2-Acetolactate Mutase: 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.Acetolactate Synthase: 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.Methylmalonyl-CoA Mutase: 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.Phosphoglycerate Mutase: An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.Oxo-Acid-Lyases: Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.Bisphosphoglycerate Mutase: 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.Herbicides: Pesticides used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Some plants develop HERBICIDE RESISTANCE.Sulfonylurea CompoundsIsoleucine: 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.Acetoin: A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.Valine: 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.Pontederiaceae: 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, Branched-Chain: Amino acids which have a branched carbon chain.Herbicide Resistance: Diminished or failed response of PLANTS to HERBICIDES.Thiamine Pyrophosphate: 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.Hydroxybutyrates: Salts and esters of hydroxybutyric acid.Intramolecular Transferases: 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.Lactates: Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.CobamidesEscherichia coli: 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.Pyruvic Acid: 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)Butyrates: Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.Physicians: Individuals licensed to practice medicine.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Lawyers: Persons whose profession is to give legal advice and assistance to clients and represent them in legal matters. (American Heritage Dictionary, 3d ed)Child Advocacy: Promotion and protection of the rights of children; frequently through a legal process.Questionnaires: Predetermined sets of questions used to collect data - clinical data, social status, occupational group, etc. The term is often applied to a self-completed survey instrument.Attitude of Health Personnel: Attitudes of personnel toward their patients, other professionals, toward the medical care system, etc.Bites, Human: Bites inflicted by humans.Prephenate Dehydrogenase: An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Molecular Sequence Data: 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.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Synteny: The presence of two or more genetic loci on the same chromosome. Extensions of this original definition refer to the similarity in content and organization between chromosomes, of different species for example.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Arabidopsis Proteins: Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.Gene Expression Profiling: The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.Herpestidae: The family of agile, keen-sighted mongooses of Asia and Africa that feed on RODENTS and SNAKES.Osteochondrodysplasias: Abnormal development of cartilage and bone.Gene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Ketoglutaric Acids: A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Citric Acid Cycle: A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.Citrate (si)-Synthase: Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.Glutamate Dehydrogenase: An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.Ketoglutarate Dehydrogenase ComplexPatents as Topic: Exclusive legal rights or privileges applied to inventions, plants, etc.Inventions: A novel composition, device, or process, independently conceived de novo or derived from a pre-existing model.Clostridium beijerinckii: A species of gram-positive bacteria in the family Clostridiaceae, capable of solventogenesis, and isolated from SOIL, infected WOUNDS, fermenting OLIVES, and spoiled CANDY.Biotechnology: Body of knowledge related to the use of organisms, cells or cell-derived constituents for the purpose of developing products which are technically, scientifically and clinically useful. Alteration of biologic function at the molecular level (i.e., GENETIC ENGINEERING) is a central focus; laboratory methods used include TRANSFECTION and CLONING technologies, sequence and structure analysis algorithms, computer databases, and gene and protein structure function analysis and prediction.Solvents: Liquids that dissolve other substances (solutes), generally solids, without any change in chemical composition, as, water containing sugar. (Grant & Hackh's Chemical Dictionary, 5th ed)Butanols: Isomeric forms and derivatives of butanol (C4H9OH).Clostridium: A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.

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)

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Butamax suggests that a broad construction is most consistent with the intrinsic evidence and skill in the art, namely, "an enzyme that is structurally similar to acetohydroxy acid isomeroreductase or ketol acid reductoisomerase ["KARI"] enzymes 1 known by the EC number 1.1.1.86 2 and that converts acetolactate to 2,3-dihydroxyisovalerate." (D.I. 492 at 9) Under this construction, to determine whether an enzyme literally meets the claim term, a skilled artisan would: (1) compare the enzymes amino acid sequence to the sequences of known KARI enzymes having EC number 1.1.1.86 (D.I. 492 at 10; [p. 599] D.I. 494 at ¶ 45); and (2) test the enzyme for activity using a standard KARI assay, e.g., the assay described in a 1969 reference by Arfin & Umbarger 3 (D.I. 492 at 10; D.I. 495 at ¶¶ 41-43). According to Butamax, "[t]his two prong analysis, consistent with the intrinsic evidence, allows a skilled artisan to come to a conclusion that an enzyme literally meets the KARI claim element." (D.I. 492 ...
Our previous studies revealed that the staphylococcal protein Gcp is essential for bacterial growth; however, the essential function of Gcp remains undefined. In this study, we demonstrated that Gcp plays an important role in the modulation of the br
The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine ...
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1OZH: The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
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Strain Information. E. coli K-12 MG1655. Description. Genotype: F- lambda- ilvG- rfb-50 rph-1. Serotype: OR:H48:K- This strain was sequenced by the Blattner laboratory because it approximates wild-type E. coli and has been maintained as a laboratory strain with minimal genetic manipulation, having only been cured of the temperate bacteriophage lambda and F plasmid by means of ultraviolet light and acridine orange, respectively. (Blattner, et al. 1997). The mutations listed in the genotype are present in most K-12 strains and were probably acquired early in the history of the laboratory strain. A frameshift at the end of rph results in decreased pyrE expression and a mild pyrimidine starvation, such that the strain grows 10 to 15% more slowly in pyrimidine-free medium than in medium containing uracil (Jensen 1993). The ilvG- mutation is a frameshift that knocks out acetohydroxy acid synthase II (Lawther, et al. 1982). The rfb-50 mutation is an IS5 insertion that results in the absence of ...
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... phosphoglycerate mutase MeSH D08.811.399.894.200 --- amino acid isomerases MeSH D08.811.399.894.200.200 --- alanine racemase ... acetolactate synthase MeSH D08.811.913.200.650 --- transaldolase MeSH D08.811.913.200.825 --- transketolase MeSH D08.811. ... chorismate mutase MeSH D08.811.399.520.250.500 --- prephenate dehydratase MeSH D08.811.399.520.250.750 --- prephenate ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 --- phosphoglucomutase MeSH D08.811.399.520.750.700 --- ...
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, ...
... 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)-a-D-glucan 1-a-D- ... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.3.1: deleted EC 5.4.3.2: lysine 2,3-aminomutase EC 5.4 ... methylaspartate mutase EC 5.4.99.2: methylmalonyl-CoA mutase EC 5.4.99.3: 2-acetolactate mutase EC 5.4.99.4: 2- ...
451 (2): 157-161. ISSN 0014-5793. PMID 10371157.. *^ a b Batista AP, Pereira MM (March 2011). "Sodium influence on energy ... 169 (2): 300-304. ISSN 0014-5793. PMID 6325245.. *^ Galkin A, Dröse S, Brandt U (December 2006). "The proton pumping ... 409 (2): 491-9. doi:10.1042/BJ20071162. PMID 17916065.. *^ Sahni, Prateek V.; Zhang, Jimmy; Sosunov, Sergey; Galkin, Alexander ... doi:10.1016/0378-8741(82)90002-2. PMID 7132401.. *^ Nakamaru-Ogiso E, Han H, Matsuno-Yagi A, Keinan E, Sinha SC, Yagi T, ...
Step two is the NADPH+ + H+ - dependent reduction of α-acetolactate and migration of the methane groups to produce α, β- ... This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. The ... It begins with the reaction of two pyruvate molecules catalyzed by Acetohydroxy acid synthase yielding α-acetolactate. ... The loop formed by strands 2 and 3 forms an anti-terminator and translation of the his genes will continue and histidine will ...
Category:EC 5.4 (intramolecular transferases -- mutases)Edit. *Category:EC 5.4.2 *Phosphoglucomutase (EC 5.4.2.2) ... Acetolactate synthase EC 2.2.1.6. *2-Succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase EC 2.2.1.9 ... Category:EC 1.3.2 (with a cytochrome as acceptor). *Category:EC 1.3.3 (with oxygen as acceptor) *Protoporphyrinogen oxidase EC ... Category:EC 1.4 (act on the CH-NH2 group of donors)Edit. *Category:EC 1.4.3 *Monoamine oxidase EC 1.4.3.4 ...
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 ... acetolactate synthase MeSH D08.811.913.200.650 --- transaldolase MeSH D08.811.913.200.825 --- transketolase MeSH D08.811. ... chorismate mutase MeSH D08.811.399.520.250.500 --- prephenate dehydratase MeSH D08.811.399.520.250.750 --- prephenate ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 --- phosphoglucomutase MeSH D08.811.399.520.750.700 --- ...
Enzyme (substance) {90668006 , SNOMED-CT } Substance with mutase mechanism of action (substance) {130945002 , SNOMED-CT } ...
5.4.99.13 isobutyryl-CoA mutase 5.4.99.14 4-carboxymethyl-4-methylbutenolide mutase ...
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 ...
MLE, malolactic enzyme; LDH, lactate dehydrogenase; CL, citrate lyase; OAD, oxaloacetate decarboxylase; ALS, α-acetolactate ... phosphoglycerate mutase; ENO, enolase; PK, pyruvate kinase; PO, pyruvate oxidase; ALDH, alcohol dehydrogenase; FK, fructokinase ... α-acetolactate decarboxylase (OENOO_54034), acetoin reductase (OENOO_48023) and diacetyl reductase (OENOO_43013). All these ... Figure 2. Comparative analyses of the predicted and the actual proteome of O. oeni ATCC BAA-1163. Frequency distribution of the ...
Substance with mutase mechanism of action (substance). Code System Preferred Concept Name. Substance with mutase mechanism of ... Methylaspartate mutase (substance) {83682009 , SNOMED-CT } Methylmalonyl-coenzyme A mutase (substance) {56024005 , SNOMED-CT } ... Bisphosphoglycerate mutase (substance) {2168009 , SNOMED-CT } Chorismate mutase (substance) {4067000 , SNOMED-CT } Cycloartenol ... Substance with mutase mechanism of action (substance) {130945002 , SNOMED-CT } Parent/Child (Relationship Type) 2-acetolactate ...
... 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)-a-D-glucan 1-a-D- ... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.3.1: deleted EC 5.4.3.2: lysine 2,3-aminomutase EC 5.4 ... methylaspartate mutase EC 5.4.99.2: methylmalonyl-CoA mutase EC 5.4.99.3: 2-acetolactate mutase EC 5.4.99.4: 2- ...
... and acetolactate synthase (T478_0886, T478_0887), and vitamin B7 is a required coenzyme for the acetyl-/propionyl-CoA ... methylmalonyl-CoA mutase (T478_0628), methionine synthase (T478_1032), and ribonucleoside reductase (T478_1341). The genome ... Reductive N2O production from NO2− has been demonstrated in enrichment cultures of Ca. N. brevis (10) and in N. maritimus (30, ... 2), and Ca. N. brevis had higher recruitment in nearly twice as many samples (SI Appendix, Dataset S4). Two regions of the Ca. ...
Phosphoglycerate mutase. Phosphoglycerate mutase (GPM) converts 3-phosphoglycerate into 2-phosphoglycerate in the later part of ... Probably via nonspecific decarboxylation of acetolactate formed in valine biosynthesis. Butanediol dehydrogenase. Glucose-6- ... Phosphoglycerate mutase (EC 5.4.2.1). Pyruvate decarboxylase (EC 4.1.1.1). Alcohol dehydrogenase (EC 1.1.1.1). Glycerol-3-P ... Phosphoglycerate mutase (GPM). Enolase (ENO). Pyruvate kinase (PYK). Pyruvate decarboxylase (PDC). Alcohol dehydrogenase (ADH) ...
Acetolactate synthase (ALS) is the first enzyme in the BCAA synthesis pathway. Although the functional contribution of ALS to ... Aspartate kinase, chorismate mutase, TyrA domain. AHAS: Acetohydroxyacid synthase. AIP: ALS-Interacting Protein ... Action mechanisms of acetolactate synthase-inhibiting herbicides. Pestic Biochem Physiol. 2007;89(2):89-96.View ArticleGoogle ... The formation of acetolactate. J Biol Chem. 1958;233(5):1156-60.PubMedGoogle Scholar. ...
ribostamycin:4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(gamma-L-glutamylamino)-(S)-2- ...
... phosphoglycerate mutase, are involved in central carbon metabolism and energy generation These proteins would be expected in ... SACOL1758 34 acetolactate synthase, catabolic (budB) SACOL2199 33 ribosomal protein L22 (rplV) SACOL2234 33 CTP synthase (pyrG ... phosphoglycerate mutase, and enolase are generally found to be downregulated in stationary phase when compared to post ... Q5HCV2 3 0 Acetolactate synthase, catabolic Q5HDZ7,Q5HDZ7 0 2 Chorismate mutase/phospho 2 dehydro 3 deoxyheptonate aldolase ...
2S,5R)-2,6-Diamino-5-hydroxyhexanoic Acid use Hydroxylysine (3 beta, 17 alpha)-19-Norpregn-4-en-20-yne-3,17 diol Diacetate 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 ...
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 ...
2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-hexahydro-3-isobutyl-9,10-dimethoxy- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... Mutase. 2-Acetylaminofluorene. 2-Alanyl-Leucine Enkephalin use Enkephalin, Leucine-2-Alanine ... 3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer ...
mutase activity. Mutase-Prephenate Dehydratase, Chorismate. Mutase-Prephenate Dehydrogenase, Chorismate. Mutase, 2-Acetolactate ... MutS Homolog 2, Colon Cancer, Nonpolyposis Type 1 (E. coli) Gene. mutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli) ... MutL Homolog 1, Colon Cancer, nonpolyposis type 2 (E. coli) Gene. mutL homolog 1, colon cancer, nonpolyposis type 2 (E. coli) ... mutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli). ... mutS homolog 2 (E. coli) protein, rat. mutS homolog 2 (E. coli ...
... α-acetolactate synthase; alsD, α-acetolactate decarboxylase; pdhABCD, pyruvate dehydrogenase complex; pta, ... phosphoglycerate mutase; eno, enolase; pykA, pyruvate kinase. Pentose-P pathway genes: yqjJ, putative glucose-6-P dehydrogenase ... α-acetolactate synthase; alsD, α-acetolactate decarboxylase; pdhABCD, pyruvate dehydrogenase complex; pta, ... phosphoglycerate mutase; eno, enolase; pykA, pyruvate kinase. Pentose-P pathway genes: yqjJ, putative glucose-6-P dehydrogenase ...
Chorismate mutase activity specified by the aroQ domain could supply PPA for both PHE and TYR biosynthesis. Likewise, HisHb, ... acetolactate synthase, phenylalanine hydroxylase, prephenate dehydratase and formyltetrahydrofolate deformylase. Recruitment of ... The fusion physically links chorismate mutase (which forms PPA) with TyrAc_Δ (which utilizes PPA). The two protein domains of ... Chen S, Vincent S, Wilson DB, Ganem B: Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia ...
The two glycolytic enzymes fructose-1,6-bisphosphate aldolase (PF1956; 4.5-fold; 1 h) and phosphoglycerate mutase (PF1959; 2.2- ... Sulfometuron methyl-sensitive and methyl-resistant acetolactate synthases of the archaebacteria Methanococcus spp. J. Bacteriol ... Molecular characterization of phosphoglycerate mutase in archaea. FEMS Microbiol. Lett. 212:111-120. ... and acetolactate synthase (PF0935). As shown in Table 3, the specific activities of both enzymes are at least fivefold higher ...
451 (2): 157-161. ISSN 0014-5793. PMID 10371157.. *^ a b Batista AP, Pereira MM (March 2011). "Sodium influence on energy ... 169 (2): 300-304. ISSN 0014-5793. PMID 6325245.. *^ Galkin A, Dröse S, Brandt U (December 2006). "The proton pumping ... 409 (2): 491-9. doi:10.1042/BJ20071162. PMID 17916065.. *^ Sahni, Prateek V.; Zhang, Jimmy; Sosunov, Sergey; Galkin, Alexander ... doi:10.1016/0378-8741(82)90002-2. PMID 7132401.. *^ Nakamaru-Ogiso E, Han H, Matsuno-Yagi A, Keinan E, Sinha SC, Yagi T, ...
Acetolactate synthase; KEGG- cac-CAC3169 3.9e-146 ilvB; acetolactate synthase large subunit K01652; COG- COG0028 Thiamine ... Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the ... Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the ... Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the ...
Atsumi, S., Li, Z., and Liao, J.C. (2009). Acetolactate Synthase from Bacillus subtilis Serves as a 2-Ketoisovalerate ... Development of a Mutagenesis, Expression and Purification System for Yeast Phosphoglycerate Mutase". European Journal of ... The Two Analogous Phosphoglycerate Mutases of Escherichia Coli". FEBS Letters 455, no. 3 (1999): 344-48. ... Table 2: This table shows all enzymatic parameters which were used for our dynamic model. Enzyme. kcat [-]. KM [mM]. Reference ...
1. Acetolactate synthase Cthe_2516, 2517, 2714; 2. Ketol-acid reductoisomerase Cthe_2518; 3. Dihydroxy-acid dehydratase Cthe_ ... Phosphoglycerate mutase Cthe_0140; 13. Enolase Cthe_0143; 14. PEP Carboxykinase Cthe_2874; 15. Malate dehydrogenase Cthe_0345; ... 1. Glucose-6-phosphate isomerase Cthe_0217; 2. Transketolase subunit A Cthe_2443, 2704; 3. Ribulose-5-phosphate 3-epimerase ... Additional file 2: Table S1. Details of metabolites detected in the time course analysis of C. thermocellum grown on ...
  • The de novo synthesis of BCAAs has been an historical object of attention for two main reasons: this pathway is a known target for at least five independent classes of inhibitory herbicides [ 2 ] and, secondly, animals lack the necessary genes encoding enzymes for BCAA synthesis thus requiring that this class of essential amino acids be obtained via dietary intake. (biomedcentral.com)
  • According to our pathway map there are 42 electrons needed for the production of one molecule isobutanol, if CO 2 is used as sole carbon source. (igem.org)
  • Dehydrogenases dedicated to L-tyrosine (TYR) biosynthesis comprise a family of TyrA homologs that have different specificities for the cyclohexadienyl substrate: ones specific for L-arogenate (AGN), ones specific for prephenate (PPA), and those that are able to use both [ 1 , 2 ]. (biomedcentral.com)
  • Other cold-inducible proteins in E. coli include initiation factor 2 (IF2) ( 7 , 13 ), ribosomal binding factor A (RbfA) ( 22 ), and DEAD-box RNA helicase ( 4 , 23 , 37 ), all of which associate with the ribosome and are believed to play a role in protein synthesis. (asm.org)
  • Therefore, a better understanding of the molecular mechanisms related to the stress adaptation and technical performance of O. oeni is crucial for the characterization and selection of strains for industrial purposes [ 2 , 3 ]. (royalsocietypublishing.org)
  • To achieve our aims we reduced the complex system shown in Figure 1 to the version shown in Figure 2. (igem.org)
  • Four different B. subtilis sugar-specific transport systems representing the four PTS classes (see Fig. 2 ) are shown. (asmscience.org)
  • Transcriptional analyses using whole-genome DNA microarrays representing 2,065 open reading frames (ORFs) in the P. furiosus genome showed that cells undergo three very different responses at 72°C: an early shock (1 to 2 h), a late shock (5 h), and an adapted response (occurring after many generations at 72°C). Each response involved the up-regulation in the expression of more than 30 ORFs unique to that response. (asm.org)
  • It revealed that 42 electrons are needed for the production of one isobutanol molecule from CO 2 . (igem.org)