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 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.
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.
Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
A genus of aerobic, chemolithotrophic, coccoid ARCHAEA whose organisms are thermoacidophilic. Its cells are highly irregular in shape, often lobed, but occasionally spherical. It has worldwide distribution with organisms isolated from hot acidic soils and water. Sulfur is used as an energy source.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
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.
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.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
A species of gram-positive bacteria that is a common soil and water saprophyte.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The rate dynamics in chemical or physical systems.
A genus of gram-negative, rod-shaped bacteria that derives energy from the oxidation of one or more reduced sulfur compounds. Many former species have been reclassified to other classes of PROTEOBACTERIA.
It is a form of protection provided by law. In the United States this protection is granted to authors of original works of authorship, including literary, dramatic, musical, artistic, and certain other intellectual works. This protection is available to both published and unpublished works. (from Circular of the United States Copyright Office, 6/30/2008)
A strictly autotrophic species of bacteria that oxidizes sulfur and thiosulfate to sulfuric acid. It was formerly called Thiobacillus thiooxidans.
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A species of gram-negative, aerobic bacteria isolated from soil and the stems, leafs, and roots of plants. Some biotypes are pathogenic and cause the formation of PLANT TUMORS in a wide variety of higher plants. The species is a major research tool in biotechnology.
Rats bearing mutant genes which are phenotypically expressed in the animals.
A condition due to a dietary deficiency of ascorbic acid (vitamin C), characterized by malaise, lethargy, and weakness. As the disease progresses, joints, muscles, and subcutaneous tissues may become the sites of hemorrhage. Ascorbic acid deficiency frequently develops into SCURVY in young children fed unsupplemented cow's milk exclusively during their first year. It develops also commonly in chronic alcoholism. (Cecil Textbook of Medicine, 19th ed, p1177)
PLANTS, or their progeny, whose GENOME has been altered by GENETIC ENGINEERING.
A 20 cM region of mouse chromosome 17 that is represented by a least two HAPLOTYPES. One of the haplotypes is referred to as the t-haplotype and contains an unusual array of mutations that affect embryonic development and male fertility. The t-haplotype is maintained in the gene pool by the presence of unusual features that prevent its recombination.
Change brought about to an organisms genetic composition by unidirectional transfer (TRANSFECTION; TRANSDUCTION, GENETIC; CONJUGATION, GENETIC, etc.) and incorporation of foreign DNA into prokaryotic or eukaryotic cells by recombination of part or all of that DNA into the cell's genome.
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.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Compositions written by hand, as one written before the invention or adoption of printing. A manuscript may also refer to a handwritten copy of an ancient author. A manuscript may be handwritten or typewritten as distinguished from a printed copy, especially the copy of a writer's work from which printed copies are made. (Webster, 3d ed)
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane.
A genus of yeast-like mitosporic Saccharomycetales fungi characterized by producing yeast cells, mycelia, pseudomycelia, and blastophores. It is commonly part of the normal flora of the skin, mouth, intestinal tract, and vagina, but can cause a variety of infections, including CANDIDIASIS; ONYCHOMYCOSIS; vulvovaginal candidiasis (CANDIDIASIS, VULVOVAGINAL), and thrush (see CANDIDIASIS, ORAL). (From Dorland, 28th ed)
A unicellular budding fungus which is the principal pathogenic species causing CANDIDIASIS (moniliasis).
Infection with a fungus of the genus CANDIDA. It is usually a superficial infection of the moist areas of the body and is generally caused by CANDIDA ALBICANS. (Dorland, 27th ed)
Procedures for identifying types and strains of fungi.
Infection of the mucous membranes of the mouth by a fungus of the genus CANDIDA. (Dorland, 27th ed)
Substances that destroy fungi by suppressing their ability to grow or reproduce. They differ from FUNGICIDES, INDUSTRIAL because they defend against fungi present in human or animal tissues.
Triazole antifungal agent that is used to treat oropharyngeal CANDIDIASIS and cryptococcal MENINGITIS in AIDS.
A species of imperfect fungi which grows on peanuts and other plants and produces the carcinogenic substance aflatoxin. It is also used in the production of the antibiotic flavicin.
An order of fungi in the phylum ASCOMYCOTA characterized by the presence of well defined peridia and cleistothecial asci. Notable anamorphs (mitosporic forms) of Eurotiales include PENICILLIUM and ASPERGILLUS.
A genus of mitosporic fungi containing about 100 species and eleven different teleomorphs in the family Trichocomaceae.
A phylum of fungi which have cross-walls or septa in the mycelium. The perfect state is characterized by the formation of a saclike cell (ascus) containing ascospores. Most pathogenic fungi with a known perfect state belong to this phylum.
Furano-furano-benzopyrans that are produced by ASPERGILLUS from STERIGMATOCYSTIN. They are structurally related to COUMARINS and easily oxidized to an epoxide form to become ALKYLATING AGENTS. Members of the group include AFLATOXIN B1; aflatoxin B2, aflatoxin G1, aflatoxin G2; AFLATOXIN M1; and aflatoxin M2.

Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis. (1/111)

A thermostabilized mutant of Bacillus subtilis 3-isopropylmalate dehydrogenase (IPMDH) obtained in a previous study contained a set of triple amino acid substitutions. To further improve the stability of the mutant, we used a random mutagenesis technique and identified two additional thermostabilizing substitutions, Thr22-->Lys and Met256-->Val, that separately endowed the protein with further stability. We introduced the two mutations into a single enzyme molecule, thus constructing a mutant with overall quintuple mutations. Other studies have suggested that an improved hydrophobic subunit interaction and a rigid type II beta-turn play important roles in enhancing the protein stability. Based on those observations, we successively introduced amino acid substitutions into the mutant with the quintuple mutations by site-directed mutagenesis: Glu253 at the subunit interface was replaced by Leu to increase the hydrophobic interaction between the subunits; Glu112, Ser113 and Ser115 that were involved in the formation of the turn were replaced by Pro, Gly and Glu, respectively, to make the turn more rigid. The thermal stability of the mutants was determined based on remaining activity after heat treatment and first-order rate constant of thermal unfolding, which showed gradual increases in thermal stability as more mutations were included.  (+info)

Functional analysis of upstream regulating regions from the Yarrowia lipolytica XPR2 promoter. (2/111)

The XPR2 gene from Yarrowia lipolytica encodes an inducible alkaline extracellular protease. Its complex regulation involves pH, carbon, nitrogen and peptones. Two previously identified upstream activating sequence (UAS) regions were analysed in a reporter system, outside the XPR2 context. Fragments from the UAS regions were inserted upstream of a minimal LEU2 promoter directing the expression of a reporter gene. The activity of the hybrid promoters was assessed following integration into the Y. lipolytica genome. This study confirmed the presence of two UASs composed of several interacting elements. Within the distal UAS (UAS1), a TUF/RAP1 binding site exhibited a UAS activity, which was enhanced by the presence of two adjacent repeats, overlapping sites similar to the CAR1 upstream repressing sequence from Saccharomyces cerevisiae. Within the proximal UAS (UAS2), the UAS activity required the interaction of both an ABF1-like binding site and a decameric repeat, containing Aspergillus nidulans PacC site consensus sequences. This decameric repeat was able to mediate repression due to carbon and/or nitrogen sources as well as pH-dependent activation. A study in the context of trans-regulatory mutations in the Y. lipolytica RIM101 gene showed that the PacC-like sites, potential binding sites for YlRim101p, were implicated in the derepression of UAS2-driven expression at neutral-alkaline pH. The in vivo response of the PacC-like decamers to external pH was dependent on the status of the pH-regulated activator YlRim101p, which is homologous to the A. nidulans PacC regulator. The carbon/nitrogen regulation imposed on the decamers was shown to be independent of YlRim101p and to override its effects.  (+info)

Escherichia coli Lrp (leucine-responsive regulatory protein) does not directly regulate expression of the leu operon promoter. (3/111)

Studies by R. Lin et al. (J. Bacteriol. 174:1948-1955, 1992) suggested that the Escherichia coli leu operon might be a member of the Lrp regulon. Their results were obtained with a leucine auxotroph; in leucine prototrophs grown in a medium lacking leucine, there was little difference in leu operon expression between lrp(+) and lrp strains. Furthermore, when leuP-lacZ transcriptional fusions that lacked the leu attenuator were used, expression from the leu promoter varied less than twofold between lrp(+) and lrp strains, irrespective of whether or not excess leucine was added to the medium. The simplest explanation of the observations of Lin et al. is that the known elevated leucine transport capacity of lrp strains (S. A. Haney et al., J. Bacteriol. 174:108-115, 1992) leads to very high intracellular levels of leucine for strains grown with leucine, resulting in the superattenuation of leu operon expression.  (+info)

Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase. (4/111)

The comparison of the three-dimensional structures of thermophilic (Thermus thermophilus) and mesophilic (Escherichia coli) 3-isopropylmalate dehydrogenases (IPMDH, EC 1.1.1.85) suggested that the existence of extra ion pairs in the thermophilic enzyme found in the intersubunit region may be an important factor for thermostability. As a test of our assumption, glutamine 200 in the E. coli enzyme was turned into glutamate (Q200E mutant) to mimic the thermophilic enzyme at this site by creating an intersubunit ion pair which can join existing ion clusters. At the same site in the thermophilic enzyme we changed glutamate 190 into glutamine (E190Q), hereby removing the corresponding ion pair. These single amino acid replacements resulted in increased thermostability of the mesophilic and decreased thermostability of the thermophilic enzyme, as measured by spectropolarimetry and differential scanning microcalorimetry.  (+info)

Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships. (5/111)

Thermal stability of the Thermus thermophilus isopropylmalate dehydrogenase enzyme was substantially lost upon the deletion of three residues from the C-terminus. However, the stability was partly recovered by the addition of two, four and seven amino acid residues (called HD177, HD708 and HD711, respectively) to the C-terminal region of the truncated enzyme. Three structures of these mutant enzymes were determined by an X-ray diffraction method. All protein crystals belong to space group P2(1) and their structures were solved by a standard molecular replacement method where the original dimer structure of the A172L mutant was used as a search model. Thermal stability of these mutant enzymes is discussed based on the 3D structure with special attention to the width of the active-site groove and the minor groove, distortion of beta-sheet pillar structure and size of cavity in the domain-domain interface around the C-terminus. Our previous studies revealed that the thermal stability of isopropylmalate dehydrogenase increases when the active-site cleft is closed (the closed form). In the present study it is shown that the active-site cleft can be regulated by open-close movement of the minor groove located at the opposite side to the active-site groove on the same subunit, through a paperclip-like motion.  (+info)

Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea. (6/111)

Two putative Methanococcus jannaschii isocitrate dehydrogenase genes, MJ1596 and MJ0720, were cloned and overexpressed in Escherichia coli, and their gene products were tested for the ability to catalyze the NAD- and NADP-dependent oxidative decarboxylation of DL-threo-3-isopropylmalic acid, threo-isocitrate, erythro-isocitrate, and homologs of threo-isocitrate. Neither enzyme was found to use any of the isomers of isocitrate as a substrate. The protein product of the MJ1596 gene, designated AksF, catalyzed the NAD-dependent decarboxylation of intermediates in the biosynthesis of 7-mercaptoheptanoic acid, a moiety of methanoarchaeal coenzyme B (7-mercaptoheptanylthreonine phosphate). These intermediates included (-)-threo-isohomocitrate [(-)-threo-1-hydroxy-1,2, 4-butanetricarboxylic acid], (-)-threo-iso(homo)(2)citrate [(-)-threo-1-hydroxy-1,2,5-pentanetricarboxylic acid], and (-)-threo-iso(homo)(3)citrate [(-)-threo-1-hydroxy-1,2, 6-hexanetricarboxylic acid]. The protein product of MJ0720 was found to be alpha-isopropylmalate dehydrogenase (LeuB) and was found to catalyze the NAD-dependent decarboxylation of one isomer of DL-threo-isopropylmalate to 2-ketoisocaproate; thus, it is involved in the biosynthesis of leucine. The AksF enzyme proved to be thermostable, losing only 10% of its enzymatic activity after heating at 100 degrees C for 10 min, whereas the LeuB enzyme lost 50% of its enzymatic activity after heating at 80 degrees C for 10 min.  (+info)

The initial step of the thermal unfolding of 3-isopropylmalate dehydrogenase detected by the temperature-jump Laue method. (7/111)

A temperature-jump (T-jump) time-resolved X-ray crystallographic technique using the Laue method was developed to detect small, localized structural changes of proteins in crystals exposed to a temperature increase induced by laser irradiation. In a chimeric protein between thermophilic and mesophilic 3-isopropylmalate dehydrogenases (2T2M6T), the initial structural change upon T-jump to a denaturing temperature (approximately 90 degrees C) was found to be localized at a region which includes a beta-turn and a loop located between the two domains of the enzyme. A mutant, 2T2M6T-E110P/S111G/S113E, having amino acid replacements in this beta-turn region with the corresponding residues of the thermophilic enzyme, showed greater stability than the original chimera (increase of T:(m) by approximately 10 degrees C) and no T-jump-induced structural change in this region was detected by our method. These results indicate that thermal unfolding of the original chimeric enzyme, 2T2M6T, is triggered in this beta-turn region.  (+info)

Functional prediction: identification of protein orthologs and paralogs. (8/111)

Orthologs typically retain the same function in the course of evolution. Using beta-decarboxylating dehydrogenase family as a model, we demonstrate that orthologs can be confidently identified. The strategy is based on our recent findings that substitutions of only a few amino acid residues in these enzymes are sufficient to exchange substrate and coenzyme specificities. Hence, the few major specificity determinants can serve as reliable markers for determining orthologous or paralogous relationships. The power of this approach has been demonstrated by correcting similarity-based functional misassignment and discovering new genes and related pathways, and should be broadly applicable to other enzyme families.  (+info)

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 ...
1DR8: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
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); ...
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.
1DPZ: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
SWISS-MODEL Repository entry for A1T6Z4 (LEU3_MYCVP), 3-isopropylmalate dehydrogenase. Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / NRRL B-24157 /PYR-1) (Mycobacterium vanbaalenii)
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 ...
Chemical Entities of Biological Interest (ChEBI) is a freely available dictionary of molecular entities focused on small chemical compounds.
SWISS-MODEL Repository entry for A1SLW5 (LEUC_NOCSJ), 3-isopropylmalate dehydratase large subunit. Nocardioides sp (strain ATCC BAA-499 / JS614)
Bacteroides species, saccharolytic Gram-negative obligate anaerobes, are frequently isolated from human infections such as peritonitis, abscesses and bacteremia. Among the species in the genus Bacteroides, thespecies called B. fragilis group areparticularly involved inhuman infections andaremedically important because they account for a major part of anaerobic isolates from clinical specimens. The purpose of this study was to develop PCR primers that specifically and simultaneously amplify theβ-isopropylmalate dehydrogenase gene leuB in B. fragilis group species. We determined partial nucleotide sequences of leuB genes and compared them in seventeen strains of nine B. fragilis group species, and the regions that are conserved among Bacteroides strains but different from other species were used as a B. fragilis group-specific PCR primer set, BacLBF-BacLBR. Specificity tests of the primer set using 52 phenotypically characterized strains and 75 isolates from rat feces showed only one case each ...
Thermoacidophilic archaeon dehydrogenase. Computer model showing the structure of 3-isopropylmalate dehydrogenase from Sulfolobus acidocaldarius. - Stock Image C035/6196
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 ...
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 ...
The long-standing problem of achieving high activity of a thermophilic enzyme at low temperatures and short reaction times with little tradeoff in thermostability has been solved by directed evolution, an alcohol dehydrogenase found in hot springs serving as the catalyst in enantioselective ketone reductions
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_2013 (SAUSA300_RS11070); symbol: leuD; product: isopropylmalate isomerase small subunit
Jez JM, Lee SG, Sherp AM (2016) The next green movement: plant biology for the environment and sustainability. Science 353, 1241-4. Kilgore M, Holland CK, Jez JM, Kutchan TM (2016) Identification of a noroxomaritidine reductase with Amaryllidaceae alkaloid biosynthesis-related activities. J Biol Chem 291, 16740-52. Lee SG, Nwumeh R, Jez JM (2016) Structure and mechanism of isopropylmalate dehydrogenase from Arabidopsis thaliana: insights on leucine and aliphatic glucosinolate biosynthesis. J Biol Chem 291, 13421-30. Herrmann J, Nathin D, Lee SG, Sun T, Jez JM (2015) Recapitulating the structural evolution of redox regulation in adenosine-5-phosphosulfate kinase from cyanobacteria to plants. J Biol Chem 290, 24705-14. Korasick DA, Jez JM, Strader LC (2015) Refining the nuclear auxin response pathway through structural biology. Curr Opin Plant Biol 27, 22-8. Cahoon RE, Lutke WK, Cameron JC, Chen S, Lee SG, Rivard RS, Rea PA, Jez JM (2015) Adaptive engineering of phytochelatin-based heavy metal ...
In vitro reconstitution of an artificial metabolic pathway has emerged as an alternative approach to conventional in vivo fermentation-based bioproduction. Particularly, employment of thermophilic and hyperthermophilic enzymes enables us a simple preparation of highly stable and selective biocatalytic modules and the construction of in vitro metabolic pathways with an excellent operational stability. In this study, we designed and constructed an artificial in vitro metabolic pathway consisting of nine (hyper)thermophilic enzymes and applied it to the conversion of glycerol to lactate. We also assessed the compatibility of the in vitro bioconversion system with methanol, which is a major impurity in crude glycerol released from biodiesel production processes. The in vitro artificial pathway was designed to balance the intrapathway consumption and regeneration of energy and redox cofactors. All enzymes involved in the in vitro pathway exhibited an acceptable level of stability at high temperature (60°C),
F-, araC14, leuB6(Am), secA206(aziR), fhuA23, lacY1, tsx-67, purE42, glnX44(AS), galK2(Oc), λ-, trpE38, sup-78(Mal+)?, rfbC1?, mgl-51?, rpsL109(strR), malA38?, glpR201, xylA5, mtl-1, thiE1 ...
1. JOSE CARLOS QUINTELA, ERNST P.,GUNTER A.,VICENTE A.,MIGUEL A. DE P. Structure of Peptidoglycan from Thermus thermophilus HB8. JOURNAL OF BACTERIOLOGY, 1995, Vol. 177. p. 4947-4962. http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=177270&blobtype=pdf 2. Henne A, Bruggemann H, Raasch C, Wiezer A, Hartsch T, Liesegang H, Johann A, Lienard T, Gohl O, Martinez-Arias R, Jacobi C, Starkuviene V, Schlenczeck S, Dencker S, Huber R, Klenk HP, Kramer W, Merkl R, Gottschalk G, Fritz HJ. The genome sequence of the extreme thermophile Thermus thermophilus. Nat Biotechnol. 2004 May, Vol 22. p.547-53. http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&list_uids=15064768&dopt=AbstractPlus&holding=f1000%2Cf1000m%2Cisrctn 3. Pantazaki AA, Tambaka MG, Langlois V, Guerin P, Kyriakidis DA. Polyhydroxyalkanoate (PHA) biosynthesis in Thermus thermophilus: purification and biochemical properties of PHA synthase. Mol Cell Biochem. 2003 Dec;254(1-2):173-83. ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Sodium atom in PDB 2dpw: Hpothetical Transferase Structure From Thermus Thermophilus
The structural characterization of glycolipids from Thermus thermophilus HB8 was performed in this study. Two neutral and one acidic glycolipids were extracted and purified by the modified TLC-blotting method, after which their chemical structures were determined by chemical composition analysis, mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy. The structure of one of the neutral glycolipids, NGL-A, was Galp(α1-6)GlcpNacyl(β1-2)Glcp(α1-)acyl2Gro, and the other, NGL-C, was Galf(β1-2)Galp(α1-6)GlcpNacyl(β1-2)Glcp(α1-)acyl2Gro. The structure of NGL-C was identical to that reported previously [Oshima, M. and Ariga, T. (1976) FEBS Lett. 64, 440]. Both neutral glycolipids shared a common structural unit found in the Thermus species. The acyl groups found in NGL-A and NGL-C, iso-type pentadecanoxy and heptadecanoxy fatty acid, were also the same as those found in this species. In contrast, the acidic glycolipid, AGL-B, possessed the structure of N-(((GlcpNAc(α1-)acyl2Gro)P-2
Thermus thermophilus ATCC ® BAA-163D-5™ Designation: Genomic DNA from Thermus thermophilus Strain DSM 7039 TypeStrain=False Application:
Looking for online definition of thermophile in the Medical Dictionary? thermophile explanation free. What is thermophile? Meaning of thermophile medical term. What does thermophile mean?
Thermophily in the Geobacteraceae: Geothermobacter ehrlichii gen. nov., sp. nov., a novel thermophilic member of the Geobacteraceae from the Bag City hydrothermal ...
F-, araC14, leuB6(Am), secA206(aziR), fhuA23, lacY1, proC83, tsx-67, purE42, glnX44(AS), galK2(Oc), λ-, trpE38, xthA15, his-208, rfbC1, mgl-51, argG77, rpsL109(strR), glpR201, xylA5, mtl-1, ilvA681, katG17::Tn10, thiE1, metA160 ...
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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 …
Thermus thermophilus ATCC ® BAA-163™ Designation: DSM 7039 TypeStrain=False Application: Produces aqualysin I Biotechnology
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 ». ...
TamA interacts with LeuB, the homologue of Saccharomyces cerevisiae Leu3p, to regulate gdhA expression in Aspergillus nidulans Journal Articles Refereed ...
Affiliation:九州大学,農学研究院,教授, Research Field:応用微生物学・応用生物化学,Applied microbiology,Environmental agriculture(including landscape science),資源開発工学,Applied biochemistry, Keywords:Streptomyces,Thermus,Thermus thermophilus,Thermus thermphilus,放線菌,微生物,プラスミド,DNA複製,ゲノム,バイオミネラリゼーション, # of Research Projects:15, # of Research Products:155, Ongoing Project:ネパール野生キノコのライブラリーと健康機能を含むデータベースの構築
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Although some progress has been made in the development of genetic technology for Bacillus stearothermophilus, strains of the genus Thermus, and Methanobacterium thermoautotrophicum, the lack of efficient and reliable genetic exchange systems, a repertoire of mutants, or plasmids that express useful genetic markers has hampered the exploitation of these organisms for basic and applied research. Recent progress in the development of genetic techniques for B. stearothermophilus NUB36 makes it possible to elucidate the molecular and genetic mechanisms of thermophily in this organism. The genetic characterization of the B. stearothermophilus NUB36 genome is the first step in attaining this goal. The map was constructed using the linkages reported by Vallier and Welker. The genetic map of B. stearothermophilus NUB36 may be similar to the B. subtilis 168 map; however, the identity of the genes in B. stearothermophilus with the putative analogous genes of B. subtilis must be rigorously established by
... (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 ... BCAAs are broken down effectively by dehydrogenase and decarboxylase enzymes expressed by immune cells, and are required for ... Degradation of branched-chain amino acids involves the branched-chain alpha-keto acid dehydrogenase complex (BCKDH). A ... Five enzymes play a major role in the parallel synthesis pathways for isoleucine, valine, and leucine: threonine dehydrogenase ...
... malate dehydrogenase MeSH D08.811.682.047.748 - malate dehydrogenase (nadp+) MeSH D08.811.682.047.892 - xanthine dehydrogenase ... 2-isopropylmalate synthase MeSH D08.811.913.050.618 - malate synthase MeSH D08.811.913.050.622 - 3-oxoacyl-(acyl-carrier- ... acetoin dehydrogenase MeSH D08.811.682.047.070 - alcohol dehydrogenase MeSH D08.811.682.047.150 - carbohydrate dehydrogenases ... acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 - acyl-coa dehydrogenase, long-chain MeSH D08.811.682.660.150.200 - acyl- ...
Parsons SJ, Burns RO (February 1969). "Purification and Properties of β-Isopropylmalate Dehydrogenase". J. Biol. Chem. 244 (3 ... 3-Isopropylmalate dehydrogenase (EC 1.1.1.85) is an enzyme that catalyzes the chemical reactions (2R,3S)-3-isopropylmalate + ... Calvo JM, Stevens CM, Kalyanpur MG, Umbarger HE (December 1964). "The Absolute Configuration of α-carboxyisocaproic Acid (3- ... 2-isopropyl-3-oxosuccinate + H+ + NADH (2S)-2-isopropyl-3-oxosuccinate + H+ ⇌ {\displaystyle \rightleftharpoons } 4-methyl-2- ...
The third step is the NAD+-dependent oxidation of β-isopropylmalate catalyzed by a dehydrogenase. The final step is the ... α-Isopropylmalate synthase catalyzes this condensation with acetyl CoA to produce α-isopropylmalate. An isomerase converts α- ... PheA uses a simple dehydrogenase to convert prephenate to phenylpyruvate, while TyrA uses a NAD-dependent dehydrogenase to make ... Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O- ...
Acetolactate synthase Acetohydroxy acid isomeroreductase Dihydroxyacid dehydratase α-Isopropylmalate synthase α-Isopropylmalate ... Isovaleryl-CoA is subsequently metabolized by isovaleryl-CoA dehydrogenase and converted to MC-CoA, which is used in the ... whereas the dehydrogenase enzyme is found exclusively in the mitochondrion (Sabourin and Bieber 1981, 1983). Importantly, this ... α-KIC is mostly metabolized by the mitochondrial enzyme branched-chain α-ketoacid dehydrogenase, which converts it to ...
... isocitrate dehydrogenase (NADP+)) kinase EC 2.7.11.6: (tyrosine 3-monooxygenase) kinase EC 2.7.11.7: myosin-heavy-chain kinase ... 2-isopropylmalate synthase EC 2.3.3.14: homocitrate synthase EC 2.3.3.15: sulfoacetaldehyde acetyltransferase EC 2.4.1.1: ... acetoin dehydrogenase EC 2.3.1.191: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase EC 2.3.1.192: glycine N- ... pyruvate dehydrogenase (acetyl-transferring)) kinase EC 2.7.11.3: dephospho-(reductase kinase) kinase EC 2.7.11.4: (3-methyl-2- ...
Oxoglutarate dehydrogenase *OGDH. *DLST. *DLD. *Branched-chain alpha-keto acid dehydrogenase complex *BCKDHA ... 3] Protista,[4] Fungi,[5] and Plantae.[6] However, it is absent from Animalia.[7] It is typically found as an α2β2 tetramer. ... The α subunits catalyze the reversible formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol ...
... , ECHB, MSTP029, MTPB, TP-BETA, hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional ... "Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ... 3 (2): 121-6. doi:10.1002/ajh.2830030202. PMID 272120.. *^ Spiekerkoetter, U; Sun, B; Khuchua, Z; Bennett, MJ; Strauss, AW ( ... Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, ...
Parsons SJ, Burns RO (February 1969). "Purification and Properties of β-Isopropylmalate Dehydrogenase". J. Biol. Chem. 244 (3 ... 3-Isopropylmalate dehydrogenase (EC 1.1.1.85) is an enzyme that catalyzes the chemical reactions (2R,3S)-3-isopropylmalate + ... Calvo JM, Stevens CM, Kalyanpur MG, Umbarger HE (December 1964). "The Absolute Configuration of α-carboxyisocaproic Acid (3- ... 2-isopropyl-3-oxosuccinate + H+ + NADH (2S)-2-isopropyl-3-oxosuccinate + H+ ⇌ {\displaystyle \rightleftharpoons } 4-methyl-2- ...
2R,3S-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH UniProt ... Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. ...
Our previous studies revealed that the thermal stability of isopropylmalate dehydrogenase increases when the active-site cleft ... Thermal stability of the Thermus thermophilus isopropylmalate dehydrogenase enzyme was substantially lost upon the deletion of ... Thermal stability of the Thermus thermophilus isopropylmalate dehydrogenase enzyme was substantially lost upon the deletion of ... 3-ISOPROPYLMALATE DEHYDROGENASE. A, B. 349. Thermus thermophilus HB8. Mutation(s): 0 Gene Names: leuB, TTHA1230. EC: 1.1.1.85. ...
... iso-propylmalate de-hydrogenase. Takayuki Nagae,a Takashi Kawamura,b Leonard M. G. Chavas,c Ken Niwa,d Masashi Hasegawa,d ... 76.044 (3) 75.671 (2) 75.504 (4) 75.213 (2) 75.067 (2) β (°). 119.070 (2). 119.090 (2). 119.023 (1). 118.978 (4). 118.758 (1). ... 118.668 (3). Resolution range (Å). 50.00-1.84 (1.87-1.84). 50.00-2.06 (2.10-2.06). 50.00-1.80 (1.83-1.80). 50.00-1.88 (1.92- ... 3. (a) and 3. (b), respectively. Simultaneous opening of the groove and closure of the active-site entrance can be observed. ...
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. ... Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily.UniRule annotation. Automatic ... 2-isopropylmalate synthase (leuA), 2-isopropylmalate synthase (leuA). *3-isopropylmalate dehydratase large subunit (leuC), 3- ... Annotation score:3 out of 5. ,p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB ...
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"3-Isopropylmalate Dehydrogenase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2- ... Revision of the amino-acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray ... This graph shows the total number of publications written about "3-Isopropylmalate Dehydrogenase" by people in Harvard Catalyst ...
IPR019818 IsoCit/isopropylmalate_DH_CS. IPR024084 IsoPropMal-DH-like_dom. IPR011828 LEU3_arc. ... IPR019818 IsoCit/isopropylmalate_DH_CS. IPR024084 IsoPropMal-DH-like_dom. IPR011828 LEU3_arc. ... 3 - 326. Iso_dhInterPro annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, ... tr,A4FYT7,A4FYT7_METM5 3-isopropylmalate dehydrogenase OS=Methanococcus maripaludis (strain C5 / ATCC BAA-1333) OX=402880 GN= ...
The apparent Km values for 3-isopropylmalate and NAD+ were estimated to be 0.13 mM and 8.7 mM, respectively. The optimum pH for ... The apparent Km values for 3-isopropylmalate and NAD+ were estimated to be 0.13 mM and 8.7 mM, respectively. The optimum pH for ... The apparent Km values for 3-isopropylmalate and NAD+ were estimated to be 0.13 mM and 8.7 mM, respectively. The optimum pH for ... The apparent Km values for 3-isopropylmalate and NAD+ were estimated to be 0.13 mM and 8.7 mM, respectively. The optimum pH for ...
Matsunami H, Kawaguchi H, Inagaki K, Eguchi T, Kakinuma K, Tanaka H. Overproduction and substrate specificity of 3- ... isopropylmalate dehydrogenase from thiobacillus ferrooxidans. Bioscience, Biotechnology and Biochemistry. 1998;62(2):372-373. ... Matsunami, H, Kawaguchi, H, Inagaki, K, Eguchi, T, Kakinuma, K & Tanaka, H 1998, Overproduction and substrate specificity of 3 ... isopropylmalate dehydrogenase from thiobacillus ferrooxidans, Bioscience, Biotechnology and Biochemistry, vol. 62, no. 2, pp. ...
STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD711 ... STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD711. Coordinates. PDB Format Method. X-RAY ... Nurachman, Z. et al., Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic ...
Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the ... Isopropylmalate dehydrogenase-like domain * Occurring in:. *3-isopropylmalate dehydrogenase. > Isocitrate/isopropylmalate ... 3-isopropylmalate dehydrogenase Chains: A, B Molecule details › Chains: A, B. Length: 358 amino acids. Theoretical weight: ... Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the ...
3-isopropylmalate dehydrogenase (IPR023698) Member database. HAMAP. HAMAP stands for High-quality Automated and Manual ...
isocitrate/isopropylmalate dehydrogenase:. icd_forward ATGGAAAGTAAAGTAGTTGTTCCGGCACA. icd_reverse GGACGCAGCAGGATCTGTT. malate ... 3. Examples of L-form-like structures observed in the patient UTI343 urine. a-c Example images taken before (a) and during (b, ... 3.. Rowe, T. A. & Juthani-Mehta, M. Diagnosis and management of urinary tract infection in older adults. Infect. Dis. Clin. ... 3). Notably, the urinary bacterial load returned to significance (,1 × 105/ml) after the treatment was concluded and the ...
3-isopropylmalate dehydrogenase. Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432) ... 3-isopropylmalate dehydrogenase UniProtKBInterProSTRINGInteractive Modelling. 347 aa; Sequence (Fasta) ...
Kotsuka T, Akanuma S, Tomuro M, Yamagishi A, Oshima T. Further stabilization of 3-isopropylmalate dehydrogenase of an extreme ... Kotsuka, T, Akanuma, S, Tomuro, M, Yamagishi, A & Oshima, T 1996, Further stabilization of 3-isopropylmalate dehydrogenase of ... Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor ... Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor ...
Isopropylmalate dehydrogenase Sixth exon ratJ7 F Feldmann + + homo kan DEAD box RNA helicase Third intron ... Wild-type ecotype Ws (1 and 3), a rat mutant deficient in the step of T-DNA integration (2), and a rat mutant deficient in an ... Wild-type ecotype Ws (1 and 3) and typical rat mutants (2 and 4) are shown. B, Transient transformation phenotype of GUS ... A, Stable transformation phenotypes of crown gall tumorigenesis (1 and 2) and ppt resistance (3 and 4) on cut root segments 4 ...
Drugs Against Mycobacterium tuberculosis 3-Isopropylmalate Dehydrogenase Can be Developed Using Homologous Enzymes as Surrogate ... Drugs Against Mycobacterium tuberculosis 3-Isopropylmalate Dehydrogenase Can be Developed Using Homologous Enzymes as Surrogate ...
The house-keeping genes sigA, hom (encoding homoserine dehydrogenase) and gap (encoding glyceraldehyde-3-phosphate ... 10.1007/s00284-002-3728-3.PubMedView ArticleGoogle Scholar. *. Tauch A, Kassing F, Kalinowski J, Pühler A: The Corynebacterium ... The cultures were grown at 30°C with a pO2 level of 30%. The pH set point was 7, regulated with 2 M NaOH and 10% (w/v) H3PO4. ... dehydrogenase) served as controls since they are known to be transcribed by SigA [19]. Transcription profiles of cg0096, cg1083 ...
Pyruvate dehydrogenase (decarboxylase). 14.14. 1.05. 0.042. acpP. Acyl carrier protein. 13.85. 0.09. 0.579. ... Glyceraldehyde-3-phosphate dehydrogenase A. 22.31. 0.04. 0.178. +. +. fusA. GTP-binding protein chain elongation factor EF-G. ... 3. Expression of iron acquisition systems in E. coli CFT073. The signal intensity, corresponding to the relative expression of ... Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp sensitive. 4.529. 0.0013. yhfI. Hypothetical oxidoreductase YdfI. 4.523. ...
0 1 2 3 4 5 6 7 8 9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z ...
Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000256,PIRNR:PIRNR000108}. CC ... DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; ... DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; ... DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256,PIRNR:PIRNR000108}; DE EC=1.1.1.42 {ECO:0000256,PIRNR:PIRNR000108 ...
Then, 5 µl of l-glutamate dehydrogenase was added to each sample and incubated for 5 min at 30 °C. The absorbance of each ... 2c). Ammonia production from other amino acids deamination pathways, including glutamate dehydrogenase, arginine deaminase, and ... glutamate transport and glutamate dehydrogenase activity, (4) threonine deaminase activity, and (5) serine deaminase activity. ... 3a, d). Yellow colony of AK13 also appeared in the agar plate culture when YS11 and AK13 were each spotted at the edge of the ...
Thermoacidophilic archaeon dehydrogenase. Computer model showing the structure of 3-isopropylmalate dehydrogenase from ... dehydrogenase, illustration, isopropylmalate, molecular model, molecular structure, molecule, nobody, space-fill, space-filled ... Caption: Thermoacidophilic archaeon dehydrogenase. Computer model showing the structure of 3-isopropylmalate dehydrogenase from ...
Inactivation of the β(1,2)-xylosyltransferase and the α(1,3)-fucosyltransferase genes in Nicotiana tabacum BY-2 Cells by a ... Promiscuous activity of 3-isopropylmalate dehydrogenase produced at physiological level affords Escherichia coli growth on d- ... 14, no.3, p. 534-542 (2019). doi:10.1021/acschembio.9b00064 (Accepté/Sous presse). ...
Isopropylmalate Dehydrogenase. The name of this superfamily has been modified since the most recent official CATH+ release (v4_ ...
... β-isopropylmalate dehydrogenase gene; MCM, mini-chromosome maintenance complex of proteins; ORC, origin recognition complex; ...
This Histri was built automatically but not manually verified. As a consequence, the Histri can be incomplete or can contain errors ...
Arabidopsis Thaliana Isopropylmalate Dehydrogenases의 기능적 특성 Gametophyte 개발에 중요 한 역할을 계시 한다 The New Phytologist. Jan, 2011 , ... Isopropylmalate dehydrogenases (IPMDHs) 산화 decarboxylation 3-isopropylmalate (3-IPM) 미생물에 신 생 합성에서의 촉매. Arabidopsis thaliana 게놈 ... Nov, 2009 , Pubmed ID: 19674406 우리 보고 glucosinolate 생 합성 및 신 생 합성에 관여 하는 Arabidopsis isopropylmalate 효소 (AtIPMDH1)의 자세한 기능 특성화 ... Glucosinolates와 Arabidopsis의 신 생 합성의 Redox Active Isopropylmalate 효소 기능 The Plant Journal : for Cell and Molecular Biology. ...
3. Temperature-dependent changes in calculated α-helical contents. (A) A. fumigatus phytase. (B) A. nigerT213 phytase. (C) A. ... The different behaviors of the two phytases are also reflected in the calculated α-helical contents shown in Fig.3 and by the ... Feed pelleting.A commercial broiler feed containing 55% maize, 27% soya 50, 10% extruded soya, 3% fish meal, 1% soya oil, and 4 ... The crystal structure of thermostable mutants of chimeric 3-isopropylmalate dehydrogenase, 2T2M6T.Protein Eng.81995763767. ...
  • 3-Isopropylmalate dehydrogenase (EC 1.1.1.85) is an enzyme that catalyzes the chemical reactions (2R,3S)-3-isopropylmalate + NAD+ ⇌ {\displaystyle \rightleftharpoons } 4-methyl-2-oxopentanoate + CO2 + NADH (2R,3S)-3-isopropylmalate + NAD+ ⇌ {\displaystyle \rightleftharpoons } (2S)-2-isopropyl-3-oxosuccinate + H+ + NADH (2S)-2-isopropyl-3-oxosuccinate + H+ ⇌ {\displaystyle \rightleftharpoons } 4-methyl-2-oxopentanoate + CO2 Burns RO, Umbarger HE, Gross SR (1963). (wikipedia.org)
  • Thermal stability of the Thermus thermophilus isopropylmalate dehydrogenase enzyme was substantially lost upon the deletion of three residues from the C-terminus. (rcsb.org)
  • The substrate specificity of the enzyme was analyzed with synthetic (2R, 3S)-3-alkylmalates. (elsevier.com)
  • Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. (embl.de)
  • The three-dimensional structure of the enzyme 3-isopropylmalate dehydrogenase from the bacterium Thermus thermophilus in complex with Mn2+, its substrate isopropylmalate and its co-factor product NADH at 2.0 Å resolution features a fully closed conformation of the enzyme. (mtak.hu)
  • Crystal structure of porcine mitochondrial NADP + -dependent isocitrate dehydrogenase complexed with Mn 2+ and isocitrate: insights into the enzyme mechanism. (microbiologyresearch.org)
  • It codes for an enzyme called isopropyl malate dehydrogenase which is involved in conversion of pyruvic acid to leucine. (biologydiscussion.com)
  • The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. (genetex.com)
  • Interestingly, the accumulated metabolite is not the direct substrate of the mutated enzyme, 3-isopropylmalate dehydrogenase, but the substrate of isopropylmalate isomerase, which acts one step further upstream in the biosynthetic pathway of leucine. (uni-bielefeld.de)
  • 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)
  • 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)
  • IPMS1 and IPMS2, isopropylmalate synthase 1 and 2. (plantcell.org)
  • Isopropylmalic acid (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. (wikipedia.org)
  • 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)
  • The results suggest that GhCER6 encodes a functional 3-ketoacyl-CoA synthase. (labome.org)
  • Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. (harvard.edu)
  • We succeeded in further improvement of the stability of 3-isopropylmalate dehydrogenase (IPMDH) from an extreme thermophile, Thermus thermophilus, by a suppressor mutation method. (elsevier.com)
  • Structure of Thermus thermophilus homoisocitrate dehydrogenase in complex with a designed inhibitor. (semanticscholar.org)
  • In this study, structures of 3-isopropylmalate dehydrogenase (IPMDH) from Shewanella oneidensis MR-1 were determined at about 2 Å resolution under pressures ranging from 0.1 to 650 MPa using a diamond anvil cell (DAC). (iucr.org)
  • We constructed an overexpression system in Escherichia coli of the leuB gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ferrooxidans. (elsevier.com)
  • Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. (harvard.edu)
  • Indeed recent work has shown that even proteins with very high sequence identity can have different folds and functions [ 1 - 3 ], and therefore caution is needed in assigning functions simply by sequence homology in the absence of experimental validation. (biomedcentral.com)
  • Homoisocitrate dehydrogenase from Candida albicans: properties, inhibition, and targeting by an antifungal pro-drug. (semanticscholar.org)
  • Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. (semanticscholar.org)
  • Thiahomoisocitrate: a highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway. (semanticscholar.org)
  • Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase. (semanticscholar.org)
  • Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. (semanticscholar.org)
  • Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase. (semanticscholar.org)
  • Two isomers are important, the 2- and 3-isopropyl derivatives, and these are interconverted by isopropylmalate dehydratase. (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)
  • Amino acid sequence comparison between S. cerevisiaeIDH2 and S. cerevisiae NADP(+)-dependent isocitrate dehydrogenase shows nosignificant sequence identity, whereas comparison of IDH2 and Escherichia coliNADP(+)-dependent isocitrate dehydrogenase reveals a 33% sequence identity. (embl.de)
  • Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. (genetex.com)
  • The protein encoded by this gene is the NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. (genetex.com)
  • T. thiooxidans 3-isopropylmalate dehydrogenase could not utilize malate as a substrate. (elsevier.com)
  • which is catalyzed by the enzymes 3-isopropylmalate dehydrogenase and D-malate / 3-isopropylmalate dehydrogenase (decarboxylating). (ymdb.ca)
  • In this structure, the volume of the cavity at 200 MPa was reduced by less than 3% compared with that in the structure at atmospheric pressure, while additional conformation changes of the protein itself were scarcely induced. (iucr.org)
  • It recognizes a 45kDa protein, which is identified as isocitrate dehydrogenase (IDH1). (genetex.com)
  • Purification, catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from Escherichia coli. (harvard.edu)
  • 3, 137-155 (1996) REFERENCE 9 AUTHORS Fujita,N., Mori,H., Yura,T. and Ishihama,A. TITLE Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region JOURNAL Nucleic Acids Res. (nig.ac.jp)
  • The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate dehydrogenase. (embl.de)
  • Journal Article] Pressure adaptation of 3-isopropylmalate dehydrogenase from an extremely piezophilic bacterium is attributed to a single amino acid substitution. (nii.ac.jp)
  • To elucidate determinants of differences in thermostability between mesophilic and psychrophilic monomeric isocitrate dehydrogenases (IDHs) from Azotobacter vinelandii ( Av IDH) and Colwellia maris ( Cm IDH), respectively, chimeric enzymes derived from the two IDHs were constructed based on the recently resolved three-dimensional structure of Av IDH, and several characteristics of the two wild-type and six chimeric IDHs were examined. (microbiologyresearch.org)
  • Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. (genetex.com)
  • Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. (rcsb.org)
  • [3] Threonine dehydrogenase catalyzes the deamination and dehydration of threonine to 2-ketobutyrate and ammonia. (wikipedia.org)
  • 2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH. (ebi.ac.uk)
  • Therefore, it comes as no surprise that isolation, characterization, and engineering of thermostable enzymes, as well as the search for the determinants of thermostability, are hot spots of current research ( 2 , 3 , 9-11 ). (asm.org)
  • Revision of the amino-acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray crystallography. (harvard.edu)
  • HQ584991 Polytomella parva strain SAG 63-3 18S ribosomal RNA gene, partial sequence. (uni-goettingen.de)
  • NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae iscomposed of two nonidentical subunits, designated IDH1 (Mr approximately 40,000) and IDH2 (Mr approximately 39,000). (embl.de)
  • 2016. Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: Insights on Leucine and Aliphatic Glucosinolate Biosynthesis. (wustl.edu)
  • Furthermore, we showed CaCO 3 that precipitates earlier in an experiment modifies membrane rigidity of YS11 strain via upregulation of branched chain fatty acid synthesis. (springer.com)
  • 146. McClerklin SA*, Lee SG*, Harper CP, Nwumeh R, Jez JM, Kunkel BN (2018) Indole-3-acetaldehyde dehydrogenase-dependent auxin synthesis contributes to virulence of Pseudomonas syringae strain DC 3000. (wustl.edu)
  • Analyses of the thermostability and kinetic parameters of the chimeric enzymes indicated that region 2, corresponding to domain II, and particularly region 3 located in the C-terminal part of domain I, are involved in the thermolability of Cm IDH, and that the corresponding two regions of Av IDH are important for exhibiting higher catalytic activity and affinity for isocitrate than Cm IDH. (microbiologyresearch.org)
  • Similar results have been found for cofactor use by isopropylmalate dehydrogenase ( 6 ) and for hormone receptors ( 7 ). (sciencemag.org)
  • The expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon T. sibiricus is reported. (iucr.org)
  • In yeast, 2-isopropyl-3-oxosuccinate is involved in the metabolic pathway called leucine biosynthesis pathway. (ymdb.ca)
  • It may tightly associate or interact with the pyruvate dehydrogenase complex. (abcam.com)
  • Overexpression of IDH2, however, did not result in increasedNAD(+)-dependent isocitrate dehydrogenase activity, suggesting that both IDH1 andIDH2 subunits are required for catalytic activity. (embl.de)
  • 148. Sherp AM, Westfall CS, Alvarez S, Jez JM (2018) A rabidopsis thaliana GH3.15 acyl acid amido synthetase has a highly specific substrate preference for the auxin precursor indole-3-butryic acid. (wustl.edu)
  • The crystal structure of the photosynthetic A 4 isoform of glyceraldehyde-3-phosphate dehydrogenase from the model plant A. thaliana has been solved at 2.6 Å resolution. (iucr.org)
  • The molecular and ecological basis of CaCO 3 precipitating (CCP) bacteria has been poorly illuminated. (springer.com)
  • Ansgar Bruning, Andrea Gingelmaier, Klaus Friese and Ioannis Mylonas, " New Prospects for Nelfinavir in Non-HIV-Related Diseases", Current Molecular Pharmacology (2010) 3: 91. (eurekaselect.com)
  • Multiple molecular forms of Acanthamoeba lactic dehydrogenase. (cbrc.jp)
  • 3-Isopropylmalate dehydrogenase was purified to homogeneity from the acidophilic autotroph Thiobacillus thiooxidans. (elsevier.com)
  • The 3-isopropylmalate dehydrogenase of Thiobacillus ferrooxidans had broad specificity toward the alkylmalates. (elsevier.com)
  • In the most plausible scenario, prior to hydride transfer the ε-amino group of Lys185 acts as a general base in the reaction, aiding the deprotonation reaction of 3-isopropylmalate prior to hydride transfer by employing a low-barrier proton shuttle mechanism involving a water molecule. (mtak.hu)
  • Isoleucine forms a negative feedback loop with threonine dehydrogenase. (wikipedia.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)
  • 3-Isopropylmalate is an intermediate in valine, leucine and isoleucine biosynthesis. (umaryland.edu)
  • Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships. (expasy.org)
  • Computer model showing the structure of 3-isopropylmalate dehydrogenase from Sulfolobus acidocaldarius. (sciencephoto.com)
  • Bacteria influence these parameters through their metabolic activity, the production of biofilm, and exopolysaccharide (EPS) formation, eventually leading to microbially induced CaCO 3 precipitation (MICP). (springer.com)
  • BCAAs are broken down effectively by dehydrogenase and decarboxylase enzymes expressed by immune cells, and are required for lymphocyte growth and proliferation and cytotoxic T lymphocyte activity. (wikipedia.org)
  • Glucosinolates (GSLs) produced by vegetables in the family Brassicaceae, such as broccoli and cabbage, have recently attracted considerable attention, because they apparently provide anticarcinogenic, antioxidative, and antimicrobial activity ( 1 - 3 ). (pnas.org)
  • Met-derived 4-methylsulfinylbutyl GSL (4MSOB) deserves special attention because its degraded product, sulforaphane, which was first isolated from broccoli, exhibits pronounced anticarcinogenic activity ( 1 - 3 ). (pnas.org)