3-Isopropylmalate Dehydrogenase: 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.Alcohol Oxidoreductases: 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).Thermus thermophilus: 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.2-Isopropylmalate Synthase: 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.Thermus: Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.Enzyme Stability: 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.MalatesIsocitrate Dehydrogenase: 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.Hot Temperature: Presence of warmth or heat or a temperature notably higher than an accustomed norm.Sulfolobus: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Protein Denaturation: Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.L-Lactate Dehydrogenase: 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.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Sequence Alignment: 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.Protein Conformation: 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).Cloning, Molecular: 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.Alcohol Dehydrogenase: 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.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Kinetics: The rate dynamics in chemical or physical systems.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Proteins: 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.Agrobacterium tumefaciens: 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, Mutant Strains: Rats bearing mutant genes which are phenotypically expressed in the animals.Ascorbic Acid Deficiency: 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, Genetically Modified: PLANTS, or their progeny, whose GENOME has been altered by GENETIC ENGINEERING.t-Complex Genome Region: 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.Transformation, Genetic: 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.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Peptides: 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.Manuscripts as Topic: 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)Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Manuscripts, MedicalAntimicrobial Cationic Peptides: 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.Aspergillus flavus: 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.Eurotiales: 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.Aspergillus: A genus of mitosporic fungi containing about 100 species and eleven different teleomorphs in the family Trichocomaceae.Ascomycota: 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.Aflatoxins: 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.Sulfolobus acidocaldarius: A species of aerobic, chemolithotrophic ARCHAEA consisting of coccoid cells that utilize sulfur as an energy source. The optimum temperature for growth is 70-75 degrees C. They are isolated from acidic fields.Sulfolobus solfataricus: A species of thermoacidophilic ARCHAEA in the family Sulfolobaceae, found in volcanic areas where the temperature is about 80 degrees C and SULFUR is present.Archaea: One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.Origin Recognition Complex: The origin recognition complex is a multi-subunit DNA-binding protein that initiates DNA REPLICATION in eukaryotes.Chromosomes, Archaeal: Structures within the nucleus of archaeal cells consisting of or containing DNA, which carry genetic information essential to the cell.Replication Origin: A unique DNA sequence of a replicon at which DNA REPLICATION is initiated and proceeds bidirectionally or unidirectionally. It contains the sites where the first separation of the complementary strands occurs, a primer RNA is synthesized, and the switch from primer RNA to DNA synthesis takes place. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)DNA Replication: The process by which a DNA molecule is duplicated.Adenosine Triphosphatases: A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.Saccharomyces cerevisiae: 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.Saccharomyces cerevisiae Proteins: 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.
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)
Sequence Similarity
- 1DR8: STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177 Sequence...
AtREG645
PDB 1a05 structure summary ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBI
RCSB PDB
for 1DPZ
2R,3S)-3-isopropylmalate(2-) (CHEBI:35121)
Simultaneous detection of Bacteroides fragilis group species by leuB -directed PCR - Arimochi, Hideki - Authors - Tokushima...
Archaeon dehydrogenase - Stock Image C035/6196 - Science Photo Library
EMBL: AE006468.LEUA
NZResearch.org
EMBL: AE006468.PE320
Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution - Chemical Communications (RSC...
SWISS-MODEL Repository | Q73B98
B3DPI3 | SWISS-MODEL Repository
Joseph Jez | Arts & Sciences
In vitro conversion of glycerol to lactate with thermophilic enzymes | Bioresources and Bioprocessing | Full Text
Mutation - sup-78(Mal+)
Difference between revisions of "Thermus thermophilus" - microbewiki
Sodium in the structure of Hpothetical Transferase Structure From Thermus Thermophilus (pdb 2dpw)
Structural Characterization of Neutral and Acidic Glycolipids from Thermus thermophilus HB8
Thermus thermophilus (Oshima and Imahori) Williams et al. ATCC ® B
Thermophile | definition of thermophile by Medical dictionary
Appl Environ Microbiol 69(5), 2985-2993, 2003 Publication Passport - StrainInfo
Mutation - trpE38
Thermus thermophilus (Oshima and Imahori) Williams et al. ATCC ® B
TamA interacts with LeuB, the homologue of Saccharomyces cerevisiae Leu3p, to regulate gdhA expression in Aspergillus nidulans ...
KAKEN - Researchers | DOI Katsumi (40253520)
Cheesemaking | Thermophile (TPM)
natural testosterone boosters :: natural testosterone boosters Review | Buy natural testosterone boosters Online
ASMscience | The Genetic Map of Bacil
Sequence Similarity
- 1DR8: STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177 Sequence...
PDB 1a05 structure summary ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBI
RCSB PDB - Protein Feature View
- 3-isopropylmalate dehydrogenase - P37412 (LEU3 SALTY)
IUCr) High-pressure-induced water penetration into 3--iso-propylmalate de-hydrogenase
leuB - 3-isopropylmalate dehydrogenase - Streptomyces bingchenggensis (strain BCW-1) - leuB gene & protein
MmarC5 1068 - 3-isopropylmalate dehydrogenase - Methanococcus maripaludis (strain C5 / ATCC BAA-1333) - MmarC5 1068 gene &...
Isocitrate/isopropylmalate dehydrogenase family - Wikipedia
LeuB type2 (MF 01035) | InterPro | EMBL-EBI
Possible role of L-form switching in recurrent urinary tract infection | Nature Communications
SWISS-MODEL Repository | C5C2I9
Identification of Arabidopsis rat Mutants | Plant Physiology
Protein & Peptide Letters, Volume 21 - Number 12
The alternative sigma factor SigB of Corynebacterium glutamicum modulates global gene expression during transition from...
Transcriptome of Uropathogenic Escherichia coli during Urinary Tract Infection | Infection and Immunity
Enhanced calcium carbonate-biofilm complex formation by alkali-generating Lysinibacillus boronitolerans YS11 and alkaliphilic...
Archaeon dehydrogenase - Stock Image C035/6196 - Science Photo Library
LIBST Publications | UCLouvain
Analysis of mutant origin recognition complex with reduced ATPase activity in vivo and in vitro | Biochemical Journal
CDBB 667 Strain Passport - StrainInfo
Protocols and Video Articles Authored by Thomas P. Mawhinney (Translated to Korean)
Comparison of the Thermostability Properties of Three Acid Phosphatases from Molds: Aspergillus fumigatusPhytase, A. niger...
Thermostable alpha-glucan phosphorylases: characteristics and industrial applications | SpringerLink
Heat-resistant cytosolic malate dehydrogenases (cMDHs) of thermophilic intertidal snails (genus Echinolittorina): protein...
Table of Contents - November 01, 2010, 431 (3) | Biochemical Journal
Molecular Analysis of the Gene Encoding a Novel Cold-Adapted Chitinase (ChiB) from a Marine Bacterium, Alteromonas sp. Strain O...
SubstrateGeneEnzymeProteinIPMDHIMDHSynthaseNADPAlcohol dehydrogenaseMalateBiosynthesisEnzymesTartrate dehydrogenaseGlyceraldehyde-3-phosphate dThermusHomologyNADHHomoisocitrate dehydrogenasePyruvateLactate dehydrogenaseIsocitrate dehydrogenasesCofactorSequenceStrainSaccharomycesCatalyzesAcetohydroxyacidBacteriumMolecularGenesIDH1MoleculeThreonineStructureEscherichiaAmino
Substrate5
- 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)
- Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase. (semanticscholar.org)
- 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)
- 143. Damodaran S, Westfall CS, Kisely BA, Jez JM, Subramanian S (2017) Nodule-enriched Gretchen Hagen 3 enzymes have distinct substrate specificities and are important for proper soybean nodule development. (wustl.edu)
- 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)
Gene5
- LEU2 Gene, and 3. (biologydiscussion.com)
- HQ584991 Polytomella parva strain SAG 63-3 18S ribosomal RNA gene, partial sequence. (uni-goettingen.de)
- The protein encoded by this gene is the NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. (genetex.com)
- Recently, an endogenous 1-butanol production pathway in yeast Saccharomyces cerevisiae was elucidated and the deletion of the alcohol dehydrogenase gene ADH1 was found to efficiently activate 1-butanol production in S. cerevisiae . (biomedcentral.com)
- Reducing ethanol formation by deletion of the ADH1 gene encoding the major alcohol dehydrogenase did not result in further increased isobutanol production, but in strongly enhanced glycerol formation. (biomedcentral.com)
Enzyme5
- 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)
- Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. (wikipedia.org)
- 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)
Protein4
- 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)
- In molecular biology, the isocitrate/isopropylmalate dehydrogenase family is a protein family consisting of the evolutionary related enzymes isocitrate dehydrogenase, 3-isopropylmalate dehydrogenase and tartrate dehydrogenase. (wikipedia.org)
- It recognizes a 45kDa protein, which is identified as isocitrate dehydrogenase (IDH1). (genetex.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)
IPMDH1
- 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)
IMDH2
- 3-isopropylmalate dehydrogenase EC 1.1.1.85 (IMDH) catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate. (wikipedia.org)
- The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate dehydrogenase. (embl.de)
Synthase6
- 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 [OMR, acetohydroxyacid synthase small subunit 2 (AHASS2), and isopropylmalate synthase 1 (IPMS1). (plantcell.org)
- IPMS1 and IPMS2, isopropylmalate synthase 1 and 2. (plantcell.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)
- 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)
NADP2
- 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)
Alcohol dehydrogenase1
- The expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon T. sibiricus is reported. (iucr.org)
Malate1
- which is catalyzed by the enzymes 3-isopropylmalate dehydrogenase and D-malate / 3-isopropylmalate dehydrogenase (decarboxylating). (ymdb.ca)
Biosynthesis3
- In yeast, 2-isopropyl-3-oxosuccinate is involved in the metabolic pathway called leucine biosynthesis pathway. (ymdb.ca)
- 3-Isopropylmalate is an intermediate in valine, leucine and isoleucine biosynthesis. (umaryland.edu)
- 2016. Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: Insights on Leucine and Aliphatic Glucosinolate Biosynthesis. (wustl.edu)
Enzymes4
- 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)
- 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)
- 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)
- 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)
Tartrate dehydrogenase2
- Tartrate dehydrogenase EC 1.1.1.93 catalyses the reduction of tartrate to oxaloglycolate. (wikipedia.org)
- This entry represents a structural domain found in all types of isocitrate dehydrogenase, and in isopropylmalate dehydrogenase and tartrate dehydrogenase. (embl.de)
Glyceraldehyde-3-phosphate d1
- 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)
Thermus1
- Structure of Thermus thermophilus homoisocitrate dehydrogenase in complex with a designed inhibitor. (semanticscholar.org)
Homology1
- 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)
NADH2
- 2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH. (ebi.ac.uk)
- 19. The method of claim 15, wherein the pyruvate dehydrogenase with reduced sensitivity to NADH is a pyruvate dehydrogenase comprising an E354K amino acid mutation. (patentsencyclopedia.com)
Homoisocitrate dehydrogenase5
- 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)
- 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)
Pyruvate1
- It may tightly associate or interact with the pyruvate dehydrogenase complex. (abcam.com)
Lactate dehydrogenase4
- Salt-induced alteration of D(-) lactate dehydrogenase from Polyspondylium pallidum. (cbrc.jp)
- Steady-state kinetic studies on D-lactate dehydrogenase from Megasphera elsdenii. (cbrc.jp)
- Nonpolar interactions in the maleimide inactivation of Haemophilus influenzae D-lactate dehydrogenase. (cbrc.jp)
- Lactate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui. (cbrc.jp)
Isocitrate dehydrogenases1
- Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. (genetex.com)
Cofactor2
- 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)
- Similar results have been found for cofactor use by isopropylmalate dehydrogenase ( 6 ) and for hormone receptors ( 7 ). (sciencemag.org)
Sequence1
- A78798 Sequence 3 from Patent EP0563527. (atcc.org)
Strain2
- 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)
Saccharomyces1
- 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)
Catalyzes2
- 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)
Acetohydroxyacid1
- ALAC is reduced and isomerized to 2,3-dihydroxyisovalerate (DIV) by acetohydroxyacid reductoisomerase Ilv5. (biomedcentral.com)
Bacterium1
- Journal Article] Pressure adaptation of 3-isopropylmalate dehydrogenase from an extremely piezophilic bacterium is attributed to a single amino acid substitution. (nii.ac.jp)
Molecular3
- 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)
Genes2
- The analysis showed that genes commonly involved in secondary metabolism have higher expression in infected leaf tissue, including genes encoding cytochrome P450s, short-chain dehydrogenases, and oxidoreductases in the 2-oxoglutarate and Fe(II)-dependent oxygenase superfamily. (beds.ac.uk)
- Then, we successively deleted essential genes of competing pathways for synthesis of 2,3-butanediol ( BDH1 and BDH2 ), leucine ( LEU4 and LEU9 ), pantothenate ( ECM31 ) and isoleucine ( ILV1 ) resulting in an optimized metabolic flux toward isobutanol and titers of up to 0.56 g/L (13.54 mg/g glucose). (biomedcentral.com)
IDH11
- 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)
Molecule1
- 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)
Threonine1
- Isoleucine forms a negative feedback loop with threonine dehydrogenase. (wikipedia.org)
Structure2
- 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)
Escherichia1
- 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)
Amino1
- More recently, the stereo-specific isotope labeling methods of prochiral methyl groups have become available, using either regio-selectively isotope-labeled precursors or stereo-specifically 13 CH 3 -labeled amino acids. (springer.com)
