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.

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)

*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- ...

*Isocitrate/isopropylmalate dehydrogenase family

In molecular biology, the isocitrate/isopropylmalate dehydrogenase family is a protein family consisting of the evolutionary ... Zhang T, Koshland DE (January 1995). "Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase". ... Tartrate dehydrogenase EC 1.1.1.93 catalyses the reduction of tartrate to oxaloglycolate. Hurley JH, Thorsness PE, Ramalingam V ... Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation ...

*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.. ...

*List of MeSH codes (D08)

... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 --- acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 --- acyl-coa ... 2-isopropylmalate synthase MeSH D08.811.913.050.618 --- malate synthase MeSH D08.811.913.050.622 --- 3-oxoacyl-(acyl-carrier- ... l-iditol 2-dehydrogenase MeSH D08.811.682.047.150.700.649 --- mannitol dehydrogenase MeSH D08.811.682.047.150.900 --- uridine ... 11-beta-hydroxysteroid dehydrogenase type 1 MeSH D08.811.682.047.436.174.600 --- 11-beta-hydroxysteroid dehydrogenase type 2 ...

*List of EC numbers (EC 1)

EC 1.1.1.1: alcohol dehydrogenase EC 1.1.1.2: alcohol dehydrogenase (NADP+) EC 1.1.1.3: homoserine dehydrogenase EC 1.1.1.4: (R ... L-arabinitol 4-dehydrogenase EC 1.1.1.13: L-arabinitol 2-dehydrogenase EC 1.1.1.14: L-iditol 2-dehydrogenase EC 1.1.1.15: D- ... glutaryl-CoA dehydrogenase EC 1.3.8.7: medium-chain acyl-CoA dehydrogenase EC 1.3.8.8: long-chain acyl-CoA dehydrogenase EC 1.3 ... NADH dehydrogenase EC 1.6.99.4: now *EC 1.18.1.2 EC 1.6.99.5: NADH dehydrogenase (quinone) EC 1.6.99.6: NADPH dehydrogenase ( ...

*Amino acid synthesis

The third step is the NAD+-dependent oxidation of β-isopropylmalate via the action of a dehydrogenase to yield α- ... α-Isopropylmalate synthase reacts with this substrate and Acetyl CoA to produce α-isopropylmalate. An isomerase then isomerizes ... Phosphoglycerate dehydrogenase is regulated by the concentration of serine in the cell. At high concentrations this enzyme will ... Glutamate dehydrogenase catalyzes the reductive amination of α-ketoglutarate to glutamate. A transamination reaction takes ...

*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- ...

*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 ...
1DR8: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
aconitate hydratase/ copper ion binding; FUNCTIONS IN: aconitate hydratase activity, copper ion binding; INVOLVED IN: response to cadmium ion; LOCATED IN: mitochondrion, chloroplast; EXPRESSED IN: 25 plant structures; EXPRESSED DURING: 16 growth stages; CONTAINS InterPro DOMAIN/s: Aconitase family, 4Fe-4S cluster binding site (InterPro:IPR018136), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha (InterPro:IPR001030), Aconitase A/isopropylmalate dehydratase small subunit, swivel (InterPro:IPR000573), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomain 2 (InterPro:IPR015932), Aconitase/Iron regulatory protein 2/2-methylisocitrate dehydratase (InterPro:IPR015934), Aconitase-like core (InterPro:IPR015937), Aconitase/3-isopropylmalate dehydratase, swivel (InterPro:IPR015928), Aconitase/iron regulatory protein 2 (InterPro:IPR006249), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomains 1 and 3 (InterPro:IPR015931); ...
The LEU3 gene of the yeast Saccharomyces cerevisiae, which is involved in the regulation of at least two LEU structural genes (LEU1 and LEU2), has been cloned by complementation of leu3 mutations and shown to reside within a 5.6-kb fragment. Transformation of leu3 mutants with LEU3-carrying multicopy plasmids restored normal, leucine-independent growth behavior in the recipients. It also restored approximately wild-type levels of isopropylmalate isomerase (LEU1) and β-isopropylmalate dehydrogenase (LEU2), which were strongly reduced when exogenous leucine was supplied. Strains containing a disrupted leu3 allele were constructed by deleting 0.7-kb of LEU3 DNA and inserting the yeast HIS3 gene in its place. Like other leu3 mutants, these strains were leaky leucine auxotrophs, owing to a basal level of expression of LEU1 and LEU2. Southern transfer and genetic analyses of strains carrying a disrupted leu3 allele demonstrated that the cloned gene was LEU3, as opposed to a suppressor. Disruption of ...
1a05: Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism.
1DPZ: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
the active site is contained within one subunit between the canonical ICDH fold and a large insert domain that itself is a probable rudiment form of ICDH fold resulted from duplication, domain swapping and deletion ...
Chemical Entities of Biological Interest (ChEBI) is a freely available dictionary of molecular entities focused on small chemical compounds.
Bacteroides species, saccharolytic Gram-negative obligate anaerobes, are frequently isolated from human infections such as peritonitis, abscesses and bacteremia. Among the species in the genus Bacteroides, thespecies called "B. fragilis group" areparticularly involved inhuman infections andaremedically important because they account for a major part of anaerobic isolates from clinical specimens. The purpose of this study was to develop PCR primers that specifically and simultaneously amplify theβ-isopropylmalate dehydrogenase gene leuB in B. fragilis group species. We determined partial nucleotide sequences of leuB genes and compared them in seventeen strains of nine B. fragilis group species, and the regions that are conserved among Bacteroides strains but different from other species were used as a B. fragilis group-specific PCR primer set, BacLBF-BacLBR. Specificity tests of the primer set using 52 phenotypically characterized strains and 75 isolates from rat feces showed only one case each ...
Thermoacidophilic archaeon dehydrogenase. Computer model showing the structure of 3-isopropylmalate dehydrogenase from Sulfolobus acidocaldarius. - Stock Image C035/6196
University of Canterbury Library α-Isopropylmalate synthase (α-IPMS) is responsible for catalysing the first committed step in leucine biosynthesis. This pathway is found in plants and microorganisms, including pathogenic bacteria such as Mycobacterium tuberculosis and Neisseria meningitidis. α-IPMS catalyses a Claisen condensation reaction between α-ketoisovalerate (KIV) and acetyl coenzyme A (AcCoA) to form the product α-isopropylmalate (IPM). This enzyme undergoes feedback inhibition by the end product of the pathway, leucine. This regulation allows the control of the rate leucine biosynthesis. This project focuses on the α-IPMS enzymes from M. tuberculosis and N. meningitidis (MtuIPMS and NmeIPMS). These α-IPMS enzymes are homodimeric in structure. Each monomer consists of a catalytic domain which comprises of a (β/α)8 barrel fold, two subdomains and a regulatory domain, to which the allosteric binding of the natural inhibitor leucine occurs. The mechanism by which the allosteric ...
The long-standing problem of achieving high activity of a thermophilic enzyme at low temperatures and short reaction times with little tradeoff in thermostability has been solved by directed evolution, an alcohol dehydrogenase found in hot springs serving as the catalyst in enantioselective ketone reductions
In vitro reconstitution of an artificial metabolic pathway has emerged as an alternative approach to conventional in vivo fermentation-based bioproduction. Particularly, employment of thermophilic and hyperthermophilic enzymes enables us a simple preparation of highly stable and selective biocatalytic modules and the construction of in vitro metabolic pathways with an excellent operational stability. In this study, we designed and constructed an artificial in vitro metabolic pathway consisting of nine (hyper)thermophilic enzymes and applied it to the conversion of glycerol to lactate. We also assessed the compatibility of the in vitro bioconversion system with methanol, which is a major impurity in crude glycerol released from biodiesel production processes. The in vitro artificial pathway was designed to balance the intrapathway consumption and regeneration of energy and redox cofactors. All enzymes involved in the in vitro pathway exhibited an acceptable level of stability at high temperature (60°C),
ID GeneChip Array ORGANISM Probe_Pairs ORF Descriptions SPOT_ID TTHB84orF1327600_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0001 DNA polymerase III, beta subunit TTHB84orF1327900_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0002 enolase (2-phosphoglycerate dehydratase) TTHB84orF1328000_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0003 pyruvate kinase TTHB84orR1328100_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0004 hypothetical protein TTHB84orR1328400_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0005 conserved hypothetical protein TTHB84orR1328500_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0006 1-deoxy-D-xylulose-5-phosphate synthase TTHB84orR1328600_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0007 conserved hypothetical protein TTHB84orR1328900_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0008 phage shock protein A TTHB84orF1330000_at TTHB8401a520105F Thermus thermophilus HB8 16 TTHA0011 molybdenum cofactor biosynthesis protein A ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Sodium atom in PDB 2dpw: Hpothetical Transferase Structure From Thermus Thermophilus
More than 50 researchers, extension staff and industry representatives attended this years IPM forum in Toowoomba. The IPM forum is an annual event and brings
The structural characterization of glycolipids from Thermus thermophilus HB8 was performed in this study. Two neutral and one acidic glycolipids were extracted and purified by the modified TLC-blotting method, after which their chemical structures were determined by chemical composition analysis, mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy. The structure of one of the neutral glycolipids, NGL-A, was Galp(α1-6)GlcpNacyl(β1-2)Glcp(α1-)acyl2Gro, and the other, NGL-C, was Galf(β1-2)Galp(α1-6)GlcpNacyl(β1-2)Glcp(α1-)acyl2Gro. The structure of NGL-C was identical to that reported previously [Oshima, M. and Ariga, T. (1976) FEBS Lett. 64, 440]. Both neutral glycolipids shared a common structural unit found in the Thermus species. The acyl groups found in NGL-A and NGL-C, iso-type pentadecanoxy and heptadecanoxy fatty acid, were also the same as those found in this species. In contrast, the acidic glycolipid, AGL-B, possessed the structure of N-(((GlcpNAc(α1-)acyl2Gro)P-2
Thermus thermophilus ATCC ® BAA-163D-5™ Designation: Genomic DNA from Thermus thermophilus Strain DSM 7039 TypeStrain=False Application:
Looking for online definition of thermophile in the Medical Dictionary? thermophile explanation free. What is thermophile? Meaning of thermophile medical term. What does thermophile mean?
Thermophily in the Geobacteraceae: Geothermobacter ehrlichii gen. nov., sp. nov., a novel thermophilic member of the Geobacteraceae from the Bag City hydrothermal ...
p>An evidence describes the source of an annotation, e.g. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.,/p> ,p>,a href="/manual/evidences">More…,/a>,/p> ...
Thermus thermophilus ATCC ® BAA-163™ Designation: DSM 7039 TypeStrain=False Application: Produces aqualysin I Biotechnology
TamA interacts with LeuB, the homologue of Saccharomyces cerevisiae Leu3p, to regulate gdhA expression in Aspergillus nidulans Journal Articles Refereed ...
Affiliation:九州大学,農学研究院,教授, Research Field:応用微生物学・応用生物化学,Applied microbiology,Environmental agriculture(including landscape science),資源開発工学,Applied biochemistry, Keywords:Streptomyces,Thermus,Thermus thermophilus,Thermus thermphilus,放線菌,微生物,プラスミド,DNA複製,ゲノム,バイオミネラリゼーション, # of Research Projects:15, # of Research Products:155, Ongoing Project:ネパール野生キノコのライブラリーと健康機能を含むデータベースの構築
Although some progress has been made in the development of genetic technology for Bacillus stearothermophilus, strains of the genus Thermus, and Methanobacterium thermoautotrophicum, the lack of efficient and reliable genetic exchange systems, a repertoire of mutants, or plasmids that express useful genetic markers has hampered the exploitation of these organisms for basic and applied research. Recent progress in the development of genetic techniques for B. stearothermophilus NUB36 makes it possible to elucidate the molecular and genetic mechanisms of thermophily in this organism. The genetic characterization of the B. stearothermophilus NUB36 genome is the first step in attaining this goal. The map was constructed using the linkages reported by Vallier and Welker. The genetic map of B. stearothermophilus NUB36 may be similar to the B. subtilis 168 map; however, the identity of the genes in B. stearothermophilus with the putative analogous genes of B. subtilis must be rigorously established by

Sequence Similarity 









- 1DR8: STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177 Sequence...Sequence Similarity - 1DR8: STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177 Sequence...

Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure ... 3-ISOPROPYLMALATE DEHYDROGENASE protein, length: 344 (BLAST) Sequence Similarity Cutoff. Rank. Chains in Cluster. Cluster ID / ...
more infohttp://www.rcsb.org/pdb/explore/sequenceCluster.do?structureId=1DR8

3-Isopropylmalate dehydrogenase - Wikipedia3-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- ...
more infohttps://en.wikipedia.org/wiki/3-Isopropylmalate_dehydrogenase

RCSB PDB - Protein Feature View 









 - 3-isopropylmalate dehydrogenase - P37412 (LEU3 SALTY)RCSB PDB - Protein Feature View - 3-isopropylmalate dehydrogenase - P37412 (LEU3 SALTY)

2R,3S-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH UniProt ... Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. ...
more infohttps://www.rcsb.org/pdb/protein/P37412

leuB - 3-isopropylmalate dehydrogenase - Streptomyces bingchenggensis (strain BCW-1) - leuB gene & proteinleuB - 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 ...
more infohttps://www.uniprot.org/uniprot/D7CCD3

MmarC5 1068 - 3-isopropylmalate dehydrogenase - Methanococcus maripaludis (strain C5 / ATCC BAA-1333) - MmarC5 1068 gene &...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= ...
more infohttps://www.uniprot.org/uniprot/A4FYT7

IUCr) High-pressure-induced water penetration into 3--iso-propylmalate de-hydrogenaseIUCr) 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. ...
more infohttp://journals.iucr.org/d/issues/2012/03/00/mh5057/index.html

SWISS-MODEL Template Library | 1dpz.1SWISS-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 ...
more infohttps://swissmodel.expasy.org/templates/1dpz

PDB 1a05 structure summary ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBIPDB 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 ...
more infohttp://www.ebi.ac.uk/pdbe/entry/pdb/1a05

LeuB type2 (MF 01035) | InterPro | EMBL-EBILeuB type2 (MF 01035) | InterPro | EMBL-EBI

3-isopropylmalate dehydrogenase (IPR023698) Member database. HAMAP. HAMAP stands for High-quality Automated and Manual ...
more infohttp://www.ebi.ac.uk/interpro/ISignatureOverview?sig=MF_01035&query=Q

Protein & Peptide Letters, Volume 21 - Number 12Protein & Peptide Letters, Volume 21 - Number 12

Drugs Against Mycobacterium tuberculosis 3-Isopropylmalate Dehydrogenase Can be Developed Using Homologous Enzymes as Surrogate ... Drugs Against Mycobacterium tuberculosis 3-Isopropylmalate Dehydrogenase Can be Developed Using Homologous Enzymes as Surrogate ...
more infohttps://benthamscience.com/journals/protein-and-peptide-letters/volume/21/issue/12/

The alternative sigma factor SigB of Corynebacterium glutamicum modulates global gene expression during transition from...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 ...
more infohttps://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-8-4

Enhanced calcium carbonate-biofilm complex formation by alkali-generating Lysinibacillus boronitolerans YS11 and alkaliphilic...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 ...
more infohttps://link.springer.com/article/10.1186%2Fs13568-019-0773-x

Identification of Arabidopsis rat Mutants | Plant PhysiologyIdentification 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 ...
more infohttp://www.plantphysiol.org/content/132/2/494/tab-figures-data

CDBB 667 Strain Passport - StrainInfoCDBB 667 Strain Passport - StrainInfo

This Histri was built automatically but not manually verified. As a consequence, the Histri can be incomplete or can contain errors ...
more infohttp://www.straininfo.net/strains/657935

Archaeon dehydrogenase - Stock Image C035/6196 - Science Photo LibraryArchaeon 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 ...
more infohttp://www.sciencephoto.com/media/847769/view

KEGG SSDB Best Search Result: zma:100191657KEGG SSDB Best Search Result: zma:100191657

ble:BleG1_0889 isopropylmalate dehydrogenase K00052 345 184 ( -) 48 0.258 349 -, 1 pcu:pc1783 probable isocitrate dehydrogenase ... sic:SiL_1275 Isocitrate/isopropylmalate dehydrogenase K00052 336 158 ( -) 42 0.266 203 -, 1 sid:M164_1411 isopropylmalate/ ... tum:CBW65_00885 isocitrate dehydrogenase 358 244 ( -) 61 0.264 409 -, 1 bag:Bcoa_3151 isocitrate/isopropylmalate dehydrogenase ... bts:Btus_2543 isocitrate/isopropylmalate dehydrogenase 363 270 ( -) 67 0.271 410 -, 1 kyr:CVV65_12635 isocitrate dehydrogenase ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=zma:100191657

KEGG SSDB Best Search Result: bll:BLJ 1607KEGG SSDB Best Search Result: bll:BLJ 1607

puv:PUV_22430 acyl-CoA dehydrogenase 381 102 ( -) 29 0.304 92 ,-, 1 rfr:Rfer_0880 aldehyde dehydrogenase K00128 510 102 ( -) 29 ... rhz:RHPLAN_42650 NAD-dependent aldehyde dehydrogenase K00128 505 100 ( 0) 29 0.310 113 -, 2 saz:Sama_2362 PQQ enzyme repeat ... cdq:BOQ54_01220 aldehyde dehydrogenase family protein K00128 512 105 ( -) 30 0.330 112 -, 1 cti:RALTA_B0367 putative GST- ... chel:AL346_08095 aldehyde dehydrogenase K00128 512 102 ( -) 29 0.321 112 -, 1 fox:FOXG_05909 hypothetical protein K10295 526 ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=bll:BLJ_1607

Table of Contents - November 01, 2010, 431 (3) | Biochemical JournalTable of Contents - November 01, 2010, 431 (3) | Biochemical Journal

Enhancement of the latent 3-isopropylmalate dehydrogenase activity of promiscuous homoisocitrate dehydrogenase by directed ... Biochemical Journal Nov 01, 2010, 431 (3) 363-371; DOI: https://doi.org/10.1042/BJ20100668 ... assembly and constitutive exocytosis by interacting with the N-peptide and the closed-conformation C-terminus of syntaxin 3 Ren ... Biochemical Journal Nov 01, 2010, 431 (3) 321-336; DOI: https://doi.org/10.1042/BJ20100766 ...
more infohttp://www.biochemj.org/content/431/3

Molecular Analysis of the Gene Encoding a Novel Cold-Adapted Chitinase (ChiB) from a Marine Bacterium, Alteromonas sp. Strain O...Molecular Analysis of the Gene Encoding a Novel Cold-Adapted Chitinase (ChiB) from a Marine Bacterium, Alteromonas sp. Strain O...

Moreover, like that of NAD+-dependent alanine dehydrogenases (12), the thermal flexibility of ChiB could not be explained by ... Cold-adapted alanine dehydrogenases from two Antarctic bacterial strains: gene cloning, protein characterization, and ... Structural basis for cold adaptation: sequence, biochemical properties, and crystal structure of malate dehydrogenase from ... The kinetic properties of ChiA, ChiB, and ChiC are shown in Table ​Table3.3. The kcat/Km value for the ChiB reaction at 20°C ...
more infohttp://pubmedcentralcanada.ca/pmcc/articles/PMC142845/?lang=en-ca

Plus itPlus it

isopropylmalate synthase. TFL. 5,5,5-trifluoro-dl-leucine. OMT. l-O-methylthreonine. MS. Murashige and Skoog. FAD. flavin ... 2015). The impact of the branched-chain ketoacid dehydrogenase complex on amino acid homeostasis in Arabidopsis. Plant Physiol. ... 2007). Two Arabidopsis genes (IPMS1 and IPMS2) encode isopropylmalate synthase, the branchpoint step in the biosynthesis of ... 2015). A feedback insensitive isopropylmalate synthase affects acylsugar composition in cultivated and wild tomato. Plant ...
more infohttp://www.plantcell.org/content/29/6/1480

Thermostable alpha-glucan phosphorylases: characteristics and industrial applications | SpringerLinkThermostable alpha-glucan phosphorylases: characteristics and industrial applications | SpringerLink

Qian X, Sujino K, Otter A, Palcic MM, Hindsgaul O (1999) Chemoenzymatic synthesis of α-(1→3)-gal(NAc)-terminating glycosides of ... Suzuki T, Yasugi M, Arisaka F, Yamagishi A, Oshima T (2001) Adaptation of a thermophilic enzyme, 3-isopropylmalate ... dehydrogenase, to low temperatures. Protein Eng 14:85-91. https://doi.org/10.1093/protein/14.2.85 CrossRefPubMedGoogle Scholar ... J Appl Anim Nutr 3:e8. https://doi.org/10.1017/jan.2015.6 CrossRefGoogle Scholar ...
more infohttps://link.springer.com/article/10.1007%2Fs00253-018-9233-9

Members - Svergun Group - EMBLMembers - Svergun Group - EMBL

Structure 23(3):558-570. doi: 10.1016/j.str.2015.01.011. Europe PMC , doi ... Biochemistry 55(3):560-574. doi: 10.1021/acs.biochem.5b00839. Europe PMC , doi ... Structure 26(3) doi: 10.1016/j.str.2018.01.016. Europe PMC , doi ... Dual Role of the Active Site Residues of Thermus thermophilus 3 ... Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.. ...
more infohttp://www.embl-hamburg.de/research/unit/svergun/members/index.php?s_personId=CP-60003233

Isocitrate/isopropylmalate dehydrogenase family - WikipediaIsocitrate/isopropylmalate dehydrogenase family - Wikipedia

In molecular biology, the isocitrate/isopropylmalate dehydrogenase family is a protein family consisting of the evolutionary ... Zhang T, Koshland DE (January 1995). "Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase". ... Tartrate dehydrogenase EC 1.1.1.93 catalyses the reduction of tartrate to oxaloglycolate. Hurley JH, Thorsness PE, Ramalingam V ... Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation ...
more infohttps://en.wikipedia.org/wiki/Isocitrate/isopropylmalate_dehydrogenase_family

homoisocitrate - Semantic Scholarhomoisocitrate - Semantic Scholar

Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase. ... Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.. *Ying Lin, Jerome Volkman, +5 authors Paul F ... Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.. *Ying Lin, Susan S Alguindigue, ... Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase.. *Takashi Yamamoto, Kentaro Miyazaki, ...
more infohttps://www.semanticscholar.org/topic/homoisocitrate/238499

Network Portal - Gene DVU2093Network Portal - Gene DVU2093

2-isopropylmalate synthase 46, 103. DVU2982. 3-isopropylmalate dehydratase large subunit 46, 103. ... POSITION A C G T 1 0.0 0.0 1.0 0.0 2 0.0 0.333333 0.666667 0.0 3 1.0 0.0 0.0 0.0 4 0.0 0.0 0.0 1.0 5 0.25 0.0 0.75 0.0 6 0.0 ... POSITION A C G T 1 0.333333 0.0 0.0 0.666667 2 0.0 0.0 1.0 0.0 3 0.166667 0.833333 0.0 0.0 4 0.0 0.0 1.0 0.0 5 0.833333 0.0 ... DVU2093 is enriched for 9 functions in 3 categories. Enrichment Table (9). Function. System. ...
more infohttp://networks.systemsbiology.net/dvu/gene/DVU2093
  • 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)
  • 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)
  • 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)
  • The reiterated domains are composed of chitin-binding domain (ChtBD) type 3 and two fibronectin type III (Fn3)-like domains. (pubmedcentralcanada.ca)
  • Outer membrane-associated GlcNAcase A and periplasmic GlcNAcase B belong to glycosyl hydrolase family 20, and cytoplasmic GlcNAcase C belongs to glycosyl hydrolase family 3 ( 35 , 36 , 39 ). (pubmedcentralcanada.ca)