and effect the conversion of ammonia into the amino acids glutamate and glutamine, respectively. (medmuv.com)
Pyruvate2
- As a therapeutic, its principal mechanism of action is to inhibit pyruvate dehydrogenase kinase (PDK). (srcinhibitors.com)
- In turn, PDK inhibits the key mitochondrial energy homeostat, pyruvate dehydrogenase complex (PDC), by reversible phosphorylation. (srcinhibitors.com)
Nonketotic hyperglycinemia1
- 1981). "Defective glycine cleavage system in nonketotic hyperglycinemia. (wikipedia.org)
Mitochondrial2
- The mitochondrial glycine cleavage system. (wikipedia.org)
- Lastly , the dihydroorotate is oxidized by dihydroorotate dehydrogenase (an integral membrane protein in the inner mitochondrial membrane ) to convert into orotate . (biologyonline.com)
Amino5
- The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor. (wikipedia.org)
- Glycine is an amino acid, which is a building block of proteins. (medlineplus.gov)
- Many of these genetic changes alter single amino acids in glycine dehydrogenase. (medlineplus.gov)
- IMP, in turn, is produced from a pre-existing ribose phosphate that forms mainly from the amino acids glycine , glutamine , and aspartic acid . (biologyonline.com)
- Subsequently, L -DOPA is decarboxylated to DA by aromatic amino acid decarboxylase [ 21 ]. (biomedcentral.com)
Enzymes2
- This protein is one of four enzymes that work together in a group called the glycine cleavage system. (medlineplus.gov)
- Enzymes of neuronal energetic pathways, such as aspartate aminotransferase (AST), alanine aminotransferase (ALT), and lactate dehydrogenase (LDH), were also evaluated. (hindawi.com)
Alanine1
- 1. O'Connor, R.J. and Halvorson, H. The substrate specificity of L -alanine dehydrogenase. (qmul.ac.uk)
Degradation1
- The glycine cleavage system catalyzes the degradation of glycine. (wikipedia.org)
Molecular1
- The observation of the disulfide bond that acts to stabilize the closed form suggests a molecular mechanism for the redox-dependent activation of glycine decarboxylase observed earlier. (nih.gov)
Ensembl2
- Acyl-CoA dehydrogenase [Ensembl]. (ntu.edu.sg)
- Possible acyl-CoA dehydrogenase FadE19 (MMGC) [Ensembl]. (ntu.edu.sg)
Disulfide1
- The presence of the disulfide bridge isolates the active site from solvent and hinders the binding of PLP and glycine in the active site. (nih.gov)
Cysteine1
- Cysteine sulfinic acid, in turn, is decarboxylated by sulfinoalanine decarboxylase to form hypotaurine . (cloudfront.net)
Liver1
- It is conjugated to GLYCINE in the liver and excreted as hippuric acid. (lookformedical.com)
Tissues1
- As a result, excess glycine can build up in the body's organs and tissues. (medlineplus.gov)
Suggests1
- As its name suggests, the glycine cleavage system breaks down a molecule called glycine by cutting (cleaving) it into smaller pieces. (medlineplus.gov)
Yield1
- Hypotaurine is enzymatically oxidized to yield taurine by hypotaurine dehydrogenase . (cloudfront.net)
Normal1
- The breakdown of excess glycine when it is no longer needed is necessary for the normal development and function of nerve cells in the brain. (medlineplus.gov)
Cleavage9
- Glycine decarboxylase is the P-protein of the glycine cleavage system in eukaryotes. (wikipedia.org)
- The glycine cleavage system catalyzes the degradation of glycine. (wikipedia.org)
- The glycine cleavage system. (wikipedia.org)
- 1981). "Defective glycine cleavage system in nonketotic hyperglycinemia. (wikipedia.org)
- This protein is one of four enzymes that work together in a group called the glycine cleavage system. (medlineplus.gov)
- As its name suggests, the glycine cleavage system breaks down a molecule called glycine by cutting (cleaving) it into smaller pieces. (medlineplus.gov)
- The breakdown of glycine by the glycine cleavage system produces a molecule called a methyl group. (medlineplus.gov)
- When an altered version of this enzyme is incorporated into the glycine cleavage system, it impairs the system's ability to break down glycine. (medlineplus.gov)
- Nonketotic hyperglycinemia (NKH) is the inborn error of glycine metabolism defined by deficient activity of the glycine cleavage enzyme system (GCS), which results in accumulation of large quantities of glycine in all body tissues including the brain. (nih.gov)
Decarboxylase complex2
Pyruvate dehydrogenase1
- The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex. (yeastrc.org)
Synthase1
- Ammonia incorporation in animals occurs through the actions of glutamate dehydrogenase and glutamine synthase. (tdmuv.com)
GcvP1
- DE Glycine dehydrogenase (decarboxylating) [gcvP]. (expasy.org)
Pyridoxal phosphate1
- The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor. (wikipedia.org)
Gene1
- The protein encoded by this gene is the P protein, which binds to glycine and enables the methylamine group from glycine to be transferred to the T protein. (nih.gov)
Tissues1
- As a result, excess glycine can build up in the body's organs and tissues. (medlineplus.gov)
Components1
- GSH that the substrate of GST and its components including glutamic acid, cysteine and glycine accumulated in transgenic rice. (bvsalud.org)
Body1
- This condition is characterized by abnormally high levels of glycine in the body (hyperglycinemia). (medlineplus.gov)
Brain1
- The breakdown of excess glycine when it is no longer needed is necessary for the normal development and function of nerve cells in the brain. (medlineplus.gov)
Current1
- Current treatment is reduction of plasma concentration of glycine by administration of sodium benzoate and blockade of overstimulated NMDA receptors. (nih.gov)