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.
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
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 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.
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 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.
Diminished or failed response of PLANTS to HERBICIDES.
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.
Amino acids which have a branched carbon chain.
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.
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
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.
A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Salts and esters of hydroxybutyric acid.
Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.

Construction of an L-isoleucine overproducing strain of Escherichia coli K-12. (1/174)

The genes for a threonine deaminase that is resistant to feedback inhibition by L-isoleucine and for an active acetohydroxyacid synthase II were introduced by a plasmid into a L-threonine-producing recombinant strain of Escherichia coli K-12. Analysis of culture broth of the strain using 13C nuclear magnetic resonance suggested that alpha, beta-dihydroxy-beta-methylvalerate (DHMV) and alpha-keto-beta-methylvalerate (KMV), the third and the fourth intermediates in the L-isoleucine biosynthetic pathway from L-threonine, respectively, accumulated in the medium in amounts comparable to that of L-isoleucine. The ratio of accumulated L-isoleucine:DHMV:KMV were approximately 2:1:1. The concentration of accumulated L-isoleucine increased by twofold after the additional introduction of the genes for dihyroxyacid dehydratase (DH) and transaminase-B (TA-B), and the intermediates no longer accumulated. The resultant strain TVD5 accumulated 10 g/l of L-isoleucine from 40 g/l of glucose.  (+info)

Effect of mutagenesis at serine 653 of Arabidopsis thaliana acetohydroxyacid synthase on the sensitivity to imidazolinone and sulfonylurea herbicides. (2/174)

Resistance to sulfonylurea and imidazolinone herbicides can occur by mutations in acetohydroxyacid synthase (EC 4.1.3.18). Changing serine 653 to asparagine is known to cause insensitivity to imidazolinones but not to sulfonylureas. Here, S-653 of the Arabidopsis thaliana enzyme was mutated to alanine, threonine and phenylalanine. The purified mutated enzymes resemble wild-type in their enzymatic properties. The threonine and phenylalanine mutants are imidazolinone-resistant and the latter is also slightly sulfonylurea-resistant. The alanine mutant remains sensitive to both herbicides. The results suggest that the beta-hydroxyl group is not required for imidazolinone binding and that the size of the side-chain determines resistance.  (+info)

Targeted manipulation of maize genes in vivo using chimeric RNA/DNA oligonucleotides. (3/174)

Site-specific heritable mutations in maize genes were engineered by introducing chimeric RNA/DNA oligonucleotides. Two independent targets within the endogenous maize acetohydroxyacid synthase gene sequence were modified in a site-specific fashion, thereby conferring resistance to either imidazolinone or sulfonylurea herbicides. Similarly, an engineered green fluorescence protein transgene was site-specifically modified in vivo. Expression of the introduced inactive green fluorescence protein was restored, and plants containing the modified transgene were regenerated. Progeny analysis indicated Mendelian transmission of the converted transgene. The efficiency of gene conversion mediated by chimeric oligonucleotides in maize was estimated as 10(-4), which is 1-3 orders of magnitude higher than frequencies reported for gene targeting by homologous recombination in plants. The heritable changes in maize genes engineered by this approach create opportunities for basic studies of plant gene function and agricultural trait manipulation and also provide a system for studying mismatch repair mechanisms in maize.  (+info)

A tool for functional plant genomics: chimeric RNA/DNA oligonucleotides cause in vivo gene-specific mutations. (4/174)

Self-complementary chimeric oligonucleotides (COs) composed of DNA and modified RNA residues were evaluated as a means to (i) create stable, site-specific base substitutions in a nuclear gene and (ii) introduce a frameshift in a nuclear transgene in plant cells. To demonstrate the creation of allele-specific mutations in a member of a gene family, COs were designed to target the codon for Pro-196 of SuRA, a tobacco acetolactate synthase (ALS) gene. An amino acid substitution at Pro-196 of ALS confers a herbicide-resistance phenotype that can be used as a selectable marker in plant cells. COs were designed to contain a 25-nt homology domain comprised of a five-deoxyribonucleotide region (harboring a single base mismatch to the native ALS sequence) flanked by regions each composed of 10 ribonucleotides. After recovery of herbicide-resistant tobacco cells on selective medium, DNA sequence analyses identified base conversions in the ALS gene at the codon for Pro-196. To demonstrate a site-specific insertion of a single base into a targeted gene, COs were used to restore expression of an inactive green fluorescent protein transgene that had been designed to contain a single base deletion. Recovery of fluorescent cells confirmed the deletion correction. Our results demonstrate the application of a technology to modify individual genetic loci by catalyzing either a base substitution or a base addition to specific nuclear genes; this approach should have great utility in the area of plant functional genomics.  (+info)

Expression vectors for Methanococcus maripaludis: overexpression of acetohydroxyacid synthase and beta-galactosidase. (5/174)

A series of integrative and shuttle expression vectors was developed for use in Methanococcus maripaludis. The integrative expression vectors contained the Methanococcus voltae histone promoter and multiple cloning sites designed for efficient cloning of DNA. Upon transformation, they can be used to overexpress specific homologous genes in M. maripaludis. When tested with ilvBN, which encodes the large and small subunits of acetohydroxyacid synthase, transformants possessed specific activity 13-fold higher than that of the wild type. An expression shuttle vector, based on the cryptic plasmid pURB500 and the components of the integrative vector, was also developed for the expression of heterologous genes in M. maripaludis. The beta-galactosidase gene from Escherichia coli was expressed to approximately 1% of the total cellular protein using this vector. During this work, the genes for the acetohydroxyacid synthase (ilvBN) and phosphoenolpyruvate synthase (ppsA) were sequenced from a M. maripaludis genomic library.  (+info)

Deletion of the pyc gene blocks clavulanic acid biosynthesis except in glycerol-containing medium: evidence for two different genes in formation of the C3 unit. (6/174)

The beta-lactamase inhibitor clavulanic acid is formed by condensation of a pyruvate-derived C3 unit with a molecule of arginine. A gene (pyc, for pyruvate converting) located upstream of the bls gene in the clavulanic acid gene cluster of Streptomyces clavuligerus encodes a 582-amino-acid protein with domains recognizing pyruvate and thiamine pyrophosphate that shows 29.9% identity to acetohydroxyacid synthases. Amplification of the pyc gene resulted in an earlier onset and higher production of clavulanic acid. Replacement of the pyc gene with the aph gene did not cause isoleucine-valine auxotrophy in the mutant. The pyc replacement mutant did not produce clavulanic acid in starch-asparagine (SA) or in Trypticase soy broth (TSB) complex medium, suggesting that the pyc gene product is involved in the conversion of pyruvate into the C3 unit of clavulanic acid. However, the beta-lactamase inhibitor was still formed at the same level as in the wild-type strain in defined medium containing D-glycerol, glutamic acid, and proline (GSPG medium) as confirmed by high-pressure liquid chromatography and paper chromatography. The production of clavulanic acid by the replacement mutant was dependent on addition of glycerol to the medium, and glycerol-free GSPG medium did not support clavulanic acid biosynthesis, suggesting that an alternative gene product catalyzes the incorporation of glycerol into clavulanic acid in the absence of the Pyc protein. The pyc replacement mutant overproduces cephamycin.  (+info)

Fermentative metabolism of Bacillus subtilis: physiology and regulation of gene expression. (7/174)

Bacillus subtilis grows in the absence of oxygen using nitrate ammonification and various fermentation processes. Lactate, acetate, and 2,3-butanediol were identified in the growth medium as the major anaerobic fermentation products by using high-performance liquid chromatography. Lactate formation was found to be dependent on the lctEP locus, encoding lactate dehydrogenase and a putative lactate permease. Mutation of lctE results in drastically reduced anaerobic growth independent of the presence of alternative electron acceptors, indicating the importance of NADH reoxidation by lactate dehydrogenase for the overall anaerobic energy metabolism. Anaerobic formation of 2,3-butanediol via acetoin involves acetolactate synthase and decarboxylase encoded by the alsSD operon. Mutation of alsSD has no significant effect on anaerobic growth. Anaerobic acetate synthesis from acetyl coenzyme A requires phosphotransacetylase encoded by pta. Similar to the case for lctEP, mutation of pta significantly reduces anaerobic fermentative and respiratory growth. The expression of both lctEP and alsSD is strongly induced under anaerobic conditions. Anaerobic lctEP and alsSD induction was found to be partially dependent on the gene encoding the redox regulator Fnr. The observed fnr dependence might be the result of Fnr-induced arfM (ywiD) transcription and subsequent lctEP and alsSD activation by the regulator ArfM (YwiD). The two-component regulatory system encoded by resDE is also involved in anaerobic lctEP induction. No direct resDE influence on the redox regulation of alsSD was observed. The alternative electron acceptor nitrate represses anaerobic lctEP and alsSD transcription. Nitrate repression requires resDE- and fnr-dependent expression of narGHJI, encoding respiratory nitrate reductase. The gene alsR, encoding a regulator potentially responding to changes of the intracellular pH and to acetate, is essential for anaerobic lctEP and alsSD expression. In agreement with its known aerobic function, no obvious oxygen- or nitrate-dependent pta regulation was observed. A model for the regulation of the anaerobic fermentation genes in B. subtilis is proposed.  (+info)

Mutagenesis studies on the sensitivity of Escherichia coli acetohydroxyacid synthase II to herbicides and valine. (8/174)

Acetohydroxyacid synthase (EC 4.1.3.18, also known as acetolactate synthase) isoenzyme II from Escherichia coli is inhibited by sulphonylurea and imidazolinone herbicides, although it is much less sensitive than the plant enzyme. This isoenzyme is also unusual in that it is not inhibited by valine. Mutating S100 (Ser(100) in one-letter amino acid notation) of the catalytic subunit to proline increases its sensitivity to sulphonylureas, but not to imidazolinones. Mutating P536 to serine, as found in the plant enzyme, had little effect on the properties of the enzyme. Mutating E14 of the regulatory subunit to glycine, either alone or in combination with the H29N (His(29)-->Asn) change, did not affect valine-sensitivity.  (+info)

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.

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.

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.

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.

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.

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!

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.

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.

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.

'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.

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.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

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.

A gene is a specific sequence of nucleotides in DNA that carries genetic information. Genes are the fundamental units of heredity and are responsible for the development and function of all living organisms. They code for proteins or RNA molecules, which carry out various functions within cells and are essential for the structure, function, and regulation of the body's tissues and organs.

Each gene has a specific location on a chromosome, and each person inherits two copies of every gene, one from each parent. Variations in the sequence of nucleotides in a gene can lead to differences in traits between individuals, including physical characteristics, susceptibility to disease, and responses to environmental factors.

Medical genetics is the study of genes and their role in health and disease. It involves understanding how genes contribute to the development and progression of various medical conditions, as well as identifying genetic risk factors and developing strategies for prevention, diagnosis, and treatment.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

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.

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.

"Entrez Gene:ILVBL ilvB (bacterial acetolactate synthase)-like". "Acetolactate synthase, chloroplastic (P17597) < InterPro < ... The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid or acetohydroxyacid synthase, abbr. AHAS) is a protein ... Acetolactate synthase, also known as acetohydroxy acid synthase, is an enzyme specifically involved in the conversion of ... acetolactate synthases and acetohydroxyacid synthases". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular ...
ALS inhibitors: Acetolactate synthase (ALS; also known as acetohydroxyacid synthase, or AHAS) is part of the first step in the ... When resistance appeared farmers turned to a group of herbicides that block acetolactate synthase. Once again, ryegrass in ... Zhou Q, Liu W, Zhang Y, Liu KK (Oct 2007). "Action mechanisms of acetolactate synthase-inhibiting herbicides". Pesticide ... It works by inhibiting acetolactate synthase, an enzyme involved in producing branched chain amino acids. Dicamba, a ...
Chapter 10.2.1: Sulfonylurea acetolactate synthase inhibitors Duke SO (July 1990). "Overview of herbicide mechanisms of action ... such as the sulfonylureas inhibit the enzyme acetolactate synthase. Both enzymes are needed for plants to make branched-chain ... application to nitric oxide synthase". AAPS PharmSci. 2 (1): 68-77. doi:10.1208/ps020108. PMC 2751003. PMID 11741224. Loo JA, ...
Its mode of action is the inhibition of acetolactate synthase, group 2 of the Herbicide Resistance Action Committee's ... Tribenuron is an herbicide that acts as an acetolactate synthase inhibitor. For the purposes of herbicide resistance management ...
... is an ALS (acetolactate synthase) inhibitor herbicide, and is a sulfonylurea compound. It was discovered by ... Chlorsulfuron is an herbicide of the acetolactate synthase inhibitor (ALS inhibitor) class, HRAC (Herbicide Resistance Action ... the acetolactate synthase target-site mutation Pro-197-Ser - was found by Roux et al 2004 to be accompanied by a 37% recessive ...
Lrp alternatively activates and represses the expression of acetolactate synthase's (ALS) several isoenzymes. Lrp, in E. coli, ...
Various alleles of ALS - the acetolactate synthase gene - in a variety of species. The same amino acid substitution in all 43 ...
α-Acetolactic acid is produced from two molecules of pyruvic acid by acetolactate synthase. α-Acetolactic acid can also be ... The name α-acetolactate is used for anion (conjugate base), salts, and esters of α-acetolactic acid. Wood, B. J. B.; Holzapfel ... decarboxylated by alpha-acetolactate decarboxylase to produce acetoin. ...
... acetolactate synthases and acetohydroxyacid synthases". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular ... The binding of FAD at this site in acetolactate synthase and the binding of ADP at a cognate site in OXC are thought to play ... Maestri O, Joset F (August 2000). "Regulation by external pH and stationary growth phase of the acetolactate synthase from ... Oxalyl-CoA decarboxylase is structurally homologous to acetolactate synthase found in plants and other microorganisms, but OXC ...
These are broad-spectrum herbicides that kill plants weeds or pests by inhibiting the enzyme acetolactate synthase. In the ...
It functions via the inhibitition of acetolactate synthase enzyme, which catalyses the first step in biosynthesis of the ... "The Sulfonylurea Herbicide Sulfometuron Methyl Is an Extremely Potent and Selective Inhibitor of Acetolactate Synthase in ...
Enzymes involved in this biosynthesis include acetolactate synthase (also known as acetohydroxy acid synthase), acetohydroxy ... It begins with the condensation of two equivalents of pyruvate catalyzed by acetohydroxy acid synthase yielding α-acetolactate ... Anthranilate synthase is regulated by the gene products of trpE and trpG. trpE encodes the first subunit, which binds to ... Anthranilate synthase is also regulated by feedback inhibition: tryptophan is a co-repressor to the TrpR repressor. The ...
Hoegrass was mostly replaced by a group of herbicides that block acetolactate synthase, again helped by poor application ...
... specifically via acetolactate synthase inhibition. Compounds in this class include amidosulfuron, azimsulfuron, bensulfuron- ... Duggleby RG, McCourt JA, Guddat LW (March 2008). "Structure and mechanism of inhibition of plant acetohydroxyacid synthase". ...
Specifically, the RNAs are upstream of genes that encode a predicted acetolactate synthase, which is involved in the synthesis ...
Some populations of tall waterhemp have been reported resistant to acetolactate synthase inhibiting (ALS) herbicides and the ...
... the southeast of the United States and has already evolved resistances to dinitroaniline herbicides and acetolactate synthase ...
2019 to produce another novel male sterility and Triticum aestivum acetolactate synthase (TaALS) and Triticum aestivum acetyl- ...
The mode of action of flazasulfuron is the inhibition of the enzyme acetolactate synthase (ALS), which results in the ...
Enzymes involved in this biosynthesis include: Acetolactate synthase (also known as acetohydroxy acid synthase) Acetohydroxy ...
In Arabidopsis thaliana, using ZFN-assisted gene targeting, two herbicide-resistant genes (tobacco acetolactate synthase SuRA ...
... hydroxymethylbilane synthase, acetolactate synthase large subunit, hypothetical protein, DEAD/ DEAH box helicase and UDP-N- ... N-acetylalpha-d-glucosaminyl l-malate synthase BshA, YpdA family putative bacillithiol disulfide reductase, penicillin-binding ...
... a bacterial plant disease Acetolactate synthase, an enzyme Advanced Light Source, a synchrotron radiation facility ALSN, ...
Acetolactate synthase (ALS) inhibition is a frequent mode of action in many of the most widely used herbicides, with target ...
Acetolactate synthase Acetohydroxy acid isomeroreductase Dihydroxyacid dehydratase α-Isopropylmalate synthase α-Isopropylmalate ...
2-hydroxy-3-oxoadipate synthase EC 2.2.1.6: acetolactate synthase EC 2.2.1.7: 1-deoxy-D-xylulose-5-phosphate synthase EC 2.2. ... 2-ethylmalate synthase EC 2.3.3.7: 3-ethylmalate synthase EC 2.3.3.8: ATP citrate synthase EC 2.3.3.9: malate synthase EC 2.3. ... synthase EC 2.3.3.2: decylcitrate synthase EC 2.3.3.3: citrate (Re)-synthase EC 2.3.3.4: decylhomocitrate synthase EC 2.3.3.5: ... synthase EC 2.4.1.12: cellulose synthase (UDP-forming) EC 2.4.1.13: sucrose synthase EC 2.4.1.14: sucrose-phosphate synthase EC ...
... may refer to: Acetolactate synthase, a protein, abbreviated ALS or AHAS ALS herbicides/AHAS herbicides, ALS inhibitors/ ...
Enzymes involved in this biosynthesis include: Acetolactate synthase (also known as acetohydroxy acid synthase) Acetohydroxy ...
... acetolactate synthase EC 4.1.3.19: Now EC 2.5.1.56 EC 4.1.3.20: Now EC 2.5.1.57 EC 4.1.3.21: Now EC 2.3.3.14 EC 4.1.3.22: ... 11-diene synthase EC 4.2.3.25: S-linalool synthase EC 4.2.3.26: R-linalool synthase EC 4.2.3.27: isoprene synthase EC 4.2.3.28 ... α-santalene synthase EC 4.2.3.83: β-santalene synthase EC 4.2.3.84: 10-epi-γ-eudesmol synthase EC 4.2.3.85: α-eudesmol synthase ... cubebol synthase EC 4.2.3.92: (+)-γ-cadinene synthase EC 4.2.3.93: δ-guaiene synthase EC 4.2.3.94: γ-curcumene synthase EC 4.2. ...
EC 2.2.1.2 Acetolactate synthase EC 2.2.1.6 2-Succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase EC 2.2. ... Thiazole synthase EC 2.8.1.11: Molybdopterin synthase sulfurtransferase EC 2.8.1.12: Molybdopterin synthase EC 2.8.1.13: tRNA- ... Trans-feruloyl-CoA synthase EC 6.2.1.35: ACP-SH:acetate ligase EC 6.2.1.36: 3-hydroxypropionyl-CoA synthase EC 6.2.1.37: 3- ... Biotin synthase EC 2.8.1.7: Cysteine desulfurase EC 2.8.1.8: Lipoyl synthase EC 2.8.1.9: Molybdenum cofactor sulfurtransferase ...
"Entrez Gene:ILVBL ilvB (bacterial acetolactate synthase)-like". "Acetolactate synthase, chloroplastic (P17597) < InterPro < ... The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid or acetohydroxyacid synthase, abbr. AHAS) is a protein ... Acetolactate synthase, also known as acetohydroxy acid synthase, is an enzyme specifically involved in the conversion of ... acetolactate synthases and acetohydroxyacid synthases". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular ...
Evolution of herbicide resistance in weeds: initial frequency of target site-based resistance to acetolactate synthase- ... The frequency of individuals resistant to two acetolactate synthase (ALS)-inhibiting herbicides in three previously untreated ...
Acetolactate synthase isozyme 1 small subunit. A [auth E],. C [auth F],. E [auth G],. G [auth H]. 127. Escherichia coli K-12. ... Acetolactate synthase isozyme 1 large subunit. B [auth A],. D [auth B],. F [auth C],. H [auth D]. 562. Escherichia coli K-12. ... Molecular architecture of the acetohydroxyacid synthase holoenzyme.. Zhang, Y., Li, Y., Liu, X., Sun, J., Li, X., Lin, J., Yang ... The acetohydroxyacid synthase (AHAS) holoenzyme catalyzes the first step of branch-chain amino acid biosynthesis and is ...
The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors ... The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors Coordinates. PDB Format Method ... Pang, S.S. et al., The Crystal Structures of Klebsiella pneumoniae Acetolactate Synthase with Enzyme-bound Cofactor and with an ...
Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Deoxy-D-Xylulose Phosphate Synthase ( HRAC Group ... Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Enolpyruvyl Shikimate Phosphate Synthase ( HRAC ... Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Enolpyruvyl Shikimate Phosphate Synthase ( HRAC ... Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Microtubule Assembly ( HRAC Group 3 (Legacy K1). ...
Engineering herbicide-resistant rice plants through CRISPR/Cas9-mediated homologous recombination of acetolactate synthase. Mol ... Engineering herbicide-resistant rice plants through CRISPR/Cas9-mediated homologous recombination of acetolactate synthase. Mol ...
The alsS gene may encode an α-acetolactate synthase that catalyzes the conversion of pyruvate to α-acetolactate. The alsD gene ... may encode an α-acetolactate decarboxylase that catalyzes the conversion of α-acetolactate to (3R)-AC. The alsR gene, which is ... Since the reaction catalyzed by α-acetolactate decarboxylase is stereospecific and only leads to the formation of the (3R)-AC [ ... crystallization and preliminary X-ray crystallographic studies on acetolactate decarboxylase. Acta Crystallogr D Biol ...
Acetolactate Synthase (ALS) Inhibitors. By: Doug Goodale, Joe Neal, Katie Jennings 2024. Herbicide Injury Factsheets This ...
The acetoin pathway included a C83S mutant of the E. coli K-12 MG1655 acetolactate synthase (ilvB) and an acetolactate ... The acetolactate synthase was framed with the VtmoJ ribozyme gene, the BCD1 bicistronic design, and the RNase III R0.5 site, ... Rostgaard, J. B., Svendsen, I., and Oitese, M. (1987). Isolation and characterization of an alpha-acetolactate decarboxylase ... whereas the acetolactate decarboxylase was surrounded with the RiboJ ribozyme gene, the BCD2 bicistronic design, and the RNase ...
and Tohru Tominaga (2007) Nucleotide substitutions in the acetolactate synthase genes of sulfonylurea-resistant biotypes of ... and Tohru Tominaga (2007) Discovery of single-nucleotide mutations in acetolactate synthase genes by Ecotilling. Pesticide ...
keywords = "acetolactate synthase, amino acid, asparagine, gene family, glutamine, herbicide resistance, shikimate pathway, ...
acetolactate synthase catalytic subunit 8, 39. MMP0651. ilvH. acetolactate synthase 3 regulatory subunit 8, 39. ... phosphoribosylaminoimidazole-succinocarboxamide synthase 8, 112, 143. MMP0572. slyD. FKBP-type peptidylprolyl isomerase 11, 96 ...
... lactis strains harbor acetolactate synthase (EC 2.2.1.6) and acetolactate decarboxylase (EC 4.1.1.5) genes. These genes are ... cardiolipin synthase A; ddl, non van d-Ala-d-Ala ligase; eis, N-acetyltransferase, kanamycin resistance; emtA, rRNA ... salicylate synthase; psaA, manganese ABC transporter); 14, stress survival (clpC, endopeptidase Clp ATP-binding chain C; clpE, ... undecaprenyl diphosphate synthase; wbtLB, glucose-1-phosphate thymidylyltransferase; ugdC, UDP-glucose 6-dehydrogenase; hasC, ...
HRAC 2 (Inhibition of Acetolactate Synthase ). *HRAC 3 (Inhibition of Microtubule Assembly) ...
Pyruvate (pyruvic acid) is converted to acetolactate by acetolactate synthase (also called acetohydroxy acid synthase). ... Acetolactate is converted to dihydroxy isovalerate by acetohydroxy acid isomeroreductase (also called ketoacid reductoisomerase ... by the action of isopropyl malate synthase, deviates into the leucine synthesis pathway. There are 3 pyruvate family amino ...
MoA: Inhibition of acetolactate synthase ALS (acetohydroxyacid synthase AHAS). Chemistry: Sulfonylurea. Herbicide: ...
Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Deoxy-D-Xylulose Phosphate Synthase ( HRAC Group ... Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Enolpyruvyl Shikimate Phosphate Synthase ( HRAC ... Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Enolpyruvyl Shikimate Phosphate Synthase ( HRAC ... Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). Inhibition of Microtubule Assembly ( HRAC Group 3 (Legacy K1). ...
Acetolactate Synthase Structure, Function, and Drug Development. More.... Last Updated: Jul 18, 2023 ... synthases, and transaminases. Pyridoxal phosphate and pyridoxamine phosphate are also involved in the break-down of amino acids ...
... "acetolactate synthase catalytic subunit [Ensembl]. central domain, C-terminal TPP binding domain, N-terminal TPP binding domain ... ","Methoxy mycolic acid synthase 2 MmaA2 (methyl mycolic acid synthase 2) (MMA2) (hydroxy mycolic acid synthase) [Ensembl]. ... ","glutamate synthase subunit small chain [Ensembl]. Dihydroprymidine dehydrogenase domain II, 4Fe-4S dicluster domain, FAD/NAD ... ","Probable tyrosyl-tRNA synthase TyrS (TYRRS) [Ensembl]. tRNA synthetases class I (W and Y) [Interproscan].","protein_coding ...
One class of herbicides, the acetolactate synthase (ALS)-inhibitors, target the enzyme ALS. Normally, the ALS enzyme carries ...
They inhibit the enzyme acetolactate synthase (ALS), which synthesizes the branched chain amino acids. When used in the field, ...
Acetolactate Synthase (ALS). * Microbiology * *Reverse Transcriptase. *HIV Integrase. *HCV Protease. *HIV Protease ...
Vegetative growth and competitiveness of common cocklebur resistant and susceptible to acetolactate synthase-inhibiting ...
SedgeHammer is based on chlorsulfuron-methyl, an ingredient that acts as an acetolactate synthase inhibitor (ALS). This enzyme ...
  • The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid or acetohydroxyacid synthase, abbr. (wikipedia.org)
  • The acetohydroxyacid synthase (AHAS) holoenzyme catalyzes the first step of branch-chain amino acid biosynthesis and is essential for plants and bacteria. (rcsb.org)
  • In weed species, resistance to herbicides inhibiting acetohydroxyacid synthase (AHAS) is often conferred by genetic mutations at one of six codons in the AHAS gene. (weedscience.org)
  • We identified the biosynthetic gene cluster (oca BGC) that encodes a modular polyketide synthase (PKS) system for assembling the polyene-polyol chain of octacosamicin A. Our analysis suggested that the N-hydroxyguanidine unit originates from a 4-guanidinobutyryl-CoA starter unit, while the PKS incorporates an α-hydroxyketone moiety using a (2R)-hydroxymalonyl-CoA extender unit. (bvsalud.org)
  • Acetolactate synthase, also known as acetohydroxy acid synthase, is an enzyme specifically involved in the conversion of pyruvate to acetolactate: 2 CH3COCO2− → −O2CC(OH)(CH3)COCH3 + CO2 The reaction uses thiamine pyrophosphate in order to link the two pyruvate molecules. (wikipedia.org)
  • Five different acetolactate synthase (ALS) mutations (Pro-197-Leu, Pro- 197-Ser, Pro-197-His, Asp-376-Glu, and Trp-574-Leu) were detected in different resistant populations. (weedscience.com)
  • Guang-Xi Wang, Mui-Keng Tan, Sujay Rakshit, Hiromasa Saitoh, Ryohei Terauchi, Toshiyuki Imaizumi, Takanori Ohsako and Tohru Tominaga (2007) Discovery of single-nucleotide mutations in acetolactate synthase genes by Ecotilling. (kpu.ac.jp)
  • A single amino acid substitution from Serine 653 to Asparagine has led to resistance to Inhibition of Acetolactate Synthase as indicated in the table below. (weedscience.org)
  • The frequency of individuals resistant to two acetolactate synthase (ALS)-inhibiting herbicides in three previously untreated populations of Lolium rigidum was determined. (edu.au)
  • Acetolactate synthase is catalytic enzyme involved in the biosynthesis of various amino acids. (wikipedia.org)
  • The most frequent resistances were to acetyl-CoA carboxylase (ACCase), acetolactate synthase (ALS), 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) inhibitors, and combinations thereof. (cambridge.org)
  • Multiple resistance has evolved to herbicides in the Groups 22 (Legacy D), and Inhibition of Enolpyruvyl Shikimate Phosphate Synthase HRAC Group 9 (Legacy G). These particular biotypes are known to have resistance to glyphosate, and paraquat and they may be cross-resistant to other herbicides in the Groups 22 (Legacy D), and Inhibition of Enolpyruvyl Shikimate Phosphate Synthase HRAC Group 9 (Legacy G). (weedresearch.com)
  • The highest degree of similarity is found with bacterial acetolactate synthases (AHAS), which are enzymes that catalyze the first step in branched-chain amino acid biosynthesis. (nih.gov)
  • Experiments * confirmed the predictions of the model, i.e. knocking out lactate * dehydrogenase and overexpressing NADH oxidase increased the * flux through the acetolactate synthase branch from 0 to 75% * of measured product formation rates. (nih.gov)
  • Comment: ilvIH (or ilvGM) is a two-subunit enzyme that forms acetolactate or acetohydroxybutanoate. (lbl.gov)
  • Group 9 (Legacy G) herbicides are known as Inhibition of Enolpyruvyl Shikimate Phosphate Synthase (Inhibition of EPSP synthase). (weedscience.com)
  • Overuse of acetolactate synthase (ALS)-inhibiting herbicides in rice has led to the evolution of halosulfuron-resistant rice flatsedge in Arkansas and Mississippi. (roadsideweeds.com)
  • 8. Acetolactate synthase regulatory subunits play divergent and overlapping roles in branched-chain amino acid synthesis and Arabidopsis development. (nih.gov)
  • A single amino acid substitution from Proline 197 to Arginine has led to resistance to Inhibition of Acetolactate Synthase as indicated in the table below. (weedscience.com)

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