An enzyme involved in the biosynthesis of isoleucine and valine. It converts 2-acetolactate into 3-hydroxy-2-oxo-isovalerate. Also acts on 2-hydroxy-2-acetobutyrate to form 2-hydroxy-2-oxo-3-methylvalerate. EC 5.4.99.3.
A flavoprotein enzyme that catalyzes the formation of acetolactate from 2 moles of PYRUVATE in the biosynthesis of VALINE and the formation of acetohydroxybutyrate from pyruvate and alpha-ketobutyrate in the biosynthesis of ISOLEUCINE. This enzyme was formerly listed as EC 4.1.3.18.
An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.
An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
An enzyme that catalyzes the transfer of phosphate from C-3 of 1,3-diphosphoglycerate to C-2 of 3-phosphoglycerate, forming 2,3-diphosphoglycerate. EC 5.4.2.4.
Pesticides used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Some plants develop HERBICIDE RESISTANCE.
Sulfonylurea compounds are a class of medications used in the treatment of diabetes mellitus type 2 that promote insulin secretion from pancreatic beta-cells by closing ATP-sensitive potassium channels in their membranes.
An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
A plant family of the order Liliales, subclass Liliidae, class Liliopsida (monocotyledons). Most species are perennials, native primarily to tropical America. They have creeping rootstocks, fibrous roots, and leaves in clusters at the base of the plant or borne on branched stems. The fruit is a capsule containing many seeds, or a one-seeded winged structure.
Amino acids which have a branched carbon chain.
Diminished or failed response of PLANTS to HERBICIDES.
The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.
Salts and esters of hydroxybutyric acid.
Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.
Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.
Cobamides are a class of compounds that function as cofactors in various enzymatic reactions, containing a corrin ring similar to vitamin B12, but with different substituents on the benzimidazole moiety, and can be found in certain bacteria and archaea.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)
Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.

The yeast A kinases differentially regulate iron uptake and respiratory function. (1/13)

Yeast has three A kinase catalytic subunits, which have greater than 75% identity and are encoded by the TPK genes (TPK1, TPK2, and TPK3) [Toda, T., Cameron, S., Sass, P., Zoller, M. & Wigler, M. (1987) Cell 50, 277-287]. Although they are redundant for viability, the three A kinases are not redundant for pseudohyphal growth [Robertson, L. S. & Fink, G. R. (1998) Proc. Natl. Acad. Sci. USA 95, 13783-13787; Pan, X. & Heitman, J. (1999) Mol. Cell. Biol. 19, 4874-4887]; Tpk2, but not Tpk1 or Tpk3, is required for pseudohyphal growth. Genome-wide transcriptional profiling has revealed unique signatures for each of the three A kinases leading to the identification of additional functional diversity among these proteins. Tpk2 negatively regulates genes involved in iron uptake and positively regulates genes involved in trehalose degradation and water homeostasis. Tpk1 is required for the derepression of branched chain amino acid biosynthesis genes that seem to have a second role in the maintenance of iron levels and DNA stability within mitochondria. The fact that TPK2 mutants grow better than wild types on nonfermentable carbon sources and on media deficient in iron supports the unique role of Tpk2 in respiratory growth and carbon source use.  (+info)

Structure and expression of a cyanobacterial ilvC gene encoding acetohydroxyacid isomeroreductase. (2/13)

Acetohydroxyacid isomeroreductase (AHAIR) is the shared second enzyme in the biosynthetic pathways leading to isoleucine and valine. AHAIR is encoded by the ilvC gene in bacteria. A 1,544-bp fragment of genomic DNA containing the ilvC gene was cloned from the cyanobacterium Synechocystis sp. strain PCC 6803, and the complete nucleotide sequence was determined. The identity of the gene was established by comparison of the nucleotide and derived peptide sequences with those of other ilvC genes. The highest degree of sequence similarity was found with the ilvC gene from Rhizobium meliloti. The isolated Synechocystis ilvC gene complemented an Escherichia coli ilvC mutant lacking AHAIR activity. The expressed Synechocystis gene encodes a protein that has a molecular mass of 35.7 kDa and that has AHAIR activity in an in vitro assay. Polyclonal antibodies raised against purified Synechocystis AHAIR produced a single band on a Western blot (immunoblot) of a Synechocystis cell extract and detected the protein in an extract of an E. coli ilvC mutant strain that was transformed with a plasmid containing the Synechocystis ilvC gene. The antibody did not react with an extract of an E. coli ilvC mutant strain that was transformed with a control plasmid lacking the Synechocystis ilvC gene or with an extract of an E. coli IlvC+ control strain.  (+info)

Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli. (3/13)

Acetohydroxy acid isomeroreductase catalyses a two-step reaction, an alkyl migration and a NADPH-dependent reduction, in the assembly of the carbon skeletons of branched-chain amino acids. Detailed investigations of acetohydroxy acid isomeroreductase aimed at elucidating the biosynthetic pathway of branched-chain amino acids and at designing new inhibitors of the enzyme having herbicidal potency have so far been conducted with the enzymes isolated from bacteria. To gain more information on a plant system, the gene encoding the mature acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) leaf chloroplasts has been used to transform Escherichia coli cells and to overexpress the enzyme. A rapid protocol is described that allows the preparation of large quantities of pure spinach chloroplast acetohydroxy acid isomeroreductase. Kinetic and structural properties of the plant enzyme expressed in Escherichia coli are compared with those reported in our previous studies on the native enzymes purified from spinach chloroplasts and with those reported for the corresponding enzymes isolated from Escherichia coli and Salmonella typhimurium. Both the plant and the bacterial enzymes obey an ordered mechanism in which NADPH binds first, followed by substrate (either 2-acetolactate or 2-aceto-2-hydroxybutyrate). Inhibition studies employing an inactive substrate analogue, 2-hydroxy-2-methyl-3-oxopentanoate, showed, however, that the binding of 2-hydroxy-2-methyl-3-oxopentanoate and NADPH occurs randomly, suggestive of some flexibility of the plant enzyme active site. The observed preference of the enzyme for 2-aceto-2-hydroxybutyrate over 2-acetolactate is discussed with regard to the contribution of acetohydroxy acid isomeroreductase activity in the partitioning between isoleucine and valine biosyntheses. Moreover, the kinetic properties of the chloroplast enzyme support the notion that biosynthesis of branched-chain amino acids in plants is controlled by light. As judged by analytical-ultracentrifugation and gel-filtration analyses the overexpressed plant enzyme is a dimer of identical subunits.  (+info)

Isolation, characterization and sequence analysis of a full-length cDNA clone encoding acetohydroxy acid reductoisomerase from spinach chloroplasts. (4/13)

Acetohydroxy acid reductoisomerase (AHRI), the second enzyme in the parallel isoleucine/valine-biosynthetic pathway, catalyses an unusual two-step reaction in which the substrate, either 2-acetolactate or 2-aceto-2-hydroxybutyrate, is converted via an alkyl migration and an NADPH-dependent reduction to give 2,3-dihydroxy-3-methylbutyrate or 2,3-dihydroxy-3-methylvalerate respectively. We have isolated and characterized a full-length cDNA from a lambda gt11 spinach library encoding the complete acetohydroxy acid reductoisomerase protein precursor. The 2050-nucleotide sequence contains a 1785-nucleotide open reading frame. The derived amino acid sequence indicates that the protein precursor consists of 595 amino acid residues including a presequence peptide of 72 amino acid residues. The N-terminal sequence of the first 16 amino acid residues of the purified AHRI confirms the identity of the cDNA. The derived amino acid sequence from this open reading frame shows 23% identity with the deduced amino acid sequences of the Escherichia coli and Saccharomyces cerevisiae AHRI proteins. There are two blocks of conserved amino acid residues in these three proteins. One of these is a sequence similar to the 'fingerprint' region of the NAD(P)H-binding site found in a large number of NAD(P)H-dependent oxidoreductases. The other, a short sequence (Lys-Xaa-Xaa-Xaa-Xaa-Xaa-Xaa-Xaa-Ser-His-Gly-Phe) containing the amino acids lysine and histidine, could well be the catalytic site of the first step of the AHRI reaction. Southern-blot analysis indicated that AHRI is encoded by a single gene per haploid genome of about 7.5 kbp containing at least four introns.  (+info)

Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp. (5/13)

Methanococcus aeolicus, Methanococcus maripaludis, and Methanococcus voltae contain similar levels of four enzymes of branched-chain amino acid biosynthesis: acetohydroxy acid synthase, acetohydroxy acid isomeroreductase, dihydroxy acid dehydratase, and transaminase B. Following growth at low partial pressures of H2-CO2, the levels of these enzymes in extracts of M. voltae are reduced three- to fivefold, which suggests that their synthesis is regulated. The enzymes from M. aeolicus were found to be similar to the eubacterial and eucaryotic enzymes with respect to molecular weights, pH optima, kinetic properties, and sensitivities to O2. The acetohydroxy acid isomeroreductase has a specific requirement for Mg2+, and other divalent cations were inhibitory. It was stimulated threefold by K+ and NH4+ ions and was able to utilize NADH as well as NADPH. The partially purified enzyme was not sensitive to O2. The dihydroxy acid dehydratase is extremely sensitive to O2, and it has a half-life under 5% O2 of 6 min at 25 degrees C. Divalent cations were required for activity, and Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ were nearly equally effective. In conclusion, the archaebacterial enzymes are functionally homologous to the eubacterial and eucaryotic enzymes, which implies that this pathway is very ancient.  (+info)

Purification and characterization of acetohydroxyacid reductoisomerase from spinach chloroplasts. (6/13)

Acetohydroxyacid reductoisomerase was purified over 400-fold to a specific activity of 62 nkat.mg-1, with 2-aceto-2-hydroxybutyrate as substrate, from the stroma of spinach leaf chloroplasts. The enzyme was not intrinsically membrane bound. The native enzyme was a tetramer with a subunit Mr of 59,000. The activity was optimum between pH 7.5 and 8.5. The apparent Km for 2-acetolactate was 25 microM and for 2-aceto-2-hydroxybutyrate was 37 microM. The enzyme required Mg2+ and the Vmax. was attained at physiological Mg2+ concentrations. NADP+ competitively inhibited the reaction when NADPH was the varied substrate. The native enzyme eluted from Mono-Q ion-exchange resins as three distinct peaks of activity. This elution pattern was preserved when the peaks were combined, dialysed and re-chromatographed. Each form exhibited identical Mr of 59,000 after SDS/polyacrylamide gel electrophoresis (PAGE), whereas they were easily distinguishable from each other after PAGE under non-denaturing conditions. These results provide evidence for the existence of multiple forms of acetohydroxyacid reductoisomerase in chloroplasts isolated from spinach leaves.  (+info)

The ILV5 gene of Saccharomyces cerevisiae is highly expressed. (7/13)

The nucleotide sequence of the yeast ILV5 gene, which codes for the branched-chain amino acid biosynthesis enzyme acetohydroxyacid reductoisomerase, has been determined. The ILV5 coding region is 1,185 nucleotides, corresponding to a polypeptide with a molecular weight of 44,280. Transcription of the ILV5 mRNA initiates at position -81 upstream from the ATG translation start codon and terminates between 218 and 222 bases downstream from the stop codon. Consensus sequences have been identified for initiation and termination of transcription, and for general control of amino acid biosynthesis, as well as repression by leucine. The ILV5 gene is regulated slightly by general amino acid control. Codon usage of the ILV5 gene has the strong bias observed in yeast genes that are highly expressed. In agreement with this, the reductoisomerase monomer, with an apparent molecular weight of 40,000, has been identified in an SDS polyacrylamide gel pattern of total soluble yeast proteins as a gene dosage dependent band.  (+info)

The herbicidally active experimental compound Hoe 704 is a potent inhibitor of the enzyme acetolactate reductoisomerase. (8/13)

Growth inhibition of plants and bacteria by the experimental herbicide Hoe 704 (2-methylphosphinoyl-2-hydroxyacetic acid) was alleviated by the addition of the branched-chain amino acids to growth media. Hoe 704 caused a massive accumulation of acetoin and acetolactate, indicating its direct interference with the branched-chain amino acid biosynthetic pathway. The second enzyme of this pathway, acetolactate reductoisomerase (EC 1.1.1.86), was found to be subject to strong inhibition by Hoe 704. The inhibition was time-dependent and competitive with the enzyme's substrate, acetolactate. This report establishes acetolactate reductoisomerase as a new target for a herbicidal compound.  (+info)

2-Acetolactate Mutase is an enzyme involved in the metabolic pathway known as the "biosynthesis of branched-chain amino acids." This enzyme specifically catalyzes the conversion of 2-acetolactate to 3-hydroxyisovalerate, which is a key intermediate in the synthesis of the essential branched-chain amino acids valine, leucine, and isoleucine.

The systematic name for this enzyme is 2-acetolactate hydro-lyase (3-hydroxyisovalerate-forming). It is classified as a member of the lyase family of enzymes, which are characterized by the cleavage of various bonds using water or other small molecules.

Defects in this enzyme have been associated with certain genetic disorders, such as maple syrup urine disease (MSUD), which is characterized by an accumulation of branched-chain amino acids and their metabolites in the body. This can lead to a variety of symptoms, including neurological problems, developmental delays, and metabolic acidosis.

Acetolactate synthase (ALS), also known as acetohydroxyacid synthase (AHAS), is a key enzyme in the biosynthetic pathway of branched-chain amino acids (valine, leucine, and isoleucine) in bacteria, fungi, and plants. It catalyzes the first step in the pathway, which is the condensation of two molecules of pyruvate to form acetolactate.

Inhibitors of ALS, such as sulfonylureas and imidazolinones, are widely used as herbicides because they disrupt the biosynthesis of amino acids that are essential for plant growth and development. These inhibitors work by binding to the active site of the enzyme and preventing the substrate from accessing it.

In humans, ALS is not involved in the biosynthesis of branched-chain amino acids, but a homologous enzyme called dihydroorotate dehydrogenase (DHOD) plays a crucial role in the synthesis of pyrimidine nucleotides. Inhibitors of DHOD are used as immunosuppressants to treat autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis.

Methylmalonyl-CoA mutase is a mitochondrial enzyme that plays a crucial role in the metabolism of certain amino acids and fatty acids. Specifically, it catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, which is an important step in the catabolic pathways of valine, isoleucine, threonine, methionine, odd-chain fatty acids, and cholesterol.

The enzyme requires a cofactor called adenosylcobalamin (vitamin B12) for its activity. In the absence of this cofactor or due to mutations in the gene encoding the enzyme, methylmalonyl-CoA mutase deficiency can occur, leading to the accumulation of methylmalonic acid and other toxic metabolites, which can cause a range of symptoms including vomiting, dehydration, lethargy, hypotonia, developmental delay, and metabolic acidosis. This condition is typically inherited in an autosomal recessive manner and can be diagnosed through biochemical tests and genetic analysis.

Phosphoglycerate Mutase (PGM) is an enzyme that plays a crucial role in the glycolytic pathway, which is a metabolic process that converts glucose into pyruvate, producing ATP and NADH as energy currency for the cell.

The enzyme catalyzes the interconversion of 3-phosphoglycerate (3-PG) and 2-phosphoglycerate (2-PG), which is the ninth step in glycolysis. Specifically, PGM transfers a phosphate group from the third carbon atom to the second carbon atom of 3-PG, resulting in the formation of 2-PG and inorganic phosphate.

There are two types of Phosphoglycerate Mutase isoenzymes in humans, including:

1. Phosphoglycerate Mutase 1 (PGAM1): This is a cytosolic enzyme that is widely expressed in various tissues, including skeletal muscle, heart, brain, and liver.
2. Phosphoglycerate Mutase 2 (PGAM2): This is a muscle-specific isoenzyme that is primarily found in cardiac and skeletal muscles.

Mutations in the PGAM1 gene have been associated with hemolytic anemia, neurodevelopmental disorders, and other metabolic abnormalities, while mutations in the PGAM2 gene have been linked to myopathies and other muscle-related disorders.

Oxo-acid lyases are a class of enzymes that catalyze the cleavage of a carbon-carbon bond in an oxo-acid to give a molecule with a carbonyl group and a carbanion, which then reacts non-enzymatically with a proton to form a new double bond. The reaction is reversible, and the enzyme can also catalyze the reverse reaction.

Oxo-acid lyases play important roles in various metabolic pathways, such as the citric acid cycle, glyoxylate cycle, and the degradation of certain amino acids. These enzymes are characterized by the presence of a conserved catalytic mechanism involving a nucleophilic attack on the carbonyl carbon atom of the oxo-acid substrate.

The International Union of Biochemistry and Molecular Biology (IUBMB) has classified oxo-acid lyases under EC 4.1.3, which includes enzymes that catalyze the formation of a carbon-carbon bond by means other than carbon-carbon bond formation to an enolate or carbonion, a carbanionic fragment, or a Michael acceptor.

Bisphosphoglycerate mutase (BPGM) is an enzyme that plays a crucial role in the regulation of oxygen transport in red blood cells. The main function of BPGM is to convert 1,3-bisphosphoglycerate (1,3-BPG) into 2,3-bisphosphoglycerate (2,3-BPG), also known as 2,3-diphosphoglycerate (2,3-DPG).

2,3-BPG is essential for modulating the affinity of hemoglobin for oxygen. By increasing the concentration of 2,3-BPG in red blood cells, BPGM reduces the ability of hemoglobin to bind to oxygen, allowing more oxygen to be released from hemoglobin and made available to tissues, particularly under low-oxygen conditions. This is especially important for individuals living at high altitudes or those with chronic lung diseases who may have impaired oxygen transport.

Defects in the BPGM gene can lead to a rare disorder called 2,3-bisphosphoglycerate deficiency, which results in an increased affinity of hemoglobin for oxygen and reduced oxygen delivery to tissues. This condition is characterized by symptoms such as shortness of breath, fatigue, and headaches, particularly during exercise or at high altitudes.

Herbicides are a type of pesticide used to control or kill unwanted plants, also known as weeds. They work by interfering with the growth processes of the plant, such as inhibiting photosynthesis, disrupting cell division, or preventing the plant from producing certain essential proteins.

Herbicides can be classified based on their mode of action, chemical composition, and the timing of their application. Some herbicides are selective, meaning they target specific types of weeds while leaving crops unharmed, while others are non-selective and will kill any plant they come into contact with.

It's important to use herbicides responsibly and according to the manufacturer's instructions, as they can have negative impacts on the environment and human health if not used properly.

Sulfonylurea compounds are a group of medications used in the management of type 2 diabetes. They work by stimulating the release of insulin from the pancreas, thereby lowering blood glucose levels. These compounds bind to specific receptors on the beta cells of the pancreas, which triggers the release of insulin.

Examples of sulfonylurea compounds include glipizide, glyburide, and glimepiride. It's important to note that these medications can cause hypoglycemia (low blood sugar) if not properly monitored and dosed. They are often used in combination with other medications, such as metformin, to achieve optimal blood glucose control.

As with any medication, sulfonylurea compounds should be taken under the supervision of a healthcare provider, who can monitor their effectiveness and potential side effects.

Isoleucine is an essential branched-chain amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H13NO2. Isoleucine is crucial for muscle protein synthesis, hemoglobin formation, and energy regulation during exercise or fasting. It is found in various foods such as meat, fish, eggs, dairy products, legumes, and nuts. Deficiency of isoleucine may lead to various health issues like muscle wasting, fatigue, and mental confusion.

Acetoin is a chemical compound that is produced as a metabolic byproduct in certain types of bacteria, including some species of streptococcus and lactobacillus. It is a colorless liquid with a sweet, buttery odor and is used as a flavoring agent in the food industry. In addition to its use as a flavoring, acetoin has been studied for its potential antibacterial properties and its possible role in the development of biofilms. However, more research is needed to fully understand the potential uses and implications of this compound.

Valine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through diet. It is a hydrophobic amino acid, with a branched side chain, and is necessary for the growth, repair, and maintenance of tissues in the body. Valine is also important for muscle metabolism, and is often used by athletes as a supplement to enhance physical performance. Like other essential amino acids, valine must be obtained through foods such as meat, fish, dairy products, and legumes.

I apologize for any confusion, but "Pontederiaceae" is not a medical term. It is a taxonomic category in botany, specifically the name of a family of flowering plants that includes water hyacinth and pickerelweed. If you have any questions about a medical term or concept, I would be happy to help with those instead!

Branched-chain amino acids (BCAAs) are a group of three essential amino acids: leucine, isoleucine, and valine. They are called "branched-chain" because of their chemical structure, which has a side chain that branches off from the main part of the molecule.

BCAAs are essential because they cannot be produced by the human body and must be obtained through diet or supplementation. They are crucial for muscle growth and repair, and play a role in energy production during exercise. BCAAs are also important for maintaining proper immune function and can help to reduce muscle soreness and fatigue after exercise.

Foods that are good sources of BCAAs include meat, poultry, fish, eggs, dairy products, and legumes. BCAAs are also available as dietary supplements, which are often used by athletes and bodybuilders to enhance muscle growth and recovery. However, it is important to note that excessive intake of BCAAs may have adverse effects on liver function and insulin sensitivity, so it is recommended to consult with a healthcare provider before starting any new supplement regimen.

Herbicide resistance is a genetically acquired trait in weeds that allows them to survive and reproduce following exposure to doses of herbicides that would normally kill or inhibit the growth of susceptible plants. It is a result of natural selection where weed populations with genetic variability are exposed to herbicides, leading to the survival and reproduction of individuals with resistance traits. Over time, this can lead to an increase in the proportion of resistant individuals within the population, making it harder to control weeds using that particular herbicide or group of herbicides.

Thiamine pyrophosphate (TPP) is the active form of thiamine (vitamin B1) that plays a crucial role as a cofactor in various enzymatic reactions, particularly in carbohydrate metabolism. TPP is essential for the functioning of three key enzymes: pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase. These enzymes are involved in critical processes such as the conversion of pyruvate to acetyl-CoA, the oxidative decarboxylation of alpha-ketoglutarate in the Krebs cycle, and the pentose phosphate pathway, which is important for generating reducing equivalents (NADPH) and ribose sugars for nucleotide synthesis. A deficiency in thiamine or TPP can lead to severe neurological disorders, including beriberi and Wernicke-Korsakoff syndrome, which are often observed in alcoholics due to poor nutrition and impaired thiamine absorption.

Hydroxybutyrates are compounds that contain a hydroxyl group (-OH) and a butyric acid group. More specifically, in the context of clinical medicine and biochemistry, β-hydroxybutyrate (BHB) is often referred to as a "ketone body."

Ketone bodies are produced by the liver during periods of low carbohydrate availability, such as during fasting, starvation, or a high-fat, low-carbohydrate diet. BHB is one of three major ketone bodies, along with acetoacetate and acetone. These molecules serve as alternative energy sources for the brain and other tissues when glucose levels are low.

In some pathological states, such as diabetic ketoacidosis, the body produces excessive amounts of ketone bodies, leading to a life-threatening metabolic acidosis. Elevated levels of BHB can also be found in other conditions like alcoholism, severe illnesses, and high-fat diets.

It is important to note that while BHB is a hydroxybutyrate, not all hydroxybutyrates are ketone bodies. The term "hydroxybutyrates" can refer to any compound containing both a hydroxyl group (-OH) and a butyric acid group.

Intramolecular transferases are a specific class of enzymes that catalyze the transfer of a functional group from one part of a molecule to another within the same molecule. These enzymes play a crucial role in various biochemical reactions, including the modification of complex carbohydrates, lipids, and nucleic acids. By facilitating intramolecular transfers, these enzymes help regulate cellular processes, signaling pathways, and metabolic functions.

The systematic name for this class of enzymes is: [donor group]-transferring intramolecular transferases. The classification system developed by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) categorizes them under EC 2.5. This category includes enzymes that transfer alkyl or aryl groups, other than methyl groups; methyl groups; hydroxylyl groups, including glycosyl groups; and various other specific functional groups.

Examples of intramolecular transferases include:

1. Protein kinases (EC 2.7.11): Enzymes that catalyze the transfer of a phosphate group from ATP to a specific amino acid residue within a protein, thereby regulating protein function and cellular signaling pathways.
2. Glycosyltransferases (EC 2.4): Enzymes that facilitate the transfer of glycosyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, playing a role in the biosynthesis and modification of complex carbohydrates.
3. Methyltransferases (EC 2.1): Enzymes that transfer methyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, contributing to the regulation of gene expression and other cellular processes.

Understanding the function and regulation of intramolecular transferases is essential for elucidating their roles in various biological processes and developing targeted therapeutic strategies for diseases associated with dysregulation of these enzymes.

Lactates, also known as lactic acid, are compounds that are produced by muscles during intense exercise or other conditions of low oxygen supply. They are formed from the breakdown of glucose in the absence of adequate oxygen to complete the full process of cellular respiration. This results in the production of lactate and a hydrogen ion, which can lead to a decrease in pH and muscle fatigue.

In a medical context, lactates may be measured in the blood as an indicator of tissue oxygenation and metabolic status. Elevated levels of lactate in the blood, known as lactic acidosis, can indicate poor tissue perfusion or hypoxia, and may be seen in conditions such as sepsis, cardiac arrest, and severe shock. It is important to note that lactates are not the primary cause of acidemia (low pH) in lactic acidosis, but rather a marker of the underlying process.

Cobamides are a class of compounds that are structurally related to vitamin B12 (cobalamin). They consist of a corrin ring, which is a large heterocyclic ring made up of four pyrrole rings, and a cobalt ion in the center. The lower axial ligand of the cobalt ion can be a variety of different groups, including cyano, hydroxo, methyl, or 5'-deoxyadenosyl groups.

Cobamides are involved in a number of important biological processes, including the synthesis of amino acids and nucleotides, the metabolism of fatty acids and cholesterol, and the regulation of gene expression. They function as cofactors for enzymes called cobamide-dependent methyltransferases, which transfer methyl groups (CH3) from one molecule to another.

Cobamides are found in a wide variety of organisms, including bacteria, archaea, and eukaryotes. In humans, the most important cobamide is vitamin B12, which is essential for the normal functioning of the nervous system and the production of red blood cells. Vitamin B12 deficiency can lead to neurological problems and anemia.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Pyruvic acid, also known as 2-oxopropanoic acid, is a key metabolic intermediate in both anaerobic and aerobic respiration. It is a carboxylic acid with a ketone functional group, making it a β-ketoacid. In the cytosol, pyruvate is produced from glucose during glycolysis, where it serves as a crucial link between the anaerobic breakdown of glucose and the aerobic process of cellular respiration in the mitochondria.

During low oxygen availability or high energy demands, pyruvate can be converted into lactate through anaerobic glycolysis, allowing for the continued production of ATP (adenosine triphosphate) without oxygen. In the presence of adequate oxygen and functional mitochondria, pyruvate is transported into the mitochondrial matrix where it undergoes oxidative decarboxylation to form acetyl-CoA by the enzyme pyruvate dehydrogenase complex (PDC). This reaction also involves the reduction of NAD+ to NADH and the release of CO2. Acetyl-CoA then enters the citric acid cycle, where it is further oxidized to produce energy in the form of ATP, NADH, FADH2, and GTP (guanosine triphosphate) through a series of enzymatic reactions.

In summary, pyruvic acid is a vital metabolic intermediate that plays a significant role in energy production pathways, connecting glycolysis to both anaerobic and aerobic respiration.

Butyrates are a type of fatty acid, specifically called short-chain fatty acids (SCFAs), that are produced in the gut through the fermentation of dietary fiber by gut bacteria. The name "butyrate" comes from the Latin word for butter, "butyrum," as butyrate was first isolated from butter.

Butyrates have several important functions in the body. They serve as a primary energy source for colonic cells and play a role in maintaining the health and integrity of the intestinal lining. Additionally, butyrates have been shown to have anti-inflammatory effects, regulate gene expression, and may even help prevent certain types of cancer.

In medical contexts, butyrate supplements are sometimes used to treat conditions such as ulcerative colitis, a type of inflammatory bowel disease (IBD), due to their anti-inflammatory properties and ability to promote gut health. However, more research is needed to fully understand the potential therapeutic uses of butyrates and their long-term effects on human health.

Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. This enzyme participates in valine, ... In enzymology, a 2-acetolactate mutase (EC 5.4.99.3) is an enzyme that catalyzes the chemical reaction 2-acetolactate ⇌ {\ ... The systematic name of this enzyme class is 2-acetolactate methylmutase. ... 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate. This enzyme belongs to the family of isomerases, ...
... phosphoglycerate mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH ... acetolactate synthase MeSH D08.811.913.200.650 - transaldolase MeSH D08.811.913.200.825 - transketolase MeSH D08.811.913.225. ... chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH D08.811.399.520.250.750 - prephenate dehydrogenase ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - ...
... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate- ... benzene mutase EC 5.4.4.2: isochorismate synthase EC 5.4.4.3: 3-(hydroxyamino)phenol mutase EC 5.4.4.4: geraniol isomerase EC ... isobutyryl-CoA mutase EC 5.4.99.14: 4-carboxymethyl-4-methylbutenolide mutase EC 5.4.99.15: (1→4)-α-D-glucan 1-α-D- ... methylaspartate mutase EC 5.4.99.2: methylmalonyl-CoA mutase EC 5.4.99.3: 2-acetolactate mutase EC 5.4.99.4: 2- ...
The second step involves the NADPH+-dependent reduction of α-acetolactate and migration of methyl groups to produce α, β- ... This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. PheA ... It begins with the condensation of two equivalents of pyruvate catalyzed by acetohydroxy acid synthase yielding α-acetolactate ... Enzymes involved in this biosynthesis include acetolactate synthase (also known as acetohydroxy acid synthase), acetohydroxy ...
Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. This enzyme participates in valine, ... In enzymology, a 2-acetolactate mutase (EC 5.4.99.3) is an enzyme that catalyzes the chemical reaction 2-acetolactate ⇌ {\ ... The systematic name of this enzyme class is 2-acetolactate methylmutase. ... 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate. This enzyme belongs to the family of isomerases, ...
2.2.1.6 acetolactate synthase 4.1.1.1 pyruvate decarboxylase - - BRENDA: BR37100; BS386675 KEGG: R00006; R00226 ... H+ + (2S)-2-isopropyl-3-oxosuccinate <=> 4-methyl-2-oxopentanoate + CO2 0.0.0.0 1.1.1.85 3-isopropylmalate dehydrogenase - - ... pyruvate + L-valine <=> L-alanine + 2-oxoisovalerate 2.6.1.12 alanine---oxo-acid transaminase 2.6.1.42 branched-chain-amino- ... 2R,3R-2,3-dihydroxy-3-methylpentanoate <=> (S)-3-methyl-2-oxopentanoate + H2O 4.2.1.9 dihydroxy-acid dehydratase - ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Fluoro-2-deoxyglucose use Fluorodeoxyglucose F18 2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-hexahydro-3-isobutyl-9,10- ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ... 2-Chloroethyl Alcohol use Ethylene Chlorohydrin 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Fluoro-2-deoxyglucose use Fluorodeoxyglucose F18 2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-hexahydro-3-isobutyl-9,10- ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ... 2-Chloroethyl Alcohol use Ethylene Chlorohydrin 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate ...
2-Fluoro-2-deoxyglucose use Fluorodeoxyglucose F18 2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-hexahydro-3-isobutyl-9,10- ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ... 2-Chloroethyl Alcohol use Ethylene Chlorohydrin 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-Glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-Glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-Glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
","alpha-acetolactate decarboxylase [Ensembl]. Alpha-acetolactate decarboxylase [Interproscan].","protein_coding" "CPD16875"," ... 2C3-bisphosphoglycerate-independent phosphoglycerate mutase [Ensembl]. Metalloenzyme superfamily, BPG-independent PGAM N- ... ","phosphoglycero mutase III, cofactor-independent [Ensembl]. Metalloenzyme superfamily, BPG-independent PGAM N-terminus (iPGM_ ... ","3-hydroxylaminophenol mutase [Ensembl]. Glutamine synthetase [Interproscan].","protein_coding" "AKP14726","metZ","Neisseria ...
EC 5.4.2.9: Phosphoenolpyruvate mutase. *EC 5.4.2.10: Phosphoglucosamine mutase. EC 5.4.3: Transferring Amino Groups. *EC 5.4. ... EC 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase. EC 5.4.4: Transferring hydroxy groups. *EC 5.4.4.1: (hydroxyamino)benzene ... EC 5.1.2: Acting on Hydroxy acids and Derivatives. *EC 5.1.2.1: lactate racemase ... EC 5.3.2: Interconverting Keto- and Enol-Groups. *EC 5.3.2.1: phenylpyruvate tautomerase ...
Alpha-acetolactate decarboxylase. O34667 LUXS. 157. 966. 31.7. 0.06. S-ribosylhomocysteine lyase. ... Chorismate mutase AroH. P42966 YCSI. 257. 799. 35.4. 0.01. UPF0317 protein YcsI. ... 2,3-diketo-5-methylthiopentyl-1-phosphate enolase. Q04777 ALDC. 255. 611. 30.4. 0.07. ...
3-bisphosphoglycerate-independent phosphoglycerate mutase OS=Mesembryanthemum crystallinum","protein_coding" "Cre06.g274994"," ... ","ACT domain; Acetolactate synthase, small subunit, C-terminal [Interproscan].","protein_coding" "Vocar.0001s1455.1","32886092 ... ","Chorismate mutase","protein_coding" "Sro543_g163470.1","Contig1245.g11633","Seminavis robusta","Peptide chain release factor ... D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain [Interproscan].","protein_coding" "Cz06g07120.t1","No alias"," ...
regulatory subunit of acetolactate synthase complex","protein_coding" "Solyc12g035520.3.1","No alias","Solanum lycopersicum"," ... ","Phosphoglycerate mutase family protein","protein_coding" "AT1G12910","LWD1","Arabidopsis thaliana","Transducin/WD40 repeat- ... ","UDP-L-arabinose mutase","protein_coding" "Gb_22250","No alias","Gingko biloba","GDSL esterase/lipase At3g26430 OS= ... japonica (sp,q5qmt0,bgl01_orysj : 739.0) & Enzyme classification.EC_3 hydrolases.EC_3.2 glycosylase(50.3.2 : 376.1)","protein_ ...
Enzyme (substance) {90668006 , SNOMED-CT } Substance with mutase mechanism of action (substance) {130945002 , SNOMED-CT } ...
Chorismate Mutase [D08.811.399.520.250] * Methylmalonyl-CoA Mutase [D08.811.399.520.625] * Phosphotransferases (Phosphomutases ... 2-Acetolactate Mutase Preferred Term Term UI T043966. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... 2-Acetohydroxy-3-Ketoacid Isomeroreductase Term UI T043965. Date11/11/1974. LexicalTag NON. ThesaurusID UNK (19XX). ... 2-Acetolactate Mutase Preferred Concept UI. M0023185. Registry Number. EC 5.4.99.3. Scope Note. An enzyme involved in the ...
Chorismate Mutase [D08.811.399.520.250] * Methylmalonyl-CoA Mutase [D08.811.399.520.625] * Phosphotransferases (Phosphomutases ... 2-Acetolactate Mutase Preferred Term Term UI T043966. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... 2-Acetohydroxy-3-Ketoacid Isomeroreductase Term UI T043965. Date11/11/1974. LexicalTag NON. ThesaurusID UNK (19XX). ... 2-Acetolactate Mutase Preferred Concept UI. M0023185. Registry Number. EC 5.4.99.3. Scope Note. An enzyme involved in the ...
ID: GO:0047927 Type: http://bio2vec.net/ontology/gene_function Label: gibberellin-44 dioxygenase activity Synonyms: gibberellin-44 dioxygenase activity Alternative IDs: als API: GO SPARQL: GO ...
Human N0000168121 Chorismate Mutase N0000166668 Chorismic Acid N0000007918 Chromans N0000007919 Chromates N0000169072 Chromatin ... Acetohexamide N0000006036 acetohydroxamic acid N0000166800 Acetoin N0000167958 Acetoin Dehydrogenase N0000169059 Acetolactate ... N0000166719 Methylmalonic Acid N0000168054 Methylmalonyl-CoA Decarboxylase N0000168120 Methylmalonyl-CoA Mutase N0000168446 ... 27 N0000170401 D-Ala(2),MePhe(4),Met(0)-ol-enkephalin N0000168380 D-Alanine Transaminase N0000167841 D-Amino-Acid Oxidase ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
D8.811.682.47.50 Acetolactate Synthase D8.586.520.224.600.100 D8.811.520.224.600.100 Acetyl Coenzyme A D8.176.211.300.75 D8.211 ... Methylmalonyl-CoA Mutase D8.586.399.520.625 D8.811.399.520.625 Methylobacillus B3.440.400.425.485 B3.660.75.495.500 B3.660. ... B1.150.900.649.77.380.120 Bisphosphoglycerate Mutase D8.586.399.520.750.250 D8.811.399.520.750.250 Black Widow Spider B1.131. ... D6.472.785.400.125 Chorismate Mutase D8.586.399.520.250 D8.811.399.520.250 Chromaffin Granules A11.284.195.190.500.207 A11.284. ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
Bisphosphoglycerate Mutase Bisphosphonate-Associated Osteonecrosis of the Jaw Bite Force Bites and Stings Bites, Human ... Acetolactate Synthase Acetone Acetonitriles Acetophenones Acetoxyacetylaminofluorene Acetrizoic Acid Acetyl Coenzyme A Acetyl- ... Chorismate Mutase Chorismic Acid Choristoma Choroid Choroid Diseases Choroid Hemorrhage Choroid Neoplasms Choroid Plexus ... 2),MePhe(4),Met(0)-ol-enkephalin D-Alanine Transaminase D-Amino-Acid Oxidase D-Aspartate Oxidase D-Aspartic Acid D-Xylulose ...
2-ME use Mercaptoethanol 2-N-Butyl-3-((2-(1H-tetrazol-5-yl)biphenyl-4-yl)methyl)-1,3-diazaspiro(4,4)non-1-en-4-one use ... 1H-2-Benzopyran-1-ones use Isocoumarins 1H-3-Benzazepine-7,8-diol, 2,3,4,5-tetrahydro-1-phenyl- use 2,3,4,5-Tetrahydro-7,8- ... 2-(1-Piperazinyl)quinoline use Quipazine 2-(1,3-Dihydro-3-oxo-5-sulpho-2H-indol-2-ylidene)-3- oxoindoline-5-sulphonic acid use ... 2-Butenoic Acids use Crotonates 2-Butyl-4-chloro-1-((2-(1H-etrazol-5-yl) (1,1-biphenyl)-4-yl)methyl)-1H-imidazole-5-methanol ...
... acetolactate synthase ALS,acid labile subunit ALS,acid-labile subunit ALS,acute lateral sclerosis ALS,advanced life support ALS ... chorismate mutase Cm,chronic meningitis Cm,chylomicron Cm,circular muscle Cm,circulating monocyte Cm,clindamycin Cm,clinical ... shell> lvg -f:a -F:1:2. II. Test Cases: IOTA,information overload testing aid IOTA,international ovarian tumor analysis IOTA, ... isoelectric point IGF-2,insulin-like growth factor 2 IGF-2,insulin-like growth factor 2 IGF-2,insulin-like growth factor 2 IGF- ...
3-bisphosphoglycerate-independent phosphoglycerate mutase; Metalloenzyme [Interproscan].","protein_coding" "Dusal.0086s00033.1 ... ","Dunaliella sp.","Acetolactate synthase, small subunit, C-terminal; ACT domain [Interproscan].","protein_coding" "Dusal. ... ","Acetolactate synthase isoform A","protein_coding" "lcl,LHPG02000028.1_cds_PRW05817.1_5977","PRW05817","Chlorella sorokiniana ... region 4 type 2 [Interproscan].","protein_coding" "SymbC1.scaffold5.726","5.726","Cladocopium sp. clade C","DNA polymerase III ...
2.919876 INESSENTIAL ILV6 Small regulatory subunit of Acetolactate synthase,acetolactate synthase, YKR065C -2.920049 ... 2.117944 INESSENTIAL GPM3 phosphoglycerate mutase, glycolysis*, phosphoglycerate mutase, cytosol YPR051W 2.114863 INESSENTIAL ... 2.473117 INESSENTIAL GPM2 phosphoglycerate mutase, involved in glycolysis, glycolysis*, phosphoglycerate mutase, cytosol ... 1.749511 INESSENTIAL PMU1 Phospo-mutase homolog, biological_process unknown, YGR125W 1.749010 INESSENTIAL biological_process ...
Small subunit of acetolactate synthase [Interproscan].","protein_coding" "CCP45809","ilvB1","Mycobacterium tuberculosis"," ... ","phosphoglucosamine mutase [Ensembl]. C-terminal domain, alpha/beta/alpha domain III [InterProScan].","protein_coding" " ... "Acetolactate synthase (large subunit) IlvB1 (acetohydroxy-acid synthase) [Ensembl].","protein_coding" "CCP45818","gatC"," ... ","Probable acetolactate synthase (small subunit) IlvN (acetohydroxy-acid synthase) (AHAS) (ALS) [Ensembl]. ACT domain, ...
Novel Synechocystis strain integrated with a native 2-keto acid pathway was generated and showed a production of 98 mg ... PCC 6803 has been engineered for the isobutanol and 3-methyl-1-butanol production by introducing a synthetic 2-keto acid ... kivdS286T, encodes α-ketoisovalerate decarboxylase (L. lactis); alsS, encodes acetolactate synthase (Bacillus subtilis); ilvC, ... 3-bisphosphoglycerate-independent phosphoglycerate mutase (Gpm), enolase (Eno), and pyruvate kinase (PK) (Additional file 1: ...
... acetolactate synthase ALS,acid labile subunit ALS,acid-labile subunit ALS,acute lateral sclerosis ALS,advanced life support ALS ... chorismate mutase Cm,chronic meningitis Cm,chylomicron Cm,circular muscle Cm,circulating monocyte Cm,clindamycin Cm,clinical ... shell> lvg -f:a -F:1:2. II. Test Cases: IOTA,information overload testing aid IOTA,international ovarian tumor analysis IOTA, ... isoelectric point IGF-2,insulin-like growth factor 2 IGF-2,insulin-like growth factor 2 IGF-2,insulin-like growth factor 2 IGF- ...
  • Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. (wikipedia.org)
  • 39504) translation initiation factor 2%2C alpha subunit CP001857 CDS Arcpr_0045 complement(39546. (go.jp)
  • Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. (wikipedia.org)
  • The 2-acetolactate is further converted to 2-ketoisovalerate by sequential enzymatic reactions catalyzed by acetohydroxy-acid isomeroreductase (IlvC) and dihydroxy-acid dehydratase (IlvD). (biomedcentral.com)
  • The systematic name of this enzyme class is 2-acetolactate methylmutase. (wikipedia.org)
  • Within the 2-keto acid pathway, the first involved enzyme, acetolactate synthase (AlsS), condenses two pyruvate molecules into a 2-acetolactate molecule. (biomedcentral.com)
  • In enzymology, a 2-acetolactate mutase (EC 5.4.99.3) is an enzyme that catalyzes the chemical reaction 2-acetolactate ⇌ {\displaystyle \rightleftharpoons } 3-hydroxy-3-methyl-2-oxobutanoate Hence, this enzyme has one substrate, 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate. (wikipedia.org)
  • As an intermediate for valine and leucine biosynthesis, 2-ketoisovalerate is decarboxylated by a heterologously expressed broad-substrate-range α-ketoisovalerate decarboxylase (Kivd) to isobutyaldehyde, and subsequently reduced into IB by an alcohol dehydrogenase (Adh). (biomedcentral.com)
  • 14787 ABC-2 type transport system ATP-binding protein BBZA01000002 CDS ARMA_0027 14784. (go.jp)
  • The significantly enhanced isobutanol and 3-methyl-1-butanol production in this study further pave the way for an industrial application of photosynthetic cyanobacteria-based biofuel and chemical synthesis from CO 2 . (biomedcentral.com)

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