Methylenetetrahydrofolate Dehydrogenase (NADP)
Formate-Tetrahydrofolate Ligase
Methenyltetrahydrofolate Cyclohydrolase
Aminohydrolases
Methylenetetrahydrofolate Reductase (NADPH2)
5,10-Methylenetetrahydrofolate Reductase (FADH2)
Oxidoreductases Acting on CH-NH Group Donors
Multienzyme Complexes
NAD
Folic Acid
Polymorphism, Genetic
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
Genotype
Hyperhomocysteinemia
Formate-tetrahydrofolate ligase, also known as formyltetrahydrofolate synthetase, is an enzyme that catalyzes the reaction between formate and tetrahydrofolate to form formyltetrahydrofolate. This reaction is an important step in the metabolic pathway of one-carbon metabolism, which is involved in the biosynthesis of purines, thymidylate, and methionine. The enzyme requires ATP for its activity and plays a crucial role in maintaining the cellular pool of one-carbon units. Deficiencies in this enzyme can lead to serious health consequences, including megaloblastic anemia and neurological disorders.
Methylenetetrahydrofolate cyclohydrolase is an enzyme that is involved in the metabolism of folate, a type of B vitamin. The official medical definition of this enzyme is:
"An enzyme that catalyzes the conversion of 5,6,7,8-tetrahydrofolate to 5,6,7,8-tetrahydropteroylglutamate, a reaction that involves the cleavage of the carbon-nitrogen bond of the methylene bridge and the formation of a cyclic structure."
This enzyme plays an important role in the synthesis of tetrahydrofolate, which is a cofactor involved in the transfer of one-carbon units in various metabolic reactions. Mutations in the gene that encodes this enzyme can lead to a rare inherited disorder called methylenetetrahydrofolate reductase deficiency, which can cause neurological symptoms and developmental delay.
Aminohydrolases are a class of enzymes that catalyze the hydrolysis of amide bonds and the breakdown of urea, converting it into ammonia and carbon dioxide. They are also known as amidases or urease. These enzymes play an essential role in various biological processes, including nitrogen metabolism and the detoxification of xenobiotics.
Aminohydrolases can be further classified into several subclasses based on their specificity for different types of amide bonds. For example, peptidases are a type of aminohydrolase that specifically hydrolyze peptide bonds in proteins and peptides. Other examples include ureases, which hydrolyze urea, and acylamidases, which hydrolyze acylamides.
Aminohydrolases are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They have important applications in biotechnology and medicine, such as in the production of pharmaceuticals, the treatment of wastewater, and the diagnosis of genetic disorders.
Tetrahydrofolates (THFs) are a type of folate, which is a form of vitamin B9. Folate is essential for the production and maintenance of new cells, especially in DNA synthesis and methylation. THFs are the active forms of folate in the body and are involved in various metabolic processes, including:
1. The conversion of homocysteine to methionine, an amino acid required for protein synthesis and the formation of S-adenosylmethionine (SAM), a major methyl donor in the body.
2. The transfer of one-carbon units in various metabolic reactions, such as the synthesis of purines and pyrimidines, which are essential components of DNA and RNA.
3. The remethylation of homocysteine to methionine, a process that helps maintain normal homocysteine levels in the body. Elevated homocysteine levels have been linked to an increased risk of cardiovascular disease.
THFs can be obtained from dietary sources, such as leafy green vegetables, legumes, and fortified cereals. They can also be synthesized endogenously in the body through the action of the enzyme dihydrofolate reductase (DHFR), which reduces dihydrofolate (DHF) to THF using NADPH as a cofactor.
Deficiencies in folate or impaired THF metabolism can lead to various health issues, including megaloblastic anemia, neural tube defects during fetal development, and an increased risk of cardiovascular disease due to elevated homocysteine levels.
Oxidoreductases acting on CH-NH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts on CH-NH group donors, where the CH-NH group is a chemical functional group consisting of a carbon atom (C) bonded to a nitrogen atom (N) via a single covalent bond.
These enzymes play a crucial role in various biological processes by transferring electrons from the CH-NH group donor to an acceptor molecule, which results in the oxidation of the donor and reduction of the acceptor. This process can lead to the formation or breakdown of chemical bonds, and plays a key role in metabolic pathways such as amino acid degradation and nitrogen fixation.
Examples of enzymes that fall within this class include:
* Amino oxidases, which catalyze the oxidative deamination of amino acids to produce alpha-keto acids, ammonia, and hydrogen peroxide.
* Transaminases, which transfer an amino group from one molecule to another, often in the process of amino acid biosynthesis or degradation.
* Amine oxidoreductases, which catalyze the oxidation of primary amines to aldehydes and secondary amines to ketones, with the concomitant reduction of molecular oxygen to hydrogen peroxide.
Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.
NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.
Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.
Homocysteine is an amino acid that is formed in the body during the metabolism of another amino acid called methionine. It's an important intermediate in various biochemical reactions, including the synthesis of proteins, neurotransmitters, and other molecules. However, elevated levels of homocysteine in the blood (a condition known as hyperhomocysteinemia) have been linked to several health issues, such as cardiovascular disease, stroke, and cognitive decline.
Homocysteine can be converted back to methionine with the help of vitamin B12 and a cofactor called betaine, or it can be converted to another amino acid called cystathionine with the help of vitamin B6 and folate (vitamin B9). Imbalances in these vitamins and other factors can lead to an increase in homocysteine levels.
It is crucial to maintain normal homocysteine levels for overall health, as high levels may contribute to the development of various diseases. Regular monitoring and maintaining a balanced diet rich in folate, vitamin B6, and vitamin B12 can help regulate homocysteine levels and reduce the risk of related health issues.
Folic acid is the synthetic form of folate, a type of B vitamin (B9). It is widely used in dietary supplements and fortified foods because it is more stable and has a longer shelf life than folate. Folate is essential for normal cell growth and metabolism, and it plays a critical role in the formation of DNA and RNA, the body's genetic material. Folic acid is also crucial during early pregnancy to prevent birth defects of the brain and spine called neural tube defects.
Medical Definition: "Folic acid is the synthetic form of folate (vitamin B9), a water-soluble vitamin involved in DNA synthesis, repair, and methylation. It is used in dietary supplementation and food fortification due to its stability and longer shelf life compared to folate. Folic acid is critical for normal cell growth, development, and red blood cell production."
Genetic polymorphism refers to the occurrence of multiple forms (called alleles) of a particular gene within a population. These variations in the DNA sequence do not generally affect the function or survival of the organism, but they can contribute to differences in traits among individuals. Genetic polymorphisms can be caused by single nucleotide changes (SNPs), insertions or deletions of DNA segments, or other types of genetic rearrangements. They are important for understanding genetic diversity and evolution, as well as for identifying genetic factors that may contribute to disease susceptibility in humans.
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase is also known as Methionine Synthase. It is a vital enzyme in the human body that plays a crucial role in methionine metabolism and homocysteine regulation.
The medical definition of 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase is as follows:
A enzyme (EC 2.1.1.13) that catalyzes the methylation of homocysteine to methionine, using 5-methyltetrahydrofolate as a methyl donor. This reaction also requires the cofactor vitamin B12 (cobalamin) as a coenzyme. The enzyme is located in the cytosol of cells and is essential for the synthesis of methionine, which is an important amino acid required for various biological processes such as protein synthesis, methylation reactions, and the formation of neurotransmitters.
Deficiency or dysfunction of this enzyme can lead to several health issues, including homocystinuria, a genetic disorder characterized by elevated levels of homocysteine in the blood, which can cause serious complications such as neurological damage, cardiovascular disease, and skeletal abnormalities.
Genotype, in genetics, refers to the complete heritable genetic makeup of an individual organism, including all of its genes. It is the set of instructions contained in an organism's DNA for the development and function of that organism. The genotype is the basis for an individual's inherited traits, and it can be contrasted with an individual's phenotype, which refers to the observable physical or biochemical characteristics of an organism that result from the expression of its genes in combination with environmental influences.
It is important to note that an individual's genotype is not necessarily identical to their genetic sequence. Some genes have multiple forms called alleles, and an individual may inherit different alleles for a given gene from each parent. The combination of alleles that an individual inherits for a particular gene is known as their genotype for that gene.
Understanding an individual's genotype can provide important information about their susceptibility to certain diseases, their response to drugs and other treatments, and their risk of passing on inherited genetic disorders to their offspring.
Hyperhomocysteinemia is a medical condition characterized by an excessively high level of homocysteine, an amino acid, in the blood. Generally, a level of 15 micromoles per liter (μmol/L) or higher is considered elevated.
Homocysteine is a byproduct of methionine metabolism, an essential amino acid obtained from dietary proteins. Normally, homocysteine gets converted back to methionine with the help of vitamin B12 and folate (vitamin B9), or it can be converted to another amino acid, cysteine, with the aid of vitamin B6.
Hyperhomocysteinemia can occur due to genetic defects in these enzymes, nutritional deficiencies of vitamins B12, B6, or folate, renal insufficiency, or aging. High homocysteine levels are associated with increased risks of cardiovascular diseases, including atherosclerosis, thrombosis, and stroke. It may also contribute to neurodegenerative disorders like Alzheimer's disease and cognitive decline.
It is essential to diagnose and manage hyperhomocysteinemia early to prevent potential complications. Treatment typically involves dietary modifications, supplementation of the deficient vitamins, and, in some cases, medication.
L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.
In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.
Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.
Methylenetetrahydrofolate dehydrogenase (NAD+)
MTHFD1
MTHFD2
Nicotinamide adenine dinucleotide
MTHFD2L
Chromosome 4
List of EC numbers (EC 1)
List of enzymes
List of MeSH codes (D08)
Riboflavin
List of EC numbers (EC 2)
Methylenetetrahydrofolate dehydrogenase (NAD+) - Wikipedia
SCOP 1.73: Protein: Methylenetetrahydrofolate dehydrogenase/cyclohydrolase
Transcript contig 90224 details
AKP14796 details
OT 03G02870.1 details
DeCS
The Ligandable Human Proteome
Search result - BRENDA Enzyme Database
BiGG Metabolite mlthf m in iLB1027 lipid
RCSB PDB - FAD Ligand Summary Page
ASA1 - MET8 | S. cerevisiae SSL interaction - Slorth
HALLMARK XENOBIOTIC METABOLISM
Characterizing acetogenic metabolism using a genome-scale metabolic reconstruction of Clostridium ljungdahlii | Microbial Cell...
BiGG Metabolite nadp c in iML1515
SMPDB
Bio2Vec
MA 10431989g0010 details
Nitrite reductases. Medical search
MARIKO NAITO (Graduate School of Biomedical and Health Sciences(Dentistry & Oral Health Sciences))
COMPARATIVE STUDY OF OVERLAPPING GENES IN THE GENOMES OF MYCOPLASMA HOMINIS AND MYCOPLASMA PENETRANS | INTERNATIONAL JOURNAL OF...
Princeton University - Research output - Princeton University
NWMN RS07540 - AureoWiki
Publications | Max Planck Institute of Biophysics
Browse
Nicotinamide adenine dinucleotide - wikidoc
Aminoidrolases/genética
MeSH Browser
KAKEN - Research Projects | 日・中・韓国における消化管がんの比較疫学的研究 (KAKENHI
Solyc12g005390.2.1 details
Identification of a species-specific aminotransferase in Pediococcus acidilactici capable of forming α-aminobutyrate | AMB...
Reductase3
- dehydrogenase/reductase 1 [Source:HGNC. (gsea-msigdb.org)
- Purification and structural characterization of the Na + -translocating ferredoxin: NAD + reductase (Rnf) complex of Clostridium tetanomorphum. (mpg.de)
- Journal Article] Polymorphisms in thymidylate synthase and methylenetetrahydrofolate reductase genes and the susceptibility to esophageal and stomach cancer with smoking and drinking habits. (nii.ac.jp)
NADH7
- 5,10-methylenetetrahydrofolate + NAD+ ⇌ {\displaystyle \rightleftharpoons } 5,10-methenyltetrahydrofolate + NADH + H+ Thus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NAD+, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADH, and H+. (wikipedia.org)
- The coenzyme is therefore found in two forms in cells: NAD + is an oxidizing agent - it accepts electrons from other molecules and becomes reduced , this reaction forms NADH, which can then be used as a reducing agent to donate electrons. (wikidoc.org)
- [2] Such reactions (summarized in formula below) involve the removal of two hydrogen atoms from the reactant (R), in the form of a hydride ion , and a proton (H + ). The proton is released into solution, while the reductant RH 2 is oxidized and NAD + reduced to NADH by transfer of the hydride. (wikidoc.org)
- The midpoint potential of the NAD + /NADH redox pair is −0.32 volts , which makes NADH a strong reducing agent. (wikidoc.org)
- This means the coenzyme can continuously cycle between the NAD + and NADH forms without being consumed. (wikidoc.org)
- Absorbance spectra of NAD + and NADH. (wikidoc.org)
- Both NAD + and NADH absorb strongly in the ultraviolet due to the adenine base. (wikidoc.org)
NADP2
- FLAVOPROTEIN containing siroheme and can utilize both NAD and NADP as cofactors. (lookformedical.com)
- The Hydride Transfer Process in NADP-dependent Methylene-tetrahydromethanopterin Dehydrogenase. (mpg.de)
Oxidoreductase2
- The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NAD+ oxidoreductase. (wikipedia.org)
- A NAD-dependent oxidoreductase that catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5,10-methenyl-tetrahdyrofolate. (bvsalud.org)
Nicotinamide4
- Nicotinamide adenine dinucleotide , abbreviated NAD + , is a coenzyme found in all living cells . (wikidoc.org)
- It is the β-nicotinamide diastereomer of NAD + , found in organisms. (wikidoc.org)
- From the hydride electron pair, one electron is transferred to the positively-charged nitrogen of the nicotinamide ring of NAD + , and the second hydrogen atom transferred to the carbon atom opposite this nitrogen. (wikidoc.org)
- In coenzyme A, the business end is the thiol group that becomes bound to the substrate, and in NAD + it is the nicotinamide moiety that undergoes reversible reduction and oxidation. (heresy.is)
1.151
- In enzymology, a methylenetetrahydrofolate dehydrogenase (NAD+) (EC 1.5.1.15) is an enzyme that catalyzes a chemical reaction. (wikipedia.org)
Enzyme4
- This enzyme is also called methylenetetrahydrofolate dehydrogenase (NAD+). (wikipedia.org)
- An NAD-dependent enzyme that catalyzes the oxidation of nitrite to nitrate. (uchicago.edu)
- 3. Pahlich, E. and Joy, K.W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. (qmul.ac.uk)
- The enzyme dihydroorotate dehydrogenase (DHODH) links oxidative phosphorylation to de novo synthesis of pyrimidines. (biomed.news)
Glutamate dehydrogenase2
- That means that AKG can neither be synthesized by the citrate cycle nor from glutamate since the genes encoding aconitase (EC 4.2.1.3), isocitrate dehydrogenase (EC 1.1.1.41), and glutamate dehydrogenase (EC 1.4.1.2) are not present. (springeropen.com)
- 1. Frieden, C. L -Glutamate dehydrogenase. (qmul.ac.uk)
Characterization1
- 1. Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L -glutamic acid dehydrogenase. (qmul.ac.uk)
Coenzyme3
- The coenzyme of various aerobic dehydrogenases, e.g. (rcsb.org)
- Structural basis of cyclic 1,3-diene forming acyl-coenzyme A dehydrogenases. (mpg.de)
- this related coenzyme has similar chemistry to NAD + , but has different roles in metabolism. (wikidoc.org)
Substrate1
- 1. O'Connor, R.J. and Halvorson, H. The substrate specificity of L -alanine dehydrogenase. (qmul.ac.uk)
Catalyzes1
- These reaction steps are similar to the ones used in the engineered bacteria, where either a transaminase or a dehydrogenase catalyzes the final step of AABA synthesis (Fotheringham et al. (springeropen.com)
Enzymes1
- Due to the importance of these functions, the enzymes involved in NAD + metabolism are targets for drug discovery . (wikidoc.org)
Reaction1
- In metabolism , NAD + is involved in redox reactions, carrying electrons from one reaction to another. (wikidoc.org)
Novo1
- In organisms, NAD + can be synthesized from scratch ( de novo ) from the amino acids tryptophan or aspartic acid . (wikidoc.org)
Class3
- alcohol dehydrogenase 1C (class I), ga. (gsea-msigdb.org)
- alcohol dehydrogenase 5 (class III), c. (gsea-msigdb.org)
- alcohol dehydrogenase 7 (class IV), mu. (gsea-msigdb.org)
Family1
- aldehyde dehydrogenase 2 family member. (gsea-msigdb.org)
Gene1
- We also included discovery of polymorphic forms of genes that code for enzymes that are inhibited by tungsten: xanthine dehydrogenase, sulfite oxidase ( SUOX gene), and aldehyde oxidase. (nih.gov)
Interproscan1
- Isopropylmalate dehydrogenase-like domain [Interproscan]. (ntu.edu.sg)
Enzyme that catalyzes3
- use ACYLTRANSFERASES 1973-1979, use COENZYME A & PHOSPHOLIPIDS 1973-1978 MH - 1-Pyrroline-5-Carboxylate Dehydrogenase UI - D050842 MN - D8.811.682.662.693 MS - An enzyme that catalyzes the oxidation of 1-pyrroline-5-carboxylate to L-GLUTAMATE in the presence of NAD. (nih.gov)
- HN - 2006(1983) MH - 2-Oxoisovalerate Dehydrogenase (Acylating) UI - D050645 MN - D8.811.682.657.350.825 MS - An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2-methylpropanoyl-CoA. (nih.gov)
- use ANTHRANILIC ACID 1974-1979 MH - 3-Isopropylmalate Dehydrogenase UI - D050539 MN - D8.811.682.47.500 MS - An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. (nih.gov)
Systematic1
- The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NAD+ oxidoreductase. (wikipedia.org)
Biosynthesis1
- Dihydroorotate Dehydrogenases - The dihydroorotate dehydrogenases (DHODs) catalyze the oxidation of dihydroorotate (DHO) to orotate in the de novo biosynthesis of pyrimidines. (umich.edu)
Reducing equivalents1
- However, the "new" thymidylate synthase apparently accomplishes this reduction by another mechanism, using an FAD prosthetic group and NAD(P)H as the source of reducing equivalents. (umich.edu)
Promotes1
- 15. NAD-dependent methylenetetrahydrofolate dehydrogenase inhibits oral squamous cell carcinoma cell proliferation and promotes apoptosis. (nih.gov)
Description1
- Description: A competitive ELISA for quantitative measurement of Human 17 β hydroxysteroid dehydrogenase type 6(HSD17B6) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (lotuskringpoeldijk.nl)