An enzyme that catalyzes the first step in the biosynthetic pathway to LEUCINE, forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. This enzyme was formerly listed as EC 4.1.3.12.
An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.
A species of gram-positive bacteria in the family Clostridiaceae. It is distinctive for its ability to ferment ETHANOL to caproic acid.
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A species of gram-negative, aerobic, rod-shaped bacteria found in hot springs of neutral to alkaline pH, as well as in hot-water heaters.
Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.
Substituted thioglucosides. They are found in rapeseed (Brassica campestris) products and related cruciferae. They are metabolized to a variety of toxic products which are most likely the cause of hepatocytic necrosis in animals and humans.
A plant family of the order Capparales, subclass Dilleniidae, class Magnoliopsida. They are mostly herbaceous plants with peppery-flavored leaves, due to gluconapin (GLUCOSINOLATES) and its hydrolysis product butenylisotrhiocyanate. The family includes many plants of economic importance that have been extensively altered and domesticated by humans. Flowers have 4 petals. Podlike fruits contain a number of seeds. Cress is a general term used for many in the Brassicacea family. Rockcress is usually ARABIS; Bittercress is usually CARDAMINE; Yellowcress is usually RORIPPA; Pennycress is usually THLASPI; Watercress refers to NASTURTIUM; or RORIPPA or TROPAEOLUM; Gardencress refers to LEPIDIUM; Indiancress refers to TROPAEOLUM.
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.
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.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.
Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.
Organized activities related to the storage, location, search, and retrieval of information.
Materials that have a limited and usually variable electrical conductivity. They are particularly useful for the production of solid-state electronic devices.
An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.
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.
A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.
A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.
Rare congenital X-linked disorder of lipid metabolism. Barth syndrome is transmitted in an X-linked recessive pattern. The syndrome is characterized by muscular weakness, growth retardation, DILATED CARDIOMYOPATHY, variable NEUTROPENIA, 3-methylglutaconic aciduria (type II) and decreases in mitochondrial CARDIOLIPIN level. Other biochemical and morphological mitochondrial abnormalities also exist.
A plant genus of the family CELASTRACEAE that is a source of triterpenoids and diterpene epoxides such as triptolide.
Voluntary cooperation of the patient in taking drugs or medicine as prescribed. This includes timing, dosage, and frequency.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The complete gene complement contained in a set of chromosomes in a fungus.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Databases devoted to knowledge about specific genes and gene products.
The functional hereditary units of FUNGI.
A plant genus in the family ROSACEAE, order Rosales, subclass Rosidae. It is best known as a source of the edible fruit (apple) and is cultivated in temperate climates worldwide.
An inherited neurological developmental disorder that is associated with X-LINKED INHERITANCE and may be lethal in utero to hemizygous males. The affected female is normal until the age of 6-25 months when progressive loss of voluntary control of hand movements and communication skills; ATAXIA; SEIZURES; autistic behavior; intermittent HYPERVENTILATION; and HYPERAMMONEMIA appear. (From Menkes, Textbook of Child Neurology, 5th ed, p199)
A broad category of sleep disorders characterized by either hypersomnolence or insomnia. The three major subcategories include intrinsic (i.e., arising from within the body) (SLEEP DISORDERS, INTRINSIC), extrinsic (secondary to environmental conditions or various pathologic conditions), and disturbances of circadian rhythm. (From Thorpy, Sleep Disorders Medicine, 1994, p187)
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.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.
The reproductive organs of plants.
A conditionally essential nutrient, important during mammalian development. It is present in milk but is isolated mostly from ox bile and strongly conjugates bile acids.
The study of the structure, growth, function, genetics, and reproduction of bacteria, and BACTERIAL INFECTIONS.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

Inhibition of Escherichia coli isoleucine biosynthesis by isoleucine tetrazole. (1/43)

Growth of a derivative of Escherichia coli K-10 was strongly inhibited by 2 times 10(-4) M L-5(1-amino-2-methylbutyl)-tetrazole (isoleucine tetrazole). Growth inhibition was reversed by isoleucine, threonine, glycyl-L-isoleucine, or glycyl-L-threonine, and, in a valine-resistant mutant, by L-valine. Partial reversal of growth inhibiton was effected by L-leucine, L-methionine, or L-homoserine. The tetrazole inhibited the activity of the biosynthetic threonine deaminase (EC 4.2.1.16 L-threonine hydrolyase [deaminating]), the inhibition being relieved by L-valine. The tetrazole also inhibited isoleucyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.5 L-isoleucine: tRNA ligase [adenosine monophosphate]), but was without effect on the activities of alpha-isopropylmalate synthetase or acetohydroxy acid synthetase. One class of isoleucine tetrazole-resistant mutants produced biosynthetic threonine deaminases which were no longer subject to feedback inhibition by either isoleucine or the tetrazole.  (+info)

Reversible, coenzyme-A-mediated inactivation of biosynthetic condensing enzymes in yeast: a possible regulatory mechanism. (2/43)

alpha-Isopropylmalate synthase [3-hydroxy-4-methyl-3-carboxyvalerate 2-oxo-3-methylbutyrate-lyase (CoA-acetylating); EC 4.1.3.12], the enzyme catalyzing the first committed step in leucine biosynthesis, and homocitrate synthase [3-hydroxy-3-carboxyadipate 2-oxoglutarate-lyase (CoA-acetylating); EC 4.1.3.21], the first enzyme in lysine biosynthesis in yeast, are rapidly inactivated in the presence of low concentrations of coenzyme A, a product of both reactions. Closely related compounds like 3-dephospho-coenzyme A or oxidized coenzyme A are almost without effect, as are other sulfhydryl compounds. Citrate (si)-synthase [citrate oxaloacetate-lyase (pro-3S-CH2-COO-minus leads to acetyl-CoA); EC 4.1.3.7] appears to be completely resistant against inactivation by coenzyme A. Inactivated alpha-isopropylmalate and homocitrate synthases can be reactivated by dialysis, but not by adding excess substrate. Protection against coenzyme-A-mediated inactivation is provided by relatively high concentrations of the alpha-ketoacid substrate or the specific end product inhibitor of each of the two enzymes. The coenzyme-A-mediated inactivation of alpha-isopropylmalate synthase has been more closely investigated. It requires the presence of divalent metal ions, with Zn++being most effective. The inactivation does not require molecular oxygen. It occurs in the presence of low concentrations of substrates and is observed in toluene-treated cells. These results, together with evidence that alpha-isopropylmalate synthase and homocitrate synthase are located in the mitochondria, suggest a mechanism by which increasing intra-mitochondrial coenzyme A concentrations might serve as a signal of decreasing acetyl-coenzyme A levels, triggering a temporary inactivation of biosynthetic acetyl-coenzyme A-consuming reactions in order to channel the available acetyl-coenzyme A into the citrate cycle.  (+info)

A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway. (3/43)

Arabidopsis and other Brassicaceae produce an enormous diversity of aliphatic glucosinolates, a group of methionine (Met)-derived plant secondary compounds containing a beta-thio-glucose moiety, a sulfonated oxime, and a variable side chain. We fine-scale mapped GSL-ELONG, a locus controlling variation in the side-chain length of aliphatic glucosinolates. Within this locus, a polymorphic gene was identified that determines whether Met is extended predominantly by either one or by two methylene groups to produce aliphatic glucosinolates with either three- or four-carbon side chains. Two allelic mutants deficient in four-carbon side-chain glucosinolates were shown to contain independent missense mutations within this gene. In cell-free enzyme assays, a heterologously expressed cDNA from this locus was capable of condensing 2-oxo-4-methylthiobutanoic acid with acetyl-coenzyme A, the initial reaction in Met chain elongation. The gene methylthioalkylmalate synthase1 (MAM1) is a member of a gene family sharing approximately 60% amino acid sequence similarity with 2-isopropylmalate synthase, an enzyme of leucine biosynthesis that condenses 2-oxo-3-methylbutanoate with acetyl-coenzyme A.  (+info)

Leucine biosynthesis in fungi: entering metabolism through the back door. (4/43)

After exploring evolutionary aspects of branched-chain amino acid biosynthesis, the review focuses on the extended leucine biosynthetic pathway as it operates in Saccharomyces cerevisiae. First, the genes and enzymes specific for the leucine pathway are considered: LEU4 and LEU9 (encoding the alpha-isopropylmalate synthase isoenzymes), LEU1 (isopropylmalate isomerase), and LEU2 (beta-isopropylmalate dehydrogenase). Emphasis is given to the unusual distribution of the branched-chain amino acid pathway enzymes between mitochondrial matrix and cytosol, on the newly defined role of Leu5p, and on regulatory mechanisms governing gene expression and enzyme activity, including new evidence for the metabolic importance of the regulation of alpha-isopropylmalate synthase by coenzyme A. Next, structure-function relationships of the transcriptional regulator Leu3p are addressed, defining its dual role as activator and repressor and discussing evidence in support of the self-masking model. Recent data pointing at a more extended Leu3p regulon are discussed. An overview of the layered controls of the extended leucine pathway is provided that includes a description of the newly recognized roles of Ilv5p and Bat1p in maintaining mitochondrial integrity. Finally, branched-chain amino acid biosynthesis and its regulation in other fungi are summarized, the question of leucine as metabolic signal is addressed, and possible directions of future research in this area are outlined.  (+info)

Repression of the tyrosine, lysine, and methionine biosynthetic pathways in a hisT mutant of Salmonella typhimurium. (5/43)

A comparison was made of the repressibility of certain enzymes in the tyrosine, methionine, and lysine biosynthetic pathways in wild-type Salmonella typhimurium and a hisT mutant. The results show that (i) tyrosine represses the synthesis of the tyrosine-sensitive 3-deoxy-D-arabino-heptulsonic acid 7-phosphate synthetase and the tyrosine aminotransferase to the same extent in a hisT mutant as in wild type and (ii) there is no detectable alteration in the extent to which methionine represses O-succinylhomoserine synthetase or in the extent to which lysine represses the lysine-sensitive beta-aspartokinase as a result of the hisT mutation.  (+info)

Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis. (6/43)

The leucine biosynthetic pathway is essential for the growth of Mycobacterium tuberculosis and is a potential target for the design of new anti-tuberculosis drugs. The crystal structure of alpha-isopropylmalate synthase, which catalyzes the first committed step in this pathway, has been determined by multiwavelength anomalous dispersion methods and refined at 2.0-A resolution in complex with its substrate alpha-ketoisovalerate. The structure reveals a tightly associated, domain-swapped dimer in which each monomer comprises an (alpha/beta)(8) TIM barrel catalytic domain, a helical linker domain, and a regulatory domain of novel fold. Mutational and crystallographic data indicate the latter as the site for leucine feedback inhibition of activity. Domain swapping enables the linker domain of one monomer to sit over the catalytic domain of the other, inserting residues into the active site that may be important in catalysis. The alpha-ketoisovalerate substrate binds to an active site zinc ion, adjacent to a cavity that can accommodate acetyl-CoA. Sequence and structural similarities point to a catalytic mechanism similar to that of malate synthase and an evolutionary relationship with an aldolase that catalyzes the reverse reaction on a similar substrate.  (+info)

Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway. (7/43)

Three leuA-like protein-coding sequences were identified in Leptospira interrogans. One of these, the cimA gene, was shown to encode citramalate synthase (EC 4.1.3.-). The other two encoded alpha-isopropylmalate synthase (EC 4.1.3.12). Expressed in Escherichia coli, the citramalate synthase was purified and characterized. Although its activity was relatively low, it was strictly specific for pyruvate as the keto acid substrate. Unlike the citramalate synthase of the thermophile Methanococcus jannaschii, the L. interrogans enzyme is temperature sensitive but exhibits a much lower K(m) (0.04 mM) for pyruvate. The reaction product was characterized as (R)-citramalate, and the proposed beta-methyl-d-malate pathway was further confirmed by demonstrating that citraconate was the substrate for the following reaction. This alternative pathway for isoleucine biosynthesis from pyruvate was analyzed both in vitro by assays of leptospiral isopropylmalate isomerase (EC 4.2.1.33) and beta-isopropylmalate dehydrogenase (EC 1.1.1.85) in E. coli extracts bearing the corresponding clones and in vivo by complementation of E. coli ilvA, leuC/D, and leuB mutants. Thus, the existence of a leucine-like pathway for isoleucine biosynthesis in L. interrogans under physiological conditions was unequivocally proven. Significant variations in either the enzymatic activities or mRNA levels of the cimA and leuA genes were detected in L. interrogans grown on minimal medium supplemented with different levels of the corresponding amino acids or in cells grown on serum-containing rich medium. The similarity of this metabolic pathway in leptospires and archaea is consistent with the evolutionarily primitive status of the eubacterial spirochetes.  (+info)

Asp578 in LEU4p is one of the key residues for leucine feedback inhibition release in sake yeast. (8/43)

We identified a new mutation, Asp578Tyr, in alpha-isopropylmalate synthase (a LEU4 gene product) that releases leucine feedback inhibition and causes hyperproduction of isoamyl alcohol (i-AmOH) in sake yeast. Spontaneous sake yeast mutants that express resistance to 5,5,5-trifluoro-DL-leucine (TFL) were isolated, and a mutant strain, TFL20, was characterized at the genetic and biochemical levels. An enzyme assay for alpha-isopropylmalate synthase showed that strain TFL20 was released from feedback inhibition by L-leucine. Furthermore, DNA sequencing of the LEU4 gene for a haploid of the mutant TFL20 revealed that aspartic acid in position 578 changes to tyrosine. A comparison of the three-dimensional structures of wild-type LEU4p and mutant LEU4D578Yp by the homology modeling method showed that Asp578 is important for leucine feedback inhibition. We conclude that the mutation from Asp to Tyr in 578 is a novel change causing release from leucine feedback inhibition.  (+info)

Methylthioalkylmalate synthase (MAM) catalyzes the committed step in the side chain elongation of Met, yielding important precursors for glucosinolate biosynthesis in Arabidopsis thaliana and other Brassicaceae species. MAM is believed to have evolved from isopropylmalate synthase (IPMS), an enzyme …
AE006468.LEUA Location/Qualifiers FT CDS_pept complement(132167..133738) FT /codon_start=1 FT /transl_table=11 FT /gene=leuA FT /locus_tag=STM0113 FT /product=2-isopropylmalate synthase FT /EC_number=2.3.3.13 FT /note=similar to E. coli 2-isopropylmalate synthase FT (AAC73185.1); Blastp hit to AAC73185.1 (523 aa), 92% FT identity in aa 1 - 523 FT /db_xref=EnsemblGenomes-Gn:STM0113 FT /db_xref=EnsemblGenomes-Tr:AAL19077 FT /db_xref=GOA:P15875 FT /db_xref=InterPro:IPR000891 FT /db_xref=InterPro:IPR002034 FT /db_xref=InterPro:IPR005671 FT /db_xref=InterPro:IPR013709 FT /db_xref=InterPro:IPR013785 FT /db_xref=InterPro:IPR036230 FT /db_xref=UniProtKB/Swiss-Prot:P15875 FT /protein_id=AAL19077.1 FT /translation=MSQQVIIFDTTLRDGEQALQASLSAKEKLQIALALERMGVDVMEV FT GFPVSSPGDFESVQTIARTIKNSRVCALARCVEKDIDVAAQALKVADAFRIHTFIATSP FT MHIATKLRSTLDEVIERAVYMVKRARNYTDDVEFSCEDAGRTPVDDLARVVEAAINAGA FT RTINIPDTVGYTMPFEFAGIISGLYERVPNIDKAIISVHTHDDLGIAVGNSLAAVHAGA FT ...
University of Canterbury Library α-Isopropylmalate synthase (α-IPMS) is responsible for catalysing the first committed step in leucine biosynthesis. This pathway is found in plants and microorganisms, including pathogenic bacteria such as Mycobacterium tuberculosis and Neisseria meningitidis. α-IPMS catalyses a Claisen condensation reaction between α-ketoisovalerate (KIV) and acetyl coenzyme A (AcCoA) to form the product α-isopropylmalate (IPM). This enzyme undergoes feedback inhibition by the end product of the pathway, leucine. This regulation allows the control of the rate leucine biosynthesis. This project focuses on the α-IPMS enzymes from M. tuberculosis and N. meningitidis (MtuIPMS and NmeIPMS). These α-IPMS enzymes are homodimeric in structure. Each monomer consists of a catalytic domain which comprises of a (β/α)8 barrel fold, two subdomains and a regulatory domain, to which the allosteric binding of the natural inhibitor leucine occurs. The mechanism by which the allosteric ...
A plant pathway that initiates with the formation of citramalate from pyruvate and acetyl-CoA by citramalate synthase (CMS) is proven to contribute to the synthesis of α-ketoacids and vital odor-active esters in apple (Malus × domestica) fruit. Microarray screening led to the invention of a gene with excessive amino acid similarity to 2-isopropylmalate synthase (IPMS). However, practical …. Citramalate synthase yields a biosynthetic pathway for isoleucine and straight- and branched-chain ester formation in ripening apple fruit Read More ». ...
First, to understand the relation between IPMs and $\phi$-divergences, the necessary and sufficient conditions under which these classes intersect are derived: the total variation distance is shown to be the only non-trivial $\phi$-divergence that is also an IPM. This shows that IPMs are essentially different from $\phi$-divergences. Second, empirical estimates of several IPMs from finite i.i.d. samples are obtained, and their consistency and convergence rates are analyzed. These estimators are shown to be easily computable, with better rates of convergence than estimators of $\phi$-divergences. Third, a novel interpretation is provided for IPMs by relating them to binary classification, where it is shown that the IPM between class-conditional distributions is the negative of the optimal risk associated with a binary classifier. In addition, the smoothness of an appropriate binary classifier is proved to be inversely related to the distance between the class-conditional distributions, measured ...
IPMS is a keyboard shorthand-acrynm for I Pissed MySelf. It is used instead of or with relation to terms like lol, lmao, and rofl Usually used in response to something funny.
Hi Chaps and Chapesses, I dont suppose anyone would have either of these kits for sale do they? Im not paying some of the collectors prices that Im seeing on auction sites, but it anyone has either off these kits at rrp, or lower, please let me know. Oh, the Gene Simmons kit need sto be the older long box, not the recent round box ...
Leu4 enzymatic activity is inhibited by leucine and CoA, and the amino acid residues responsible for this property have been identified (7). Although no detailed biochemical characterization of the LEU9-encoded isozyme has been performed, it has been shown that it is less sensitive to leucine inhibition than Leu4 is (3).. It is noteworthy that the leucine biosynthesis intermediate α-IPM plays a dual cellular role. On the one hand, it acts as an intermediate in leucine biosynthesis (5, 6), and on the other, it acts as the coactivator of the Leu3 master regulator (6), which modulates the expression of a number of genes within and beyond amino acid metabolism (6). At low α-IPM concentrations, Leu3 acts as a transcriptional repressor, while at high α-IPM concentrations, it acts as an activator (6). It has been recently found that α-IPM could also have a role in the ability of Leu3 to determine the chronological life span of yeast (11, 12).. A LEU4 deletion (leu4Δ) results in leucine bradytrophy ...
I second every thing thats been said here. As a long time friend (I hope) or pain in the ass (more likely) Ive got to throw in a few thoughts. The bad news is that this happens to us all. The good news is that were around for it to happen. This wouldnt be a Dave story without the next words: Many years back - I built plastic models. Some aircraft but mostly tanks. I was deeply involved in the International Plastic Modelers Society (IPMS) and I was able to build models that were competitive at the national level. By the way if you think that gun people are different and at least a little strange check out the modeling subculture. Its a refuge for people who have very severe cases of Aspergers Syndrome. Ask me how I know. Anyway when I hit around 40 I discovered that my eyes just wouldnt work to do the close up level of detail that I wanted. My eye doc said that even with bifocals or close up reading glasses there wasnt much he could do for me. So I regretfully put the xacto knives and ...
Such a component will lead to new generation of personalized information systems that on one hand provide visual information to the user and on the other hand are sensitive to visual interaction. Using some sort of modified eyeglasses the user will perceive her or his environment the usual way, additional optical information will be provided using the information system (Augmented Reality). This information may be adapted to the overall context, both unconsciously and by intent. Without using the hands or spoken commands the user can control the presented information just with movement or actions of the eyes. At SID 2008, Fraunhofer IPMS will present a respective demonstrator for the first time, which clearly shows the future possibilities of this technology.. ...
Since 25 years our highly reliable SKiiP IPMs are driving light rails, trams and subways all over the world. SEMIKRON stands also for innovative solutions for auxiliary power supplies.
16 June 2014 at Doha Helicopters Club House Branch: IPMS/Doha Modeler: Michael Yare Country of Residence: United Kingdom Chapter: IPMS/Doha Name of Model: UH43D Choctaw Scale: 1/72 Manufacturer: Hobby Boss Comments: Built Out of Box, painted with Revell Acrylics, and built with limited tools and materials
Low-Side Gate Driver}]},{id:16901,link:/products/discrete-power-modules/power-modules/intelligent-power-modules-ipms?blockId=13124,name:Intelligent Power Modules (IPMs),products:[{partId:STK541UC62K-E,description:Intelligent Power Module (IPM), 600 V, 10 A}]}],documentations:[{taxonomyId:13124,documentType:Package Drawing,documentOfficialType:Package Drawings,abbreviation:drawing,numberOf:6},{taxonomyId:13124,documentType:Design & Development Tools,documentOfficialType:Design & Development Tools,abbreviation:tools,numberOf:1},{taxonomyId:13124,documentType:Data Sheet,documentOfficialType:Data Sheets,abbreviation:Datasheets,numberOf:7},{taxonomyId:13124,documentType:Application Notes,documentOfficialType:Application Notes,abbreviation:AppNotes,numberOf:4},{taxonomyId:13124,documentType:Eval Board,documentOfficialType:Evaluation Board ...
We develop an efficient homogeneous and self-dual interior-point method (IPM) for the linear programs arising in economic model predictive control (MPC) of constrained linear systems with linear objective functions. The algorithm is based on a Riccati iteration procedure, which is adapted to the linear system of equations solved in homogeneous and self-dual IPMs. Fast convergence is further achieved by means of a recent warm-start strategy for homogeneous and self-dual IPMs. We implement the algorithm in MATLAB and C. Its performance is tested using a conceptual power management case study. Closed loop simulations show that 1) the proposed algorithm is significantly faster than several state-of-the-art IPMs based on sparse linear algebra, and 2) warm-start reduces the average number of iterations by 35-40%.. ...
Meanwhile, NaMLab has explored ferroelectric properties in atomic layer deposition (ALD) based thin-films of doped HfO2, and has achieved revolutionary results (LINK). A variety of dopant materials (Si, Al, Ge, Y, Gd, La and Sr) with a crystal radius ranging from 50 to 130 pm has been studied in addition to a mixed Hf1-xZrxO2. The aim is to develop a memory concept with the HfO2 based ferroelectric transistors (FeFET) as building blocks. The FeFET is a long-term contender for an ultra-fast, low-power and non-volatile memory technology. In these devices the information is stored as a polarization state of the gate dielectric and can be read non-destructively as a shift of the threshold voltage. The advantage of a FeFET memory compared to the Flash memory is its faster access times and much lower power consumption at high data rates. In the framework of a project together with GLOBALFOUNDRIES and Fraunhofer IPMS, which was funded by the Free State of Saxony, a one-transistor (1T) FeFET eNVM was ...
Hi guys, Ive been really busy recently, work, moving house, trying to get to most shows on weekends etc, its been non-stop. Loads going on in the background, I have a few kits that are nearing completion (see RFI soon) but decided to keep them off BM due to time reasons but Im putting this up as its a really unusual-unseen built kit.., Ive also just set up a new SIG with the IPMS called Scale Water Bombers, basically, anything thats dropped water or retardant etc over the years from Ford Trimotors to DC-10s... one aircraft that Ive always been fond of is the AJ-1 Savage and two were used for aerial firefighting so Im going to try and replicate that using the lovely Mach2 kit. Some photos - Lovely patina seen on the box, Im guessing from having a nice long holiday up in a loft Mach 2 AJ-2 Savage 1/72nd by Totallyrad.co.uk, on Flickr Bang up-to-date 3D CAD style instructions Mach 2 AJ-2 Savage 1/72nd by Totallyrad.co.uk, on Flickr Tamiya-like mouldings. Mach 2 AJ-2 Savage 1/72nd by ...
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1DR8: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
1a05: Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism.
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AE006468.PE320 Location/Qualifiers FT CDS_pept 374197..374823 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=STM0330 FT /product=putative 3-isopropylmalate isomerase FT (dehydratase), subunit with LeuC FT /note=similar to E. coli isopropylmalate isomerase subunit FT (AAC73182.1); Blastp hit to AAC73182.1 (201 aa), 39% FT identity in aa 3 - 193 FT /db_xref=EnsemblGenomes-Gn:STM0330 FT /db_xref=EnsemblGenomes-Tr:AAL19284 FT /db_xref=GOA:Q8ZRI9 FT /db_xref=InterPro:IPR000573 FT /db_xref=InterPro:IPR004431 FT /db_xref=InterPro:IPR015928 FT /db_xref=InterPro:IPR033940 FT /db_xref=UniProtKB/Swiss-Prot:Q8ZRI9 FT /protein_id=AAL19284.1 FT /translation=MDTFKQISGRIAPMLEPNIDTDVIMPKQFLKGIDRQGLDKGVFFD FT RRFMAGGQPNPDFILNMPGWQSATFLLVGPNFGCGSSREHAVWGLKQLGVRGLIGSTFA FT GIFDDNCQRNGILTVSLDEPALARLAQLAASADTNSITVSLDRCEITTAEETISFVISE FT LKRAMLAAGEDAIAWTLQYLPEIENFEVAHYSRRPWLKRPASPRG atggatacgt ttaagcaaat cagcgggcga attgcgccga tgctggaacc gaatatcgac 60 actgatgtga ttatgccaaa acagttcctg ...
Chemical Entities of Biological Interest (ChEBI) is a freely available dictionary of molecular entities focused on small chemical compounds.
The invention relates to tetrazole derivatives of bile acids, processes for their preparation, and use of these compounds as medicaments and cholesterol lowering agents. The tetrazole-bile acid derivatives are of the formula G1--X--G2, where G1 is H, a bile acid radical, or a bile acid radical which is modified on the hydroxyl functions and/or on the carboxyl group, X is a single bond or a bridge group between G1 and G2, and G2 is of the formula: ##STR1##
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_2013 (SAUSA300_RS11070); symbol: leuD; product: isopropylmalate isomerase small subunit
SWISS-MODEL Repository entry for A0A5S3QAK9 (A0A5S3QAK9_9PSED), 3-isopropylmalate dehydratase small subunit. Pseudomonas protegens
떨어져 있던 미토콘드리아와 소포체가 만나면 MAM이 형성되면서 칼슘의 이동통로가 되는데, 이 때 미토콘드리아로 칼슘이 과도하게 들어가면 미토콘드리아의 기능이 저하되면서 질환이 발생하게 된다. 최근에 MAM은 세포 내 신호전달이 오가는 허브로 주목받고 있으며, 실제로 많은 신경퇴행성질환 환자들의 유전자 변성이 해당 부위에서 발견된 바 있다 ...
Norvaline (abbreviated as Nva) is an amino acid with the formula CH3(CH2)2CH(NH2)CO2H. The compound is an isomer of the more common amino acid valine. Like most other α-amino acids, norvaline is chiral. It is a white, water-soluble solid. Norvaline is a non-proteinogenic unbranched-chain amino acid. It has previously been reported to be a natural component of an antifungal peptide of Bacillus subtilis. Norvaline and other modified unbranched chain amino acids have received attention because they appear to be incorporated in some recombinant proteins found in E. coli. Its biosynthesis has been examined. The incorporation of Nva into peptides reflects the imperfect selectivity of the associated aminoacyl-tRNA synthetase. In Miller-Urey experiments probing prebiotic synthesis of amino acids, norvaline, but also norleucine, are produced. Norvaline is known to promote tissue regeneration and muscle growth, and to become a precursor in the penicillin biosynthetic pathway. Norvaline and norleucine ...
5-Amino-1, 2, 3, 4-Tetrazole Potassium Salt CAS 136369-04-5 specifications & features from suppliers/manufacturer We offer 5-Amino-1, 2, 3, 4-tetrazole potassium salt for competitive price. Synonym: 1H-Tetrazol-5-amine potassium saltIf you need a specific offer, please send us your enquiry mentioning the quantity you are interested in, so we are able to give you
1DPZ: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
SWISS-MODEL Repository entry for B3DPI3 (LEUD_BIFLD), 3-isopropylmalate dehydratase small subunit. Bifidobacterium longum (strain DJO10A)
The highlight of the Argosy Universitys Sept. 29, 2017 graduation was the awarding of doctorate degrees to five graduates: (l-r) Dr. Johnny Siaumau Mapu, Dr. Lisa Tasi Vasai Mapu, Dr. Sheri Saeni Vasai -Taase, Dr. Lealofi Seau, and Dr. Usoalii Faiai Jr. Congratulations! [photo: Leua Aiono Frost]. ...
TY - JOUR. T1 - Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans. AU - Matsunami, Hideyuki. AU - Kawaguchi, Hiroshi. AU - Inagaki, Kenji. AU - Eguchi, Tadashi. AU - Kakinuma, Katsumi. AU - Tanaka, Hidehiko. N1 - Copyright: Copyright 2017 Elsevier B.V., All rights reserved.. PY - 1998. Y1 - 1998. N2 - We constructed an overexpression system in Escherichia coli of the leuB gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ferrooxidans. E. coli harboring the plasmid we constructed, pKK leuB1, produced 17-fold the enzyme protein of the expression system previously used for purification. The substrate specificity of the enzyme was analyzed with synthetic (2R, 3S)-3-alkylmalates. The 3-isopropylmalate dehydrogenase of Thiobacillus ferrooxidans had broad specificity toward the alkylmalates.. AB - We constructed an overexpression system in Escherichia coli of the leuB gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ...
Making his debut with Marvel Comics in 1962, Spiderman has been an icon of the comic superhero scene for over 50 years. Similarly, since the end of World War II, and with a bit more longevity, the VW Beetle has become a worldwide automotive icon in and of itself. Combine the two, and you get Polar Lights Marvel Comics The Amazing Spide
aconitate hydratase/ copper ion binding; FUNCTIONS IN: aconitate hydratase activity, copper ion binding; INVOLVED IN: response to cadmium ion; LOCATED IN: mitochondrion, chloroplast; EXPRESSED IN: 25 plant structures; EXPRESSED DURING: 16 growth stages; CONTAINS InterPro DOMAIN/s: Aconitase family, 4Fe-4S cluster binding site (InterPro:IPR018136), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha (InterPro:IPR001030), Aconitase A/isopropylmalate dehydratase small subunit, swivel (InterPro:IPR000573), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomain 2 (InterPro:IPR015932), Aconitase/Iron regulatory protein 2/2-methylisocitrate dehydratase (InterPro:IPR015934), Aconitase-like core (InterPro:IPR015937), Aconitase/3-isopropylmalate dehydratase, swivel (InterPro:IPR015928), Aconitase/iron regulatory protein 2 (InterPro:IPR006249), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomains 1 and 3 (InterPro:IPR015931); ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Bromine atom in PDB 3hpz: Crystal Structure of Mycobacterium Tuberculosis Leua Complexed With Bromopyruvate
Bauerle, R.H., Freundlich, M., Størmer, F.C. and Umbarger, H.E. (1964). Control of isoleucine, valine and leucine biosynthesis. II. Endproduct inhibition by valine of acetohydroxy acid synthetase in Salmonella typhimurium. Biochim. Biophys. Acta 92: 142-149. PMID 14243762. ...
Andreas Dräger, Marcel Kronfeld, Jochen Supper, Hannes Planatscher, Jørgen B. Magnus, Marco Oldiges, and Andreas Zell. Benchmarking Evolutionary Algorithms on Convenience Kinetics Models of the Valine and Leucine Biosynthesis in C. glutamicum. In Dipti Srinivasan and Lipo Wang, editors, IEEE Congress on Evolutionary Computation (CEC 2007), pages 896-903, Singapore, September 2007. IEEE Computational Intelligence Society, IEEE Press. [ DOI , details , link , pdf ...
One of the enzymes involved in a novel pyruvate pathway for isoleucine biosynthesis that is found in some, mainly archaeal, bacteria [1,2]. The enzyme can be inhibited by isoleucine, the end-product of the pathway, but not by leucine [2]. The enzyme is highly specific for pyruvate as substrate, as the 2-oxo acids 3-methyl-2-oxobutanoate, 2-oxobutanoate, 4-methyl-2-oxopentanoate, 2-oxohexanoate and 2-oxoglutarate cannot act as substrate [1,2 ...
SwissBioIsostere is a knowledgebase that provides information on more than 4.5 million molecular substructural replacements extracted from literature and that are useful for compound optimization in drug design. It provides a tool for replacements for a single substructure (e.g. an amide group) or a particular substructure of interest (e.g. carboxylic acid vs tetrazole).. ...
Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway.
It is well-known that azide salts can engage nitriles at elevated temperatures to yield tetrazoles; however, there is continued debate as to the mechanism of the reaction. Density functional theory calculations with the hybrid functional B3LYP have been performed to study different mechanisms of tetrazole formation, including concerted cycloaddition and stepwise addition of neutral or anionic azide species. The calculations presented here suggest a previously unsuspected nitrile activation step en route to an imidoyl azide, which then cyclizes to give the tetrazole. The activation barriers are found to correlate strongly with the electron-withdrawing potential of the substituent on the nitrile ...
MAJ Ulises Taymes - Executive Officer mo le USArmy Reserve i Tafuna lea ua faailoa maia lenei galuega o le a amata fausia i le lotoa a le Reserve i Tafuna ina ia kolenia ai fitafita i tomai tau fanafana. [L-R] 1st Lt. Melendez, Jose 411th PSC, LTC Clinton Seybold TSA/AS Det. Commander ma MAJ Ulisses Taymes TSG AS Det. Executive Officer. [ata: Leua Aiono Frost ...
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In enzymology , a valine-tRNA ligase ( EC 6.1.1.9 ) is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are ATP , L-valine , and tRNA(Val) , whereas its 3 products are AMP , diphosphate , and L-valyl-tRNA(Val) . This enzyme belongs to the family of ligases , to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP-forming) . Other names in common use include valyl-tRNA synthetase , valyl-transfer ribonucleate synthetase , valyl-transfer RNA synthetase , valyl-transfer ribonucleic acid synthetase , valine transfer ribonucleate ligase , and valine translase . This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis . Structural studies As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GAX , 1IVS , 1IYW , 1WK9 , and 1WKA . See also VARS References Berg P, Bergmann FH, Ofengand
Since treatment of uremic hyperphosphatemia still represents a major problem and phosphate-binding agents carry the well-known… Expand ...
The expert panel further noted that a poor response to IFN beta or GA should be defined as 2 or more relapses within a year of treatment, 1 significant relapse in the past year, a single relapse accompanied by new MRI activity (eg, new Gd+ lesions, new or enlarging T2 hyperintense lesions, or new T1 black holes) within 1 year, or a significant increase in MRI activity even in the absence of clinical activity.9 Natalizumab can also be given to patients who cannot tolerate IFN beta or GA (ie, those who develop flulike symptoms or injection-site reactions). Finally, patients fitting into a poor prognosis category may also benefit from natalizumab (Table 1). In these groups of patients, natalizumab as firstline therapy can be considered. For example, first-line therapy with natalizumab is recommended for patients with a devastating first relapse, or accompanying poor prognosis MRI activity (eg, T1 black hole formation, high number and volume of Gd+ lesions).9 ...
A systematic name for this compound is 2-aminohexanoic acid. The compound is an isomer of the more common amino acid leucine. ... It arises via the action of 2-isopropylmalate synthase on α-ketobutyrate. The incorporation of Nle into peptides reflects the ...
Specifically they are upstream of genes encoding 2-isopropylmalate synthase and related genes, which participate in the ...
... (isopropylmalate) is an intermediate in the biosynthesis of leucine, synthesized from oxoisovalerate by 2- ... isopropylmalate synthase and converted into isopropyl-3-oxosuccinate by 3-isopropylmalate dehydrogenase. Two isomers are ... and these are interconverted by isopropylmalate dehydratase.. ...
... isopropylmalate synthase, isopropylmalate isomerase, isopropylmalate dehydrogenase, and aminotransferase - are necessary for ... Acetohydroxyacid synthase is the first enzyme for the parallel pathway performing condensation reaction in both steps - ... acetohydroxyacid synthase, ketoacid reductoisomerase, dihydroxyacid dehygrogenase and aminotransferase.[3] Threonine ... Role in diabetes mellitus type 2[edit]. In addition to cell signaling, the mTOR pathway also plays a role in beta cell growth ...
... alpha-isopropylmalate synthase, alpha-isopropylmalic synthetase, isopropylmalate synthase, and isopropylmalate synthetase. This ... Mycobacterium tuberculosis α-isopropylmalate synthase requires a divalent metal ion, of which Mg2+ and Mn2+ give highest ... Kohlhaw G, Leary TR, Umbarger HE (1969). "Alpha-isopropylmalate synthase from Salmonella typhimurium Purification and ... Carvalho LP, Blanchard, JS (2006). "Kinetic and Chemical Mechanism of alpha-Isopropylmalate Synthase from Mycobacterium ...
... homocitrate synthases, (3) biotin carboxyl carrier proteins, (4) isopropylmalate synthases and (5) acyl-CoA carboxylase. The α- ... The generalized reaction for the NaT-DC family is: R - CO− 2 (in) + H+ (out) and 1 or 2 Na+ (in) ←→ R-H + CO2 (in) and 1 or 2 ... 31 (2): 473-87. doi:10.1046/j.1365-2958.1999.01189.x. PMID 10027965. S2CID 35018668. Balsera M, Buey RM, Li XD (March 2011). " ... 10 (2-4): 105-19. doi:10.1159/000091558. PMID 16645308. S2CID 22898166. Granjon T, Maniti O, Auchli Y, Dahinden P, Buchet R, ...
... riboflavin synthase MeSH D08.811.913.225.825 - spermidine synthase MeSH D08.811.913.225.912 - spermine synthase MeSH D08.811. ... 3-isopropylmalate dehydrogenase MeSH D08.811.682.047.524 - ketol-acid reductoisomerase MeSH D08.811.682.047.551 - lactate ... nitric oxide synthase type i MeSH D08.811.682.664.500.772.500 - nitric oxide synthase type ii MeSH D08.811.682.664.500.772.750 ... glycogen synthase kinases MeSH D08.811.913.696.620.682.700.429.500 - glycogen synthase kinase 3 MeSH D08.811.913.696.620.682. ...
... 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 ... squalene synthase EC 2.5.1.22: spermine synthase EC 2.5.1.23: sym-norspermidine synthase EC 2.5.1.24: discadenine synthase EC ... acridone synthase EC 2.3.1.160: vinorine synthase EC 2.3.1.161: lovastatin nonaketide synthase EC 2.3.1.162: taxadien-5a-ol O- ...
α-Isopropylmalate synthase catalyzes this condensation with acetyl CoA to produce α-isopropylmalate. An isomerase converts α- ... isopropylmalate to β-isopropylmalate. The third step is the NAD+-dependent oxidation of β-isopropylmalate catalyzed by a ... Leucine, like valine, regulates the first step of its pathway by inhibiting the action of the α-Isopropylmalate synthase. ... Enzymes involved in this biosynthesis include acetolactate synthase (also known as acetohydroxy acid synthase), acetohydroxy ...
Cystathionine beta synthase. *Porphobilinogen synthase. *3-Isopropylmalate dehydratase. *Urocanase. *Uroporphyrinogen III ... Tryptophan synthase (indole-salvaging). References[edit]. *^ Dunn MF, Niks D, Ngo H, Barends TR, Schlichting I (June 2008). " ... Tryptophan synthase or tryptophan synthetase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. ... Subunits: Tryptophan synthase typically exists as an α-ββ-α complex. The α and β subunits have molecular masses of 27 and 43 ...
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 ... 3-isopropylmalate dehydratase EC 4.2.1.34: (S)-2-methylmalate dehydratase EC 4.2.1.35: (R)-2-methylmalate dehydratase EC 4.2. ... d-cadinene synthase EC 4.2.3.14: pinene synthase EC 4.2.3.15: myrcene synthase EC 4.2.3.16: (4S)-limonene synthase EC 4.2.3.17 ... chorismate synthase EC 4.2.3.6: trichodiene synthase EC 4.2.3.7: pentalenene synthase EC 4.2.3.8: casbene synthase EC 4.2.3.9: ...
Cystathionine beta synthase. *Porphobilinogen synthase. *3-Isopropylmalate dehydratase. *Urocanase. *Uroporphyrinogen III ... Avermitilol synthase (EC 4.2.3.96) is an enzyme with systematic name avermitilol hydrolase (cyclizing, avermitilol-forming).[1] ... Avermitilol synthase at the US National Library of Medicine Medical Subject Headings (MeSH) ... 2E,6E)-farnesyl diphosphate + H2O ⇌. {\displaystyle \rightleftharpoons }. avermitilol + diphosphate. This enzyme requires Mg2+. ...
Cystathionine beta synthase. *Porphobilinogen synthase. *3-Isopropylmalate dehydratase. *Urocanase. *Uroporphyrinogen III ... The systematic name of this enzyme class is 6-phospho-D-gluconate hydro-lyase (2-dehydro-3-deoxy-6-phospho-D-gluconate-forming) ... 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O. Hence, this enzyme has one substrate, 6-phospho-D-gluconate, and two products, 2 ... 2-keto-3-deoxy-6-phosphogluconate, a product of the reaction catalysed by phosphogluconate dehydratase ...
Cystathionine beta synthase. *Porphobilinogen synthase. *3-Isopropylmalate dehydratase. *Urocanase. *Uroporphyrinogen III ... 5-dehydro-4-deoxy-D-glucarate + H2O. Hence, this enzyme has one substrate, D-glucarate, and two products, 5-dehydro-4-deoxy-D- ... glucarate and H2O. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds ...
Cystathionine beta synthase. *Porphobilinogen synthase. *3-Isopropylmalate dehydratase. *Urocanase. *Uroporphyrinogen III ... S)-2-amino-6-oxohexanoate + NH3 + phosphate. This enzyme is a pyridoxal-phosphate protein. ... This page was last edited on 2 May 2017, at 06:45. ... 2] This enzyme catalyses the following chemical reaction ...
Fatty acid synthase. *Beta-ketoacyl-ACP synthase. *Β-Ketoacyl ACP reductase. *3-Hydroxyacyl ACP dehydrase ... 3 (2): 121-6. doi:10.1002/ajh.2830030202. PMID 272120.. *^ Spiekerkoetter, U; Sun, B; Khuchua, Z; Bennett, MJ; Strauss, AW ( ... 22 (2): 427-31. doi:10.1042/bst0220427. PMID 7958339.. *. Zhao Y, Meng XM, Wei YJ, et al. (2003). "Cloning and characterization ... The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons ...
Acetolactate synthase Acetohydroxy acid isomeroreductase Dihydroxyacid dehydratase α-Isopropylmalate synthase α-Isopropylmalate ... 226 (2): 411-8. doi:10.1152/ajplegacy.1974.226.2.411. PMID 4855772. Brioche T, Pagano AF, Py G, Chopard A (August 2016). " ... 569 (Pt 2): 489-99. doi:10.1113/jphysiol.2005.098004. PMC 1464228. PMID 16195315. Archived from the original on 16 May 2008. ... 16 (2): 520-530. doi:10.1016/j.celrep.2016.05.092. PMC 4947548. PMID 27346343. Lynch CJ, Adams SH (December 2014). "Branched- ...
... promiscuity can be decreased as was the case of γ-humulene synthase (a sesquiterpene synthase) from Abies grandis that is known ... and the bifunctional isopropylmalate isomerase/homoaconitase from Pyrococcus horikoshii have revealed that active site loop ... Codexis). Another example is the possibility of using the promiscuous activities of cysteine synthase (cysM) towards ... including overexpression of the large component of a synthase in the absence of the amine transferase subunit), pathway bypass ...
... alpha-isopropylmalate synthase, alpha-isopropylmalic synthetase, isopropylmalate synthase, and isopropylmalate synthetase. This ... Mycobacterium tuberculosis α-isopropylmalate synthase requires a divalent metal ion, of which Mg2+ and Mn2+ give highest ... Kohlhaw G, Leary TR, Umbarger HE (1969). "Alpha-isopropylmalate synthase from Salmonella typhimurium Purification and ... Carvalho LP, Blanchard, JS (2006). "Kinetic and Chemical Mechanism of alpha-Isopropylmalate Synthase from Mycobacterium ...
Total deletion of yeast LEU4: further evidence for a second alpha-isopropylmalate synthase and evidence for tight LEU4-MET4 ... alpha-isopropylmalate synthase, and repression of the second two enzymes, alpha-isopropylmalate isomerase and beta- ... the gene that encodes alpha-isopropyl malate synthase I (alpha-IPM synthase I), and that the mutation involved a codon deletion ... Identification by functional analysis of the gene encoding alpha-isopropylmalate synthase II (LEU9) in Saccharomyces cerevisiae ...
"Yeast LEU4 encodes mitochondrial and nonmitochondrial forms of alpha-isopropylmalate synthase." J Biol Chem 263:368-374.3275644 ... Involved in 2-isopropylmalate synthase activity. Specific Function. Catalyzes the condensation of the acetyl group of acetyl- ... Acetyl-CoA + Alpha-Ketoisovaleric acid + water → 2-Isopropylmalic acid + hydron + Coenzyme A ... CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). ...
MAM is believed to have evolved from isopropylmalate synthase (IPMS), an enzyme … ... Methylthioalkylmalate synthase (MAM) catalyzes the committed step in the side chain elongation of Met, yielding important ... MAM is believed to have evolved from isopropylmalate synthase (IPMS), an enzyme involved in Leu biosynthesis, based on ... Methylthioalkylmalate synthase (MAM) catalyzes the committed step in the side chain elongation of Met, yielding important ...
Belongs to the alpha-IPM synthase/homocitrate synthase family.Curated. Phylogenomic databases. evolutionary genealogy of genes ... Putative (R)-citramalate synthase CimA (EC:2.3.1.182*Search proteins in UniProtKB for this EC number. ... IPR024890 Citramalate_synthase_CimA. IPR011830 LEU1_arch. IPR036230 LeuA_allosteric_dom_sf. IPR000891 PYR_CT. ... IPR024890 Citramalate_synthase_CimA. IPR011830 LEU1_arch. IPR036230 LeuA_allosteric_dom_sf. IPR000891 PYR_CT. ...
Belongs to the alpha-IPM synthase/homocitrate synthase family.Curated. Phylogenomic databases. evolutionary genealogy of genes ... R)-citramalate synthaseCurated (EC:2.3.1.182*Search proteins in UniProtKB for this EC number. ... Citramalate synthase1 Publication. ,p>Manually curated information that is based on statements in scientific articles for which ... Cells lacking this gene show a great reduction in citramalate synthase activity and are capable of growth in the absence of ...
UDeacetoxycephalosporin C synthase. Not Available. Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / NBRC ... Deacetoxycephalosporin C synthase. Kind. Protein. Organism. Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 ... 2-oxo monocarboxylic acid (CHEBI:16530) / Branched fatty acids (C00141) / Branched fatty acids (LMFA01020274) Targets. ... 2-isopropylmalate synthase activity. Gene Name. leuA. Uniprot ID. P9WQB3. Uniprot Name. 2-isopropylmalate synthase. Molecular ...
"Expression of a Brassica Isopropylmalate Synthase Gene in Arabidopsis Perturbs Both Glucosinolate and Amino Acid Metabolism, ... Isopropylmalate synthase (IPMS) is a key enzyme in the biosynthesis of the essential amino acid leucine, and ... Isopropylmalate synthase (IPMS) is a key enzyme in the biosynthesis of the essential amino acid leucine, and thus primary ... Alpha-isopropylmalate synthase from Salmonella typhimurium. Purification and properties. Kohlhaw, G.B.; Leary, T.R.; Umbarger, ...
A systematic name for this compound is 2-aminohexanoic acid. The compound is an isomer of the more common amino acid leucine. ... It arises via the action of 2-isopropylmalate synthase on α-ketobutyrate. The incorporation of Nle into peptides reflects the ...
2-Isopropylmalate synthase (IPMS) catalyzes the first step of leucine biosynthesis and is regulated via feedback inhibition by ... 2-oxoisovalerate Dehydrogenase (acylating). An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2- ... Alanine/glycine and rice powder containing ORS demonstrated some reduction in the stool output [2-5]. However, none of the ... 2. Reducing the concentration of glucose and sodium and thus osmolarity of ORS solution. ...
Hypothetical protein (NCBI blast: 3-oxoacyl-(Acyl-carrier-protein (ACP)) synthase III) ... 2c).. Open image in new window. Fig. 2 a Quantification of ammonia production from supernatant of YS11 cultured in YL medium. b ... 2b). YS11 could increase the pH in both conditions, highly suggesting that deamination of rich amino acids provided by yeast ... 2a, b). Transcriptomic analysis from RNA-seq at CaAc and NaAc conditions support that genes involved in deamination were ...
Homocitrate synthase, fungi/archaea (IPR011872). Short name: Homocitrate_synth_fun/arc Overlapping homologous superfamilies * ... Homocitrate synthase is located in the nucleus in the yeast Saccharomyces cerevisiae.. J. Biol. Chem. 272 10839-46 1997 ... Inactivation of homocitrate synthase causes lysine auxotrophy in copper/zinc-containing superoxide dismutase-deficient yeast ... GO:0004410 homocitrate synthase activity GO:0046912 transferase activity, transferring acyl groups, acyl groups converted into ...
cpec:CPE3_0650 V-type ATP synthase subunit A K02117 591 109 ( -) 31 0.355 62 -, 1 cpeo:CPE1_0649 V-type ATP synthase subunit A ... cper:CPE2_0650 V-type ATP synthase subunit A K02117 591 109 ( -) 31 0.355 62 -, 1 cpm:G5S_1059 V-type ATP synthase alpha chain ... bsj:UP17_12840 n-acetylglutamate synthase 113 107 ( -) 30 0.302 86 ,-, 1 bur:Bcep18194_A3254 SET domain protein K07117 176 107 ... part:PARC_a1678 cyclic pyranopterin phosphate synthase K03639 323 100 ( -) 29 0.426 54 -, 1 pbor:BSF38_04347 hypothetical ...
2008) Identification of a cryptic type III polyketide synthase (1,3,6,8-tetrahydroxynaphthalene synthase) from Streptomyces ... 2010) Mechanistic Studies on (s)-Norcoclaurine synthase and Dimethylallyltryptophan Synthase, The University of British ... 2011) Argininosuccinate synthase: at the center of arginine metabolism. Int. J. Biochem. Mol. Biol. 2, 8-23 pmid:21494411. ... 2007) Structure and mechanism of spermidine synthases. Biochemistry 46, 8331-8339 doi:10.1021/bi602498k pmid:17585781. ...
hor:Hore_19320 biotin synthase K03150 481 106 ( -) 30 0.300 80 -, 1 kln:LH22_18420 DNA polymerase III subunit alpha K02337 1160 ... aps:CFPG_592 D-citramalate synthase K09011 503 104 ( -) 30 0.315 89 -, 1 ars:ADJ73_08700 sodium:proton antiporter K03593 377 ... drt:Dret_2308 Carbamoyl-phosphate synthase L chain ATP- K01958 1229 101 ( -) 29 0.314 70 -, 1 dsh:Dshi_3044 feruloyl esterase ... pyr:P186_1158 tryptophan synthase subunit alpha K01695 233 114 ( -) 32 0.315 127 -, 1 avi:Avi_2699 ABC transporter nucleotide ...
It should be noted that E. coli has three acetohydroxyacid synthase isoenzymes (AHAS I, II, III), which are encoded by the ... Feedback inhibition of acetohydroxy acid synthase isoenzyme III by l-valine was removed by site-directed mutagenesis, and the ... encoding pantothenate synthase) and ilvA (encoding threonine dehydratase) genes were deleted; and the ilvBNC operon, encoding ... in which a feedback inhibition-resistant small subunit of acetohydroxy acid synthase (AHAS; encoded by ilvN) was generated by ...
Isopropylmalate synthase forward. TCCCGAATGCTTCTCCGACA. qPCR. Isopropylmalatesynthase_rev. GCTCTCTCTGTCTCCGATGTTGG. qPCR. Locus ... 2 Properties of the hax1 locus and its encoded regulatory factor. a Locus targeted by amdS integration in QM9414_Dhax1 strains ... 2d), which is a typical property of lncRNAs. To this end, the function of the lncRNA HAX1 as a regulatory factor of PBDE ... Additional file 2. Codon usage of the predicted hax1 gene. For each of the 64 codons potentially making up a protein the ...
... chorismate synthase, serine hydroxymethyltransferase, transaminase and glutamine synthetase (spots 495, 436, 187, 590, and 547 ... Figure 2. Examples of protein spots from BETL total protein extracts [spot 185 [M(G/TP)/WT(G/TP) = 0.97], spot 357 [M(G/TP)/WT( ... Figure 2 also includes an example of a protein, spot 185, with the glycosylation ratio of 0.97 that represented no significant ... The spot 547 in Figure 2 is one of those proteins with glycosylation levels in the mutant being more than two-fold of those in ...
Alpha-isopropylmalate synthase involved in leucine biosynthesis; catalyzes the conversion of 2-keto-isovalerate to 2- ... isopropylmalate; localizes to the mitochondria. 0 GO Terms curated. GO Slim Terms The yeast GO Slim terms are higher level ...
Alpha-isopropylmalate synthase.. Alpha-isopropylmalate synthetase.. Alpha-isopropylmalic synthetase.. Isopropylmalate synthase. ... All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-. SIB Swiss Institute of Bioinformatics , Disclaimer Back to ... Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O <=> (2S)-2-isopropylmalate + CoA. ... 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase (CoA-acetylating).. ...
Citramalate synthase yields a biosynthetic pathway for isoleucine and straight- and branched-chain ester formation in ripening ... Citramalate synthase yields a biosynthetic pathway for isoleucine and straight- and branched-chain ester formation in ripening ... Citramalate synthase yields a biosynthetic pathway for isoleucine and straight- and branched-chain ester formation in ripening ... A plant pathway that initiates with the formation of citramalate from pyruvate and acetyl-CoA by citramalate synthase (CMS) is ...
Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step ... alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4- ... Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step ... Structure:3BLE_A; Leptospira interrogans citramalate synthase binds Zn2+ and malonate, contacts at 4A.. - View structure with ...
acetohydroxyacid synthase. IPMS. isopropylmalate synthase. TFL. 5,5,5-trifluoro-dl-leucine. OMT. l-O-methylthreonine. MS. ... 2007). Two Arabidopsis genes (IPMS1 and IPMS2) encode isopropylmalate synthase, the branchpoint step in the biosynthesis of ... 2015). A feedback insensitive isopropylmalate synthase affects acylsugar composition in cultivated and wild tomato. Plant ... and isopropylmalate synthase 1 (IPMS1). In this model, OMR1 exerts primary control on Ile accumulation and functions ...
"2-isopropylmalate synthase" FT /EC_number="2.3.3.13" FT /note="similar to E. coli 2-isopropylmalate synthase FT (AAC73185.1); ...
... the earlier putative identification of the MJ1392 gene product as isopropylmalate synthase was incorrect. ... R )-Citramalate Synthase in Methanogenic Archaea Message Subject (Your Name) has forwarded a page to you from Journal of ... R )-Citramalate Synthase in Methanogenic Archaea. David M. Howell, Huimin Xu, Robert H. White ... Thus, this gene (cimA) encodes an (R)-citramalate synthase (CimA). This is the first identification of this enzyme, which is ...
"2-isopropylmalate synthase" FT /note="MG1655 equivalent: b0074" FT /db_xref="EnsemblGenomes-Gn:BWG_0070" FT /db_xref=" ...
A recombinant C. glutamicum strain was constructed by expressing a feedback-resistant leuA-encoded 2-isopropylmalate synthase ( ...
The modifications involved (1) deletion of the gene encoding the repressor LtbR to increase expression of leuBCD, (2) deletion ... The modifications involved (1) deletion of the gene encoding the repressor LtbR to increase expression of leuBCD, (2) deletion ... A recombinant C. glutamicum strain was constructed by expressing a feedback-resistant leuA-encoded 2-isopropylmalate synthase ( ... A recombinant C. glutamicum strain was constructed by expressing a feedback-resistant leuA-encoded 2-isopropylmalate synthase ( ...
cystathionine beta-synthase 1665 54 transporter protein 1666 56 sporulation proteins 1667 58 ferric uptake regulation protein ... 2 and SEQ ID No. 60 (Table 2).. TABLE 2 SEQ Orf ID No. Annotated function 1639 2 2-isopropylmalate synthase 1640 4 ... 50 (orf1663)), Dap synthase (SEQ ID No. 52 (orf1664)), and multidrug-efflux transporter (SEQ ID No. 54 (orf1665)). (B) ... This reaction is catalyzed by the concerted actions of a Dap synthase (VioB/ZWA5A) and an ornithine cyclodeaminase (VioK/ZWA5B ...
Isopropylmalate synthase Cthe_1391, 2519; 5. 3-Isopropylmalate dehydratase Cthe_2210, 2211; 6. 3-Isopropylmalate dehydrogenase ... 1. Acetolactate synthase Cthe_2516, 2517, 2714; 2. Ketol-acid reductoisomerase Cthe_2518; 3. Dihydroxy-acid dehydratase Cthe_ ... PEP synthase Cthe_1253; 19. Lactate dehydrogenase Cthe_1053; 20. Pyruvate formate lyase Cthe_0506, 0505; 21. Pyruvate ... Fatty acid synthase enzymes (Fab H,G,J,I reported in Additional File 10: Table S7 ...
  • This enzyme is closely related to 2-isopropylmalate synthase (LeuA) and citramalate synthase (CimA), both of which are present in the euryarchaeota. (ebi.ac.uk)
  • A recombinant C. glutamicum strain was constructed by expressing a feedback-resistant leuA-encoded 2-isopropylmalate synthase (IPMS) that carries three amino acid exchanges (R529H, G532D and L535V) from the mutant strain C. glutamicum ML1-9 which was obtained by screening for. (academicjournals.org)
  • MAM is believed to have evolved from isopropylmalate synthase (IPMS), an enzyme involved in Leu biosynthesis, based on phylogenetic analyses and an overlap of catalytic abilities. (nih.gov)
  • Mithen, Richard 2005-11-29 00:00:00 Isopropylmalate synthase (IPMS) is a key enzyme in the biosynthesis of the essential amino acid leucine, and thus primary metabolism. (deepdyve.com)
  • Microarray screening led to the invention of a gene with excessive amino acid similarity to 2-isopropylmalate synthase (IPMS). (rsrf.org)
  • The enzyme α-isopropylmalate synthase (IPMS) catalyses the reaction between acetyl coenzyme A (AcCoA) and α-ketoisovalerate (KIV) to produce free coenzyme A and α isopropylmalate (IPM). (canterbury.ac.nz)
  • The known KARA subfamilies are IPMS, citramalate synthases (CMSs), homocitrate synthases (HCSs), methylthioalkylmalate synthases (MAMSs) and re-citrate synthases (RCSs), respectively involved in the biosynthesis of isoleucine, lysine, glucosinolates and TCA cycle intermediates. (canterbury.ac.nz)
  • Chapter 2 details the expression and characterisation of the Eco like IPMS from N. meningitidis (NmeIPMS). (canterbury.ac.nz)
  • Jan-Willem de Kraker and Jonathan Gershenzon reported that the enzyme methylthioalkylmalate synthase (MAM), which catalyzes glucosinolate formation, strongly resembles another enzyme with a completely different function: The enzyme IPMS (isopropylmalate synthase) is involved in the synthesis of the amino acid leucine. (uni-protokolle.de)
  • Thus the function of IPMS is to bind 2-oxoisovalerate and acetyl-CoA and thereby produce leucine precursors. (uni-protokolle.de)
  • We present an in vivo regulatory model of BCAA homeostasis derived from analysis of feedback-resistant Arabidopsis thaliana mutants for the three allosteric committed enzymes in the biosynthetic network: threonine deaminase (also named l - O -methylthreonine resistant 1 [OMR1]), acetohydroxyacid synthase small subunit 2 (AHASS2), and isopropylmalate synthase 1 (IPMS1). (plantcell.org)
  • 2007). The isomerization step is catalysed by isopropylmalate isomerases (IPMIs), which exist as heterodimeric enzymes and each consists of a large subunit encoded by a single gene, named LeuC, and a small subunit encoded by one of three genes, named LeuD1, LeuD2, and LeuD3. (nih.gov)
  • In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction acetyl-CoA + 3-methyl-2-oxobutanoate + H2O ⇌ {\displaystyle \rightleftharpoons } (2S)-2-isopropylmalate + CoA The three substrates of this enzyme are acetyl-CoA, 3-methyl-2-oxobutanoate, and H2O, and its products are (2S)-2-isopropylmalate and CoA. (wikipedia.org)
  • The systematic name of this enzyme class is acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). (wikipedia.org)
  • In Arabidopsis, the functionally similar enzyme, methythiolalkylmalate synthase (MAM), is an important enzyme in the elongation of methionine prior to glucosinolate (GSL) biosynthesis, as part of secondary metabolism. (deepdyve.com)
  • Acetohydroxyacid synthase is the first enzyme for the parallel pathway performing condensation reaction in both steps - condensation of pyruvate to acetoacetate in the valine pathway and condensation of pyruvate and 2-ketobutyrate to form acetohydroxybtylrate in the isoleucine pathway. (wikipedia.org)
  • The enzyme transfers CO 2 from glutaconyl-CoA to a biotin carrier protein (the γ-subunit) that is subsequently decarboxylated by the carboxybiotin decarboxylation site within the Na + pumping beta subunit (Gcdβ). (tcdb.org)
  • Tryptophan synthase or tryptophan synthetase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan . (wikipedia.org)
  • As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target . (wikipedia.org)
  • Cystathionine β-synthase (CBS) is a multidomainal enzyme with three modules and a heme domain. (bionity.com)
  • The human enzyme cystathionine β-synthase is a tetramer and comprises 551 amino acids with a subunit molecular weight of 63 kDa. (bionity.com)
  • The yeast enzyme is also activated by the deletion of the C-terminal to produce the dimeric enzyme [2] . (bionity.com)
  • Cystathionine-β-synthase , also known as CBS , is an enzyme ( EC 4.2.1.22 ) that in humans is encoded by the CBS gene . (wikidoc.org)
  • Phylogenetic analyses of the glucose 6-phosphate transporter UhpC (Fig. S1), the catalytic subunit of the ferredoxin/flavodoxin dependent 2-oxoacid oxidoreductases (Fig. S2), the catalytic subunit (EchE) of [NiFe]-hydrogenases (Fig. S3), isopropylmalate/citramalate/homocitrate synthases (Fig. S4), transporter proteins for aromatic amino acids, proline, and serine (Fig. S5), and amino acid sequences of ThiE and ThiH (Fig. S6). (asm.org)
  • Five enzymes play a major role in the parallel synthesis pathways for isoleucine, valine, and leucine: threonine dehydrogenase, acetohydroxyacid synthase, ketoacid reductoisomerase, dihydroxyacid dehygrogenase and aminotransferase . (wikipedia.org)
  • Interestingly, a similar cycle of 2-oxo acid-based chain-elongation reactions is also utilized in leucine biosynthesis. (nih.gov)
  • 2014). Similarly, in the oxidative decarboxylation step, isopropylmalate decarboxylase 1 (IPMDH1) works in methionine chain elongation, while IPMDH2 and IPMDH3 are involved in leucine biosynthesis (He et al. (nih.gov)
  • 2016. Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: Insights on Leucine and Aliphatic Glucosinolate Biosynthesis. (wustl.edu)
  • [3] Threonine dehydrogenase catalyzes the deamination and dehydration of threonine to 2-ketobutyrate and ammonia. (wikipedia.org)
  • 8. The method of claim 1, wherein the recombinant host cell further has a deficiency in activity of one or more enzymes selected from the group consisting of pyruvate oxidase (poxB), pyruvate-formate lyase (pflB), phosphotransacetylase (pta), acetate kinase (ackA), aldehyde dehydrogenase (aldB), alcohol dehydrogenase (adhE), alcohol dehydrogenase (adhP), methylglyoxal synthase (mgsA), and lactate dehydrogenase (ldhA). (patentsencyclopedia.com)
  • 13. The method of claim 1, wherein the recombinant host cell further expresses at least one protein selected from the group consisting of citrate synthase with reduced sensitivity to NADH and pyruvate dehydrogenase with reduced sensitivity to NADH. (patentsencyclopedia.com)
  • Isocitrate dehydrogenase NAD-dependent (IPR004434) Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the multimeric forms of isocitrate dehydrogenase, share a nuc. (ebi.ac.uk)
  • A plant pathway that initiates with the formation of citramalate from pyruvate and acetyl-CoA by citramalate synthase (CMS) is proven to contribute to the synthesis of α-ketoacids and vital odor-active esters in apple (Malus × domestica) fruit. (rsrf.org)
  • Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. (nih.gov)
  • Leptospira interrogans citramalate synthase binds Zn2+ and malonate, contacts at 4A. (nih.gov)
  • Thus, this gene ( cimA ) encodes an ( R )-citramalate synthase (CimA). (asm.org)
  • We report here that this gene product is ( R )-citramalate synthase. (asm.org)
  • 17. The method of claim 15, wherein the citrate synthase with reduced sensitivity to NADH is a citrate synthase comprising an R163L amino acid mutation. (patentsencyclopedia.com)
  • In mitochondria (for eukaryotes), TCA cycle begins with acetyl-CoA and oxaloacetic acid (oxaloacetate) be catalyzed to form citric acid (citrate) by citrate synthase 3. (smpdb.ca)
  • Pathways for amino acid biosynthesis that are present in En. (asm.org)
  • At the condensation step, two methylthioalkylmalate synthases (MAM1 and MAM3) share ~60% amino acid identity with the two isopropylmalate synthases (IPMS1 and IPMS2) (Textor et al. (nih.gov)
  • Mutations in the Arabidopsis ROL17/isopropylmalate synthase 1 locus alter amino acid content, modify the TOR network, and suppress the root hair cell development mutant lrx1. (nih.gov)
  • As such, the inhibition of tryptophan synthase along with other PLP-enzymes in amino acid metabolism has the potential to help solve medical problems. (wikipedia.org)
  • The approach that was used to identify this gene was the outcome of other work aimed at identifying the reactions catalyzed by archaeal enzymes with sequences homologous to homocitrate synthase (NifV) ( 24 ). (asm.org)
  • B) Organization of the gene sets encoding the [FeFe]-hydrogenases in En. (asm.org)
  • In category 2, the levels of individual gene products are altered, and the impact on the flux is measured. (biomedcentral.com)
  • Methylthioalkylmalate synthase (MAM) catalyzes the committed step in the side chain elongation of Met, yielding important precursors for glucosinolate biosynthesis in Arabidopsis thaliana and other Brassicaceae species. (nih.gov)
  • It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. (sickkids.ca)
  • Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction. (wikidoc.org)
  • IPMS1 and IPMS2, isopropylmalate synthase 1 and 2. (plantcell.org)
  • The α-subunits of the oxaloacetate and methylmalonyl-CoA decarboxylases are homologous to many biotin-containing enzymes including (1) pyruvate carboxylases, (2) homocitrate synthases, (3) biotin carboxyl carrier proteins, (4) isopropylmalate synthases and (5) acyl-CoA carboxylase. (tcdb.org)
  • Archives of Biochemistry and Biophysics , 451 (2), 141-148. (elsevier.com)
  • de Carvalho, LPS & Blanchard, JS 2006, ' Kinetic analysis of the effects of monovalent cations and divalent metals on the activity of Mycobacterium tuberculosis α-isopropylmalate synthase ', Archives of Biochemistry and Biophysics , vol. 451, no. 2, pp. 141-148. (elsevier.com)
  • Other names in common use include 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase, (CoA-acetylating), alpha-isopropylmalate synthetase, alpha-isopropylmalate synthase, alpha-isopropylmalic synthetase, isopropylmalate synthase, and isopropylmalate synthetase. (wikipedia.org)
  • The alpha-isopropylmalate synthetase of Neurospora. (wikipedia.org)
  • Alpha-isopropylmalate synthetase. (expasy.org)
  • Belongs to the alpha-IPM synthase/homocitrate synthase family. (string-db.org)
  • Mycobacterium tuberculosis α-isopropylmalate synthase requires a divalent metal ion, of which Mg2+ and Mn2+ give highest activity, and a monovalent cation, with K+ as the best activator. (wikipedia.org)
  • Mycobacterium tuberculosis α-isopropylmalate synthase (MtIPMS) is a member of the family of enzymes that catalyze a Claisen-type condensation. (elsevier.com)
  • To elucidate the molecular mechanism of how VeA regulates asexual and sexual spore development in A. cristatus , 2D electrophoresis (2-DE) combined with MALDI-tandem ToF MS analysis were applied to identify 173 differentially expressed proteins (DEPs) by comparing the agamotype (24 h) and teleomorph (72 h) with wild-type (WT) A. cristatus strains. (bioscirep.org)
  • The 2-DE and mass spectrometry analyses of the proteome revealed that 46 proteins of H. hepaticus were differentially expressed in human bile, 18 up-regulated and 28 down-regulated. (biomedcentral.com)
  • At the C-terminus, the regulatory domain of CBS contains a tandem repeat of two CBS domains of β-α-β-β-α, a secondary structure motif found in other proteins [2] . (bionity.com)
  • The C-terminal domain of cystathionine β-synthase regulates its activity via both intrasteric and allosteric effects and is important for maintaining the tetrameric state of the protein [2] . (bionity.com)
  • orange, genes present only in En. (asm.org)
  • The mn 1 mutation in maize is associated with a loss of 70% seed weight at maturity due to a loss-of-function mutation at the Mn 1 locus that codes for the endosperm-specific cell wall invertase 2 (INCW2). (frontiersin.org)
  • In addition to the complex requirements for a divalent metal and further activation by K+, M. tuberculosis α-isopropylmalate synthase follows a random kinetic mechanism for catalysis. (wikipedia.org)
  • T-box anti-termination is an elegant and sensitive mechanism by which many bacteria maintain constant levels of tRNA charged with amino acids [ 2 , 8 ]. (biomedcentral.com)
  • The energy metabolism has been subject to many investigations ( 5 , 6 , 13 ), but its understanding, especially the mechanism of H 2 formation via ferredoxin from NADH, has remained a challenge until today because this is thermodynamically an uphill reaction requiring energy to proceed. (pnas.org)
  • The reaction afforded a γ-butyrolactone that could serve as a potential intermediate en route to the synthesis of the biologically interesting compounds thromboxanes A₂ and B₂. (nzresearch.org.nz)
  • [8] The active sites of tryptophan synthase are allosterically coupled. (wikipedia.org)
  • Tryptophan synthase typically exists as an α-ββ-α complex. (wikipedia.org)
  • Then, 3-isopropylmalate dehydratase with cofactor 4Fe-4S can catalyze citrate to form cis-aconitic acid as the intermediate compound and catalyze cis-aconitic acid to form isocitric acid. (smpdb.ca)
  • It displays a modular organization of three modules with the N-terminal heme domain followed by a core that contains the PLP cofactor [2] .The cofactor is deep in the heme domain and is linked by a Schiff base [3] . (bionity.com)
  • Homocitrate synthase is located in the nucleus in the yeast Saccharomyces cerevisiae. (ebi.ac.uk)
  • Inactivation of homocitrate synthase causes lysine auxotrophy in copper/zinc-containing superoxide dismutase-deficient yeast Schizosaccharomyces pombe. (ebi.ac.uk)
  • Feedback inhibition of acetohydroxy acid synthase isoenzyme III by l -valine was removed by site-directed mutagenesis, and the native promoter containing the transcriptional attenuator leader regions of the ilvGMEDA and ilvBN operon was replaced with the tac promoter. (pnas.org)
  • A systematic name for this compound is 2-aminohexanoic acid. (wikipedia.org)
  • and the ilvBNC operon, encoding acetohydroxy acid synthase ( ilvBN ), and acetohydroxy acid isomeroreductase ( ilvC ) were overexpressed ( 8 ). (pnas.org)
  • In this pathway, glutamate is converted via l - threo -β-methylaspartate [(2 S ,3 R )-3-methylaspartate] to mesaconate [( E )-2-methyl-2-butenedionic acid], which is then hydrated by citramalate hydrolyase ( 15 , 16 ) to l -(+)-citramalate ( S -citramalate). (asm.org)
  • Hydration of citraconic acid [( Z )-2-methyl-2-butenedionic acid] to d -(−)-citramalate ( R -citramalate) has also been described ( 13 , 18 ). (asm.org)
  • The chemical synthesis of [S,S]-EDDS starting from L-aspartic acid and 1,2-dibromomethane in the presence of trivalent cobalt is well-known (Neal and Rose, Inorganic Chemistry (1968), 7(11):2405-12). (justia.com)
  • [1] Non-proteinogenic BCAAs include 2-aminoisobutyric acid . (wikipedia.org)
  • 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase (IPR004433) MenD was thought to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. (ebi.ac.uk)
  • 2,4--dihydroxyhept--2--ene--1,7--dioic acid aldolase (EC 4.1.2. (sbri.org)
  • Methylcysteine synthase was assigned the EC number EC 4.2.1.23 in 1961. (wikidoc.org)
  • [2] Synthesis for BCAAs occurs in all locations of plants, within the plastids of the cell, as determined by presence of mRNAs which encode for enzymes in the metabolic pathway. (wikipedia.org)
  • Citramalate (2-methylmalate) is a biochemical intermediate known to be involved in several aspects of bacterial metabolism, including, among others, the anaerobic metabolism of glutamate via the methylaspartate pathway of Clostridium tetanomorphum ( 2 ). (asm.org)