3-Isopropylmalate Dehydrogenase
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
2-Isopropylmalate Synthase
Thermus
Enzyme Stability
Isocitrate 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.
Sulfolobus
Substrate Specificity
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
Mutagenesis, Site-Directed
Protein Denaturation
L-Lactate Dehydrogenase
Crystallography, X-Ray
Models, Molecular
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
Alcohol Dehydrogenase
Base Sequence
Thiobacillus
Copyright
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)
Acidithiobacillus thiooxidans
Databases, Protein
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
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
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
Arabidopsis
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
Antimicrobial 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.
Candida
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)
Candida albicans
Candidiasis
Candidiasis, Oral
Antifungal Agents
Fluconazole
Aspergillus flavus
Eurotiales
Aspergillus
Ascomycota
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.
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)
Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans<...
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
A1T6Z4 | SWISS-MODEL Repository
Diversification of Paralogous α-Isopropylmalate Synthases by Modulation of Feedback Control and Hetero-Oligomerization in...
2R,3S)-3-isopropylmalate(2-) (CHEBI:35121)
A1SLW5 | SWISS-MODEL Repository
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...
SAUSA300 2013 - AureoWiki
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
Drosophila nikananu - Wikipèdia bahsa Acèh, ènsiklopèdia bibeuëh
Drosophila tenebrosa - Wikipèdia bahsa Acèh, ènsiklopèdia bibeuëh
From amino acid to glucosinolate biosynthesis: protein sequence changes in the evolution of methylthioalkylmalate synthase in...
Thermus thermophilus (Oshima and Imahori) Williams et al. ATCC ® B
creatinine assay kits - Rett syndrome Research Forum
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)
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ASMscience | The Genetic Map of Bacil
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. Two isomers are ... and these are interconverted by isopropylmalate dehydratase.. ...
Branched-chain amino acid
... 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 ...
List of MeSH codes (D08)
... 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- ...
3-Isopropylmalate dehydrogenase
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- ...
Amino acid synthesis
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- ...
Leucine
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 ...
List of EC numbers (EC 2)
... 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- ...
Tryptophan synthase
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 ...
HADHB
... , 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, ...
3-Isopropylmalate dehydrogenase - Wikipedia
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- ...
RCSB PDB - Protein Feature View
- 3-isopropylmalate dehydrogenase - P37412 (LEU3 SALTY)
RCSB PDB - 1DPZ: STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD711
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. ...
IUCr) High-pressure-induced water penetration into 3--iso-propylmalate de-hydrogenase
... 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. ...
leuB - 3-isopropylmalate dehydrogenase - Streptomyces bingchenggensis (strain BCW-1) - leuB gene & protein
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 ...
WikiGenes - NCU06232 - 3-isopropylmalate dehydrogenase
3-Isopropylmalate Dehydrogenase | Harvard Catalyst Profiles | Harvard Catalyst
"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 ...
MmarC5 1068 - 3-isopropylmalate dehydrogenase - Methanococcus maripaludis (strain C5 / ATCC BAA-1333) - MmarC5 1068 gene &...
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= ...
Purification and characterization of 3-isopropylmalate dehydrogenase from Thiobacillus thiooxidans<...
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 ...
Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans<...
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. ...
SWISS-MODEL Template Library | 1dpz.1
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 ...
PDB 1a05 structure summary ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBI
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 ...
LeuB type2 (MF 01035) | InterPro | EMBL-EBI
Possible role of L-form switching in recurrent urinary tract infection | Nature Communications
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 ...
SWISS-MODEL Repository | C5C2I9
Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor...
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 ...
Identification of Arabidopsis rat Mutants | Plant Physiology
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 ...
Protein & Peptide Letters, Volume 21 - Number 12
The alternative sigma factor SigB of Corynebacterium glutamicum modulates global gene expression during transition from...
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 ...
Transcriptome of Uropathogenic Escherichia coli during Urinary Tract Infection | Infection and Immunity
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. ...
Browse ORF cDNA clones by species Candida dubliniensis CD36, letter l, page 1
UniProt/TrEMBL: B8N000 ASPFN
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 ...
Enhanced calcium carbonate-biofilm complex formation by alkali-generating Lysinibacillus boronitolerans YS11 and alkaliphilic...
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 ...
Archaeon dehydrogenase - Stock Image C035/6196 - Science Photo Library
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 ...
LIBST Publications | UCLouvain
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). ...
CATH Superfamily 3.40.718.10
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)
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. ...
Comparison of the Thermostability Properties of Three Acid Phosphatases from Molds: Aspergillus fumigatusPhytase, A. niger...
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. ...
EnzymeSynthaseThermusIPMDHGene coding for 3-isopropylmalate dehydrHomologyHomoisocitrate DehydrogenaseLEU2DehydrataseNADPMalateProteinEscherichiaIMDHBacteriumIsocitrate dehydrogenasesCatalyzesNADHCharacterizationSequenceSaccharomycesArabidopsisStrainThermostabilityCofactorArchaeonYeastPyruvateIDH1PrecursorIsoformMolecularThiobacillusMoleculeThreonineAcidValineStructureActivity
Enzyme9
- 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)
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 [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)
Thermus3
- 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)
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)
Gene coding for 3-isopropylmalate dehydr1
- We constructed an overexpression system in Escherichia coli of the leuB gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ferrooxidans. (elsevier.com)
Homology2
- 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 Dehydrogenase6
- 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)
LEU21
- LEU2 Gene, and 3. (biologydiscussion.com)
Dehydratase2
- 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)
NADP3
- 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)
Malate2
- 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)
Protein2
- 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)
Escherichia2
- 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)
IMDH1
- The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate dehydrogenase. (embl.de)
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)
Isocitrate dehydrogenases2
- 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)
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)
NADH1
- 2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + NADH. (ebi.ac.uk)
Characterization1
- 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)
Sequence2
- 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)
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)
Arabidopsis1
- 2016. Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis thaliana: Insights on Leucine and Aliphatic Glucosinolate Biosynthesis. (wustl.edu)
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)
Thermostability1
- 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)
Cofactor1
- Similar results have been found for cofactor use by isopropylmalate dehydrogenase ( 6 ) and for hormone receptors ( 7 ). (sciencemag.org)
Archaeon1
- The expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon T. sibiricus is reported. (iucr.org)
Yeast1
- In yeast, 2-isopropyl-3-oxosuccinate is involved in the metabolic pathway called leucine biosynthesis pathway. (ymdb.ca)
Pyruvate1
- It may tightly associate or interact with the pyruvate dehydrogenase complex. (abcam.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)
Precursor1
- 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)
Isoform1
- 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)
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)
Thiobacillus2
- 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)
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)
Acid1
- 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)
Valine1
- 3-Isopropylmalate is an intermediate in valine, leucine and isoleucine biosynthesis. (umaryland.edu)
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)
Activity4
- 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)