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Betaine—homocysteine S-methyltransferase
In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively: * Trimethylglycine (methyl donor) + homocysteine (hydrogen donor) → dimethylglycine (hydrogen receiver) + methionine (methyl receiver) This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. This enzyme participates in the metabolism of glycine, serine, threonine and also methionine. Isozymes In humans, there are two isozymes, BHMT and BHMT2, each encoded by a separate gene. Tissue distribution BHMT is expressed most predominantly in the liver and kidney. Clinical significance Mutations in the BHMT gene are known to exist in humans. Anomalies may influence the metabolism of homocysteine, which ...
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Enzymology
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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Serine
Serine (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated − form under biological conditions), a carboxyl group (which is in the deprotonated − form under biological conditions), and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC. Occurrence This compound is one of the proteinogenic amino acids. Only the L- stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. Its name is derived from the Latin for silk, '' sericum''. Serine's structure was established in ...
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Betaine
A betaine () in chemistry is any neutral chemical compound with a positively charged cationic functional group that bears no hydrogen atom, such as a Quaternary ammonium cation, quaternary ammonium or phosphonium cation (generally: Onium compounds, onium ions), and with a negatively charged functional group, such as a carboxylate group that may not be adjacent to the cationic site. Historically, the term was reserved for trimethylglycine (TMG), which is involved in methylation reactions and detoxification of homocysteine. This is a modified amino acid consisting of glycine with three methyl groups serving as methyl donor for various metabolic pathways. Pronunciation The pronunciation of the compound reflects its origin and first isolation from sugar ''beets'' (''Beta vulgaris'' subsp. ''vulgaris''), and does not derive from the Greek letter beta (β). It is commonly pronounced ''beta-INE'' or ''BEE-tayn''. Glycine betaine The original betaine, ''N'',''N'',''N''-trimethyl ...
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Spina Bifida
Spina bifida (SB; ; Latin for 'split spine') is a birth defect in which there is incomplete closing of the vertebral column, spine and the meninges, membranes around the spinal cord during embryonic development, early development in pregnancy. There are three main types: spina bifida occulta, meningocele and myelomeningocele. Meningocele and myelomeningocele may be grouped as spina bifida cystica. The most common location is the Lumbar vertebrae, lower back, but in rare cases it may be in the Thoracic vertebrae, middle back or Cervical vertebrae, neck. Occulta has no or only mild signs, which may include a hairy patch, dimple, dark spot or swelling on the back at the site of the gap in the spine. Meningocele typically causes mild problems, with a sac of fluid present at the gap in the spine. Myelomeningocele, also known as open spina bifida, is the most severe form. Problems associated with this form include poor ability to walk, impaired Neurogenic bladder dysfunction, bladder o ...
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Schizophrenia
Schizophrenia () is a mental disorder characterized variously by hallucinations (typically, Auditory hallucination#Schizophrenia, hearing voices), delusions, thought disorder, disorganized thinking and behavior, and Reduced affect display, flat or inappropriate affect. Symptoms Prodrome, develop gradually and typically begin during young adulthood and rarely resolve. There is no objective diagnostic test; diagnosis is based on observed behavior, a psychiatric history that includes the person's reported experiences, and reports of others familiar with the person. For a diagnosis of schizophrenia, the described symptoms need to have been present for at least six months (according to the DSM-5) or one month (according to the ICD-11). Many people with schizophrenia have other mental disorders, especially mood disorder, mood, anxiety disorder, anxiety, and substance use disorders, substance use disorders, as well as obsessive–compulsive disorder (OCD). About 0.3% to 0.7% of peo ...
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Autism
Autism, also known as autism spectrum disorder (ASD), is a neurodevelopmental disorder characterized by differences or difficulties in social communication and interaction, a preference for predictability and routine, sensory processing differences, focused interests, and repetitive behaviors, which may include stimming. Formal diagnosis requires significant challenges in multiple domains of life, with characteristics that are atypical or more pronounced than expected for one's age and sociocultural context.(World Health Organization: International Classification of Diseases version 11 (ICD-11)): https://icd.who.int/browse/2024-01/mms/en#437815624 Motor coordination difficulties are common but not required for diagnosis. Autism is a spectrum disorder, resulting in wide variations in presentation and support needs, such as that between speaking and non-speaking populations. Increased estimates of autism prevalence since the 1990s are primarily attributed to broader c ...
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Isozyme
In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different ''K''M values), or are regulated differently. They permit the fine-tuning of metabolism to meet the particular needs of a given tissue or developmental stage. In many cases, isozymes are encoded by homologous genes that have diverged over time. Strictly speaking, enzymes with different amino acid sequences that catalyse the same reaction are isozymes if encoded by different genes, or allozymes if encoded by different alleles of the same gene; the two terms are often used interchangeably. Introduction Isozymes were first described by R. L. Hunter and Clement Markert (1957) who defined them as ''different variants of the same enzyme having identical functions and present in the same individual''. This definition encompasses ...
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Threonine
Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form when dissolved in water), a carboxyl group (which is in the deprotonated −COO− form when dissolved in water), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as ''E. coli''. It is encoded by all the codons starting AC (ACU, ACC, ACA, and ACG). Threonine sidechains are often hydrogen bonded; the most common small motifs formed are based on interactions with serine: ST turns, ST motifs (often at the beginning of alpha helices) and ST staples (usually at the middle of alpha helices). Modifications The threonine residue is susceptible to numerous posttranslational modifications. The hydroxyl side-chain can und ...
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Glycine
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine disrupts the formation of alpha-helices in secondary protein structure. Its small side chain causes it to favor random coils instead. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a '' Clostridium tetani'' infection) can cause spastic paralysis due to uninhibited muscle contraction. It is the only achiral proteinogenic amino acid. It can fit into both hydrophilic and hydrophobic environments, due to its minimal side chain of only one hydrogen atom. History and etymology Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. He originally called it "sugar of ...
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Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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Transferase
In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor). They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes. Transferases are involved in myriad reactions in the cell. Three examples of these reactions are the activity of coenzyme A (CoA) transferase, which transfers thiol esters, the action of N-acetyltransferase, which is part of the pathway that metabolizes tryptophan, and the regulation of pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl CoA. Transferases are also utilized during translation. In this case, an amino acid chain is the functional group transferred by a peptidyl transferase. The transfer involves the removal of the growing amino acid chain from the tRNA molecule in the A-site of the ...
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Betaine—homocysteine S-methyltransferase
In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively: * Trimethylglycine (methyl donor) + homocysteine (hydrogen donor) → dimethylglycine (hydrogen receiver) + methionine (methyl receiver) This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. This enzyme participates in the metabolism of glycine, serine, threonine and also methionine. Isozymes In humans, there are two isozymes, BHMT and BHMT2, each encoded by a separate gene. Tissue distribution BHMT is expressed most predominantly in the liver and kidney. Clinical significance Mutations in the BHMT gene are known to exist in humans. Anomalies may influence the metabolism of homocysteine, which ...
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