OrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation ScienceHealth Care
3-Isopropylmalate DehydrogenaseAlcohol OxidoreductasesThermus thermophilus2-Isopropylmalate SynthaseThermusEnzyme StabilityMalatesIsocitrate DehydrogenaseHot TemperatureSulfolobusSubstrate SpecificityMolecular Sequence DataEscherichia coliAmino Acid SequenceMutagenesis, Site-DirectedProtein DenaturationL-Lactate DehydrogenaseCrystallography, X-RayModels, MolecularSequence AlignmentProtein ConformationCloning, MolecularAlcohol DehydrogenaseBacillus subtilisBase SequenceKinetics
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.
Malates
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.
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)

Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans<...
TY - JOUR. T1 - Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans. AU - Matsunami, Hideyuki. AU - Kawaguchi, Hiroshi. AU - Inagaki, Kenji. AU - Eguchi, Tadashi. AU - Kakinuma, Katsumi. AU - Tanaka, Hidehiko. N1 - Copyright: Copyright 2017 Elsevier B.V., All rights reserved.. PY - 1998. Y1 - 1998. N2 - We constructed an overexpression system in Escherichia coli of the leuB gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ferrooxidans. E. coli harboring the plasmid we constructed, pKK leuB1, produced 17-fold the enzyme protein of the expression system previously used for purification. The substrate specificity of the enzyme was analyzed with synthetic (2R, 3S)-3-alkylmalates. The 3-isopropylmalate dehydrogenase of Thiobacillus ferrooxidans had broad specificity toward the alkylmalates.. AB - We constructed an overexpression system in Escherichia coli of the leuB gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ...
https://okayama.pure.elsevier.com/en/publications/overproduction-and-substrate-specificity-of-3-isopropylmalate-deh
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...
1DR8: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
http://www.rcsb.org/pdb/explore/sequenceCluster.do?structureId=1DR8
AtREG645AtREG645
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); ...
http://ppdb.agr.gifu-u.ac.jp/ppdb/cgi-bin/tag_list.cgi?organism=At&tag=AtREG645
PDB 1a05 structure summary ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBIPDB 1a05 structure summary ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBI
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.
http://www.ebi.ac.uk/pdbe/entry/pdb/1a05
RCSB PDB for 1DPZRCSB PDB for 1DPZ
1DPZ: Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
http://www.rcsb.org/pdb/explore/biologyAndChemistry.do?structureId=1DPZ
A1T6Z4 | SWISS-MODEL Repository
SWISS-MODEL Repository entry for A1T6Z4 (LEU3_MYCVP), 3-isopropylmalate dehydrogenase. Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / NRRL B-24157 /PYR-1) (Mycobacterium vanbaalenii)
https://swissmodel.expasy.org/repository/uniprot/A1T6Z4
Diversification of Paralogous α-Isopropylmalate Synthases by Modulation of Feedback Control and Hetero-Oligomerization in...Diversification of Paralogous α-Isopropylmalate Synthases by Modulation of Feedback Control and Hetero-Oligomerization in...
Leu4 enzymatic activity is inhibited by leucine and CoA, and the amino acid residues responsible for this property have been identified (7). Although no detailed biochemical characterization of the LEU9-encoded isozyme has been performed, it has been shown that it is less sensitive to leucine inhibition than Leu4 is (3).. It is noteworthy that the leucine biosynthesis intermediate α-IPM plays a dual cellular role. On the one hand, it acts as an intermediate in leucine biosynthesis (5, 6), and on the other, it acts as the coactivator of the Leu3 master regulator (6), which modulates the expression of a number of genes within and beyond amino acid metabolism (6). At low α-IPM concentrations, Leu3 acts as a transcriptional repressor, while at high α-IPM concentrations, it acts as an activator (6). It has been recently found that α-IPM could also have a role in the ability of Leu3 to determine the chronological life span of yeast (11, 12).. A LEU4 deletion (leu4Δ) results in leucine bradytrophy ...
https://ec.asm.org/content/14/6/564
2R,3S)-3-isopropylmalate(2-) (CHEBI:35121)2R,3S)-3-isopropylmalate(2-) (CHEBI:35121)
Chemical Entities of Biological Interest (ChEBI) is a freely available dictionary of molecular entities focused on small chemical compounds.
http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:1565
A1SLW5 | SWISS-MODEL Repository
SWISS-MODEL Repository entry for A1SLW5 (LEUC_NOCSJ), 3-isopropylmalate dehydratase large subunit. Nocardioides sp (strain ATCC BAA-499 / JS614)
https://swissmodel.expasy.org/repository/uniprot/A1SLW5
Simultaneous detection of Bacteroides fragilis group species by leuB -directed PCR - Arimochi, Hideki - Authors - Tokushima...
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 ...
https://repo.lib.tokushima-u.ac.jp/en/list/author-page/60214/item/110763
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 Sulfolobus acidocaldarius. - Stock Image C035/6196
http://www.sciencephoto.com/media/847769/view
EMBL: AE006468.LEUA
AE006468.LEUA Location/Qualifiers FT CDS_pept complement(132167..133738) FT /codon_start=1 FT /transl_table=11 FT /gene=leuA FT /locus_tag=STM0113 FT /product=2-isopropylmalate synthase FT /EC_number=2.3.3.13 FT /note=similar to E. coli 2-isopropylmalate synthase FT (AAC73185.1); Blastp hit to AAC73185.1 (523 aa), 92% FT identity in aa 1 - 523 FT /db_xref=EnsemblGenomes-Gn:STM0113 FT /db_xref=EnsemblGenomes-Tr:AAL19077 FT /db_xref=GOA:P15875 FT /db_xref=InterPro:IPR000891 FT /db_xref=InterPro:IPR002034 FT /db_xref=InterPro:IPR005671 FT /db_xref=InterPro:IPR013709 FT /db_xref=InterPro:IPR013785 FT /db_xref=InterPro:IPR036230 FT /db_xref=UniProtKB/Swiss-Prot:P15875 FT /protein_id=AAL19077.1 FT /translation=MSQQVIIFDTTLRDGEQALQASLSAKEKLQIALALERMGVDVMEV FT GFPVSSPGDFESVQTIARTIKNSRVCALARCVEKDIDVAAQALKVADAFRIHTFIATSP FT MHIATKLRSTLDEVIERAVYMVKRARNYTDDVEFSCEDAGRTPVDDLARVVEAAINAGA FT RTINIPDTVGYTMPFEFAGIISGLYERVPNIDKAIISVHTHDDLGIAVGNSLAAVHAGA FT ...
http://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-id?query=AE006468.LEUA&db=EMBL&ident=ACNUC7421
NZResearch.org
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 ...
https://nzresearch.org.nz/records?i%5Bthesis_level%5D=Masters&i%5Byear%5D=2013&locale=en&recordset=research
EMBL: AE006468.PE320
AE006468.PE320 Location/Qualifiers FT CDS_pept 374197..374823 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=STM0330 FT /product=putative 3-isopropylmalate isomerase FT (dehydratase), subunit with LeuC FT /note=similar to E. coli isopropylmalate isomerase subunit FT (AAC73182.1); Blastp hit to AAC73182.1 (201 aa), 39% FT identity in aa 3 - 193 FT /db_xref=EnsemblGenomes-Gn:STM0330 FT /db_xref=EnsemblGenomes-Tr:AAL19284 FT /db_xref=GOA:Q8ZRI9 FT /db_xref=InterPro:IPR000573 FT /db_xref=InterPro:IPR004431 FT /db_xref=InterPro:IPR015928 FT /db_xref=InterPro:IPR033940 FT /db_xref=UniProtKB/Swiss-Prot:Q8ZRI9 FT /protein_id=AAL19284.1 FT /translation=MDTFKQISGRIAPMLEPNIDTDVIMPKQFLKGIDRQGLDKGVFFD FT RRFMAGGQPNPDFILNMPGWQSATFLLVGPNFGCGSSREHAVWGLKQLGVRGLIGSTFA FT GIFDDNCQRNGILTVSLDEPALARLAQLAASADTNSITVSLDRCEITTAEETISFVISE FT LKRAMLAAGEDAIAWTLQYLPEIENFEVAHYSRRPWLKRPASPRG atggatacgt ttaagcaaat cagcgggcga attgcgccga tgctggaacc gaatatcgac 60 actgatgtga ttatgccaaa acagttcctg ...
http://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-id?query=AE006468.PE320&db=EMBL&ident=ACNUC7421
Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution - Chemical Communications (RSC...Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution - Chemical Communications (RSC...
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
http://pubs.rsc.org/en/content/articlelanding/2017/cc/c7cc05377k
SAUSA300 2013 - AureoWikiSAUSA300 2013 - AureoWiki
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_2013 (SAUSA300_RS11070); symbol: leuD; product: isopropylmalate isomerase small subunit
https://aureowiki.med.uni-greifswald.de/SAUSA300_2013
Joseph Jez | Arts & SciencesJoseph Jez | Arts & Sciences
Jez JM, Lee SG, Sherp AM (2016) The next green movement: plant biology for the environment and sustainability. Science 353, 1241-4. Kilgore M, Holland CK, Jez JM, Kutchan TM (2016) Identification of a noroxomaritidine reductase with Amaryllidaceae alkaloid biosynthesis-related activities. J Biol Chem 291, 16740-52. Lee SG, Nwumeh R, Jez JM (2016) Structure and mechanism of isopropylmalate dehydrogenase from Arabidopsis thaliana: insights on leucine and aliphatic glucosinolate biosynthesis. J Biol Chem 291, 13421-30. Herrmann J, Nathin D, Lee SG, Sun T, Jez JM (2015) Recapitulating the structural evolution of redox regulation in adenosine-5-phosphosulfate kinase from cyanobacteria to plants. J Biol Chem 290, 24705-14. Korasick DA, Jez JM, Strader LC (2015) Refining the nuclear auxin response pathway through structural biology. Curr Opin Plant Biol 27, 22-8. Cahoon RE, Lutke WK, Cameron JC, Chen S, Lee SG, Rivard RS, Rea PA, Jez JM (2015) Adaptive engineering of phytochelatin-based heavy metal ...
https://artsci.wustl.edu/faculty-staff/joseph-jez
In vitro conversion of glycerol to lactate with thermophilic enzymes | Bioresources and Bioprocessing | Full TextIn vitro conversion of glycerol to lactate with thermophilic enzymes | Bioresources and Bioprocessing | Full Text
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),
https://bioresourcesbioprocessing.springeropen.com/articles/10.1186/s40643-014-0018-4
Mutation - sup-78(Mal+)
F-, araC14, leuB6(Am), secA206(aziR), fhuA23, lacY1, tsx-67, purE42, glnX44(AS), galK2(Oc), λ-, trpE38, sup-78(Mal+)?, rfbC1?, mgl-51?, rpsL109(strR), malA38?, glpR201, xylA5, mtl-1, thiE1 ...
https://cgsc2.biology.yale.edu/Mutation.php?ID=11873
Difference between revisions of Thermus thermophilus - microbewiki
1. JOSE CARLOS QUINTELA, ERNST P.,GUNTER A.,VICENTE A.,MIGUEL A. DE P. Structure of Peptidoglycan from Thermus thermophilus HB8. JOURNAL OF BACTERIOLOGY, 1995, Vol. 177. p. 4947-4962. http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=177270&blobtype=pdf 2. Henne A, Bruggemann H, Raasch C, Wiezer A, Hartsch T, Liesegang H, Johann A, Lienard T, Gohl O, Martinez-Arias R, Jacobi C, Starkuviene V, Schlenczeck S, Dencker S, Huber R, Klenk HP, Kramer W, Merkl R, Gottschalk G, Fritz HJ. The genome sequence of the extreme thermophile Thermus thermophilus. Nat Biotechnol. 2004 May, Vol 22. p.547-53. http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&list_uids=15064768&dopt=AbstractPlus&holding=f1000%2Cf1000m%2Cisrctn 3. Pantazaki AA, Tambaka MG, Langlois V, Guerin P, Kyriakidis DA. Polyhydroxyalkanoate (PHA) biosynthesis in Thermus thermophilus: purification and biochemical properties of PHA synthase. Mol Cell Biochem. 2003 Dec;254(1-2):173-83. ...
https://microbewiki.kenyon.edu/index.php?title=Thermus_thermophilus&diff=next&oldid=26502
Sodium in the structure of Hpothetical Transferase Structure From Thermus Thermophilus (pdb 2dpw)
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Sodium atom in PDB 2dpw: Hpothetical Transferase Structure From Thermus Thermophilus
http://sodium.atomistry.com/pdb2dpw.html
Structural Characterization of Neutral and Acidic Glycolipids from Thermus thermophilus HB8Structural Characterization of Neutral and Acidic Glycolipids from Thermus thermophilus HB8
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
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0035067
Thermus thermophilus (Oshima and Imahori) Williams et al. ATCC ® BThermus thermophilus (Oshima and Imahori) Williams et al. ATCC ® B
Thermus thermophilus ATCC ® BAA-163D-5™ Designation: Genomic DNA from Thermus thermophilus Strain DSM 7039 TypeStrain=False Application:
https://www.atcc.org/Products/All/BAA-163D-5.aspx?slp=1
Thermophile | definition of thermophile by Medical dictionaryThermophile | definition of thermophile by Medical dictionary
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?
https://medical-dictionary.thefreedictionary.com/thermophile
Appl Environ Microbiol 69(5), 2985-2993, 2003 Publication Passport - StrainInfo
Thermophily in the Geobacteraceae: Geothermobacter ehrlichii gen. nov., sp. nov., a novel thermophilic member of the Geobacteraceae from the Bag City hydrothermal ...
http://www.straininfo.net/publications/3347
Mutation - trpE38
F-, araC14, leuB6(Am), secA206(aziR), fhuA23, lacY1, proC83, tsx-67, purE42, glnX44(AS), galK2(Oc), λ-, trpE38, xthA15, his-208, rfbC1, mgl-51, argG77, rpsL109(strR), glpR201, xylA5, mtl-1, ilvA681, katG17::Tn10, thiE1, metA160 ...
https://cgsc.biology.yale.edu/Mutation.php?ID=4955
Drosophila nikananu - Wikipèdia bahsa Acèh, ènsiklopèdia bibeuëhDrosophila nikananu - Wikipèdia bahsa Acèh, ènsiklopèdia bibeuëh
Naseukah nyoë na di yup Creative Commons Attribution-ShareAlike License; syarat laén kadang na Eu Syarat Ngui keu leubèh trang ...
https://ace.wikipedia.org/wiki/Drosophila_nikananu
Drosophila tenebrosa - Wikipèdia bahsa Acèh, ènsiklopèdia bibeuëhDrosophila tenebrosa - Wikipèdia bahsa Acèh, ènsiklopèdia bibeuëh
Naseukah nyoë na di yup Creative Commons Attribution-ShareAlike License; syarat laén kadang na Eu Syarat Ngui keu leubèh trang ...
https://ace.wikipedia.org/wiki/Drosophila_tenebrosa
From amino acid to glucosinolate biosynthesis: protein sequence changes in the evolution of methylthioalkylmalate synthase in...From amino acid to glucosinolate biosynthesis: protein sequence changes in the evolution of methylthioalkylmalate synthase in...
Methylthioalkylmalate synthase (MAM) catalyzes the committed step in the side chain elongation of Met, yielding important precursors for glucosinolate biosynthesis in Arabidopsis thaliana and other Brassicaceae species. MAM is believed to have evolved from isopropylmalate synthase (IPMS), an enzyme …
https://pubmed.ncbi.nlm.nih.gov/21205930/
Thermus thermophilus (Oshima and Imahori) Williams et al. ATCC ® BThermus thermophilus (Oshima and Imahori) Williams et al. ATCC ® B
Thermus thermophilus ATCC ® BAA-163™ Designation: DSM 7039 TypeStrain=False Application: Produces aqualysin I Biotechnology
https://www.atcc.org/Products/Cells_and_Microorganisms/Bacteria/Extremophiles/BAA-163.aspx
creatinine assay kits - Rett syndrome Research Forumcreatinine assay kits - Rett syndrome Research Forum
A plant pathway that initiates with the formation of citramalate from pyruvate and acetyl-CoA by citramalate synthase (CMS) is proven to contribute to the synthesis of α-ketoacids and vital odor-active esters in apple (Malus × domestica) fruit. Microarray screening led to the invention of a gene with excessive amino acid similarity to 2-isopropylmalate synthase (IPMS). However, practical …. Citramalate synthase yields a biosynthetic pathway for isoleucine and straight- and branched-chain ester formation in ripening apple fruit Read More ». ...
https://rsrf.org/tag/creatinine-assay-kits/
TamA interacts with LeuB, the homologue of Saccharomyces cerevisiae Leu3p, to regulate gdhA expression in Aspergillus nidulans ...TamA interacts with LeuB, the homologue of Saccharomyces cerevisiae Leu3p, to regulate gdhA expression in Aspergillus nidulans ...
TamA interacts with LeuB, the homologue of Saccharomyces cerevisiae Leu3p, to regulate gdhA expression in Aspergillus nidulans Journal Articles Refereed ...
https://findanexpert.unimelb.edu.au/display/publication33513
KAKEN - Researchers | DOI Katsumi (40253520)KAKEN - Researchers | DOI Katsumi (40253520)
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
https://nrid.nii.ac.jp/nrid/1000040253520/
Cheesemaking | Thermophile (TPM)Cheesemaking | Thermophile (TPM)
Cheesemaking provides courses and equipment to home cheese makers in Australia. If you love cheese and want to learn how to make it at home, then register for our intensive courses.
https://www.cheesemaking.com.au/shop/tpm/
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ASMscience | The Genetic Map of Bacil
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
http://www.asmscience.org/content/book/10.1128/9781555818388.chap33
3-Isopropylmalate dehydrogenase3-Isopropylmalate dehydrogenase
Parsons SJ, Burns RO (February 1969). "Purification and Properties of β-Isopropylmalate Dehydrogenase". J. Biol. Chem. 244 (3 ... is an enzyme that is a part of the isopropylmalate dehydrogenase family, which catalyzes the chemical reactions: (2R,3S)-3- ... isopropylmalate + NAD+ ⇌ {\displaystyle \rightleftharpoons } 4-methyl-2-oxopentanoate + CO2 + NADH (2R,3S)-3-isopropylmalate + ... Calvo JM, Stevens CM, Kalyanpur MG, Umbarger HE (December 1964). "The Absolute Configuration of α-carboxyisocaproic Acid (3- ...
https://en.wikipedia.org/wiki/3-Isopropylmalate_dehydrogenase
Isopropylmalic acidIsopropylmalic 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. (Articles lacking sources from July 2013, All articles lacking ...
https://en.wikipedia.org/wiki/Isopropylmalic_acid
Isocitrate dehydrogenaseIsocitrate dehydrogenase
Isocitrate/isopropylmalate dehydrogenase family The isocitrate dehydrogenase 3 isozyme is a heterotetramer that is composed of ... Eukaryotic isocitrate dehydrogenase enzymes on the other hand, have not been fully discovered yet. Each dimer of IDH has two ... Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) and (EC 1.1.1.41) is an enzyme that catalyzes the oxidative decarboxylation of ... Isocitrate dehydrogenase: RCSB PDB Molecule of the Month Archived 2013-12-24 at the Wayback Machine Overview of all the ...
https://en.wikipedia.org/wiki/Isocitrate_dehydrogenase
List of MeSH codes (D08)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- ...
https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)
GottfriediaGottfriedia
112 (3): 417-429. doi:10.1111/j.1365-2672.2011.05204.x. ISSN 1364-5072. PMID 22121830. La Duc, Myron T; Satomi, Masataka; Agata ... 56 (3): 383-394. doi:10.1016/j.mimet.2003.11.004. ISSN 0167-7012. PMID 14967230. Patel, Sudip; Gupta, Radhey S. (2020-01-01). " ... 49 (3): 1083-1090. doi:10.1099/00207713-49-3-1083. ISSN 1466-5026. PMID 10425765. Shida, O.; Takagi, H.; Kadowaki, K.; Komagata ... 3-oxoacid CoA-transferase subunit B, LTA synthase family protein, sulphate ABC transporter permease subunit CysW, class I SAM- ...
https://en.wikipedia.org/wiki/Gottfriedia
Branched-chain amino acidBranched-chain amino acid
A series of four more enzymes - isopropylmalate synthase, isopropylmalate isomerase, isopropylmalate dehydrogenase, and ... Threonine dehydrogenase catalyzes the deamination and dehydration of threonine to 2-ketobutyrate and ammonia. Isoleucine forms ... BCAAs are broken down effectively by dehydrogenase and decarboxylase enzymes expressed by immune cells, and are required for ... On the other hand, unchecked activity of this complex causes branched-chain keto acid dehydrogenase kinase deficiency. The ...
https://en.wikipedia.org/wiki/Branched-chain_amino_acid
Amino acid synthesisAmino 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- ...
https://en.wikipedia.org/wiki/Amino_acid_synthesis
List of EC numbers (EC 1)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- ... L-rhamnose 1-dehydrogenase [NAD(P)+] EC 1.1.1.379: (R)-mandelate dehydrogenase EC 1.1.1.380: L-gulonate 5-dehydrogenase EC 1.1. ... uronate dehydrogenase EC 1.2.1.36: retinal dehydrogenase EC 1.2.1.37: Now EC 1.17.1.4, xanthine dehydrogenase EC 1.2.1.38: N- ...
https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)
LeucineLeucine
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 ... whereas the dehydrogenase enzyme is found exclusively in the mitochondrion (Sabourin and Bieber 1981, 1983). Importantly, this ...
https://en.wikipedia.org/wiki/Leucine
List of EC numbers (EC 2)List of EC numbers (EC 2)
... isocitrate dehydrogenase (NADP+)] kinase EC 2.7.1.117: Now EC 2.7.11.18, myosin-light-chain kinase EC 2.7.1.118: ADP-thymidine ... 2-isopropylmalate synthase EC 2.3.3.14: homocitrate synthase EC 2.3.3.15: sulfoacetaldehyde acetyltransferase EC 2.3.3.16: ... pyruvate dehydrogenase (acetyl-transferring)] kinase EC 2.7.1.100: S-methyl-5-thioribose kinase EC 2.7.1.101: tagatose kinase ... isocitrate dehydrogenase (NADP+)] kinase EC 2.7.11.6: [tyrosine 3-monooxygenase] kinase EC 2.7.11.7: myosin-heavy-chain kinase ...
https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)
1D PFV: 1DR81D PFV: 1DR8
STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177. Help ...
https://www.rcsb.org/sequence/1DR8
PDB 3UDU | Chain CRYSTAL STRUCTURE OF PUTATIVE 3-ISOPROPYLMALATE DEHYDROGENASE FROM CAMPYLOBACTER JEJUNI | 3UDU A | 3D...PDB 3UDU | Chain CRYSTAL STRUCTURE OF PUTATIVE 3-ISOPROPYLMALATE DEHYDROGENASE FROM CAMPYLOBACTER JEJUNI | 3UDU A | 3D...
CRYSTAL STRUCTURE OF PUTATIVE 3-ISOPROPYLMALATE DEHYDROGENASE FROM CAMPYLOBACTER JEJUNI - 3UDU , canSAR.ai ...
https://cansar.ai/structure/3UDU/3d/3UDU_A
Genome Summary of Neisseria meningitidis M22822
Putative Neisseria meningitidis M22822 RM systems. Ref: Retchless,A.C. et al. unpublished. REBASE ref # 22542. Complete sequence: 2,173,901 bp. GenBank #: CP016680. REBASE acronym: Nme22822. Org_num: 20176. All begin A6L50_. ...
http://tools.neb.com/genomes/summary.php?genome_id=24815
Identification and Characterisation of a pH-stable GFP | Scientific ReportsIdentification and Characterisation of a pH-stable GFP | Scientific Reports
Figure 3: Characterisation of pH-tdGFP as a biomarker.. (a) Intracellular oligomerisation of pH-tdGFP was examined. Indicated ... 3). Furthermore, the introduction of the mutation I167T resulted in a shift of the emission maxima from 510 nm to 503 nm at pH ... After screening, 3 m. of LB medium were added to the Petri dish, the cells were released into the medium and incubated ... 1a). For the initial two screening rounds, we diversified our library using error-prone PCR with 3-4 base changes per gene. In ...
https://www.nature.com/articles/srep28166?error=cookies_not_supported&code=5e22cac7-bdaa-4c01-b4b6-c28d367357f1
SCOP 1.69: Domain d1t0la : 1t0l ASCOP 1.69: Domain d1t0la : 1t0l A
Family c.77.1.1: Dimeric isocitrate & isopropylmalate dehydrogenases [53660] (3 proteins). the active site is between the two ... Fold c.77: Isocitrate/Isopropylmalate dehydrogenase-like [53658] (1 superfamily). consists of two intertwined (sub)domains ... Superfamily c.77.1: Isocitrate/Isopropylmalate dehydrogenase-like [53659] (5 families) the constituent families form similar ... Protein NADP-dependent isocitrate dehydrogenase [82524] (2 species). *. Species Human (Homo sapiens) [TaxId:9606] [110715] (2 ...
http://scop.berkeley.edu/sunid=106216&ver=1.69
SMART: Iso dh domain annotationSMART: Iso dh domain annotation
... and in isopropylmalate dehydrogenase and tartrate dehydrogenase. The crystal structure of Escherichia coli isopropylmalate ... Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - complex with Mn. 2y41. Structure of Isopropylmalate ... Tartrate dehydrogenase ( EC 1.1.1.93 ) shows strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser ... The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate ...
https://smart.embl.de/smart/do_annotation.pl?DOMAIN=Iso_dh&START=33&END=358&E_VALUE=1.37e-169&TYPE=SMART&BLAST=TVTLIPGDGIGPEISASVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEEASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAAKIEAACFATIKDGKSLTKDLGGNAKCSDFTEEI
HOMD :: SEQF2448HOMD :: SEQF2448
Inosine-5-monophosphate dehydrogenase. 116. SEQF2448,KI273077.1. SEQF2448_00119 jb [NA] [AA] 2001/666. 109421-111421. ... Acetolactate synthase isozyme 3 small subunit. 88. SEQF2448,KI273077.1. SEQF2448_00090 jb [NA] [AA] 372/123. 78400-78771. 2- ... Acetolactate synthase isozyme 3 small subunit. 84. SEQF2448,KI273077.1. SEQF2448_00086 jb [NA] [AA] 1014/337. 73875-74888. ... 3-isopropylmalate dehydrogenase. 45. SEQF2448,KI273077.1. SEQF2448_00046 jb [NA] [AA] 2070/689. 24134-26203. ATP-dependent zinc ...
https://homd.org/genome/explorer?gid=SEQF2448&anno=prokka
New Discovery Fuels Case for Intelligent Design - Reasons to BelieveNew Discovery Fuels Case for Intelligent Design - Reasons to Believe
This reaction sequence is catalyzed by the enzymes dubbed LeuA, LeuC, LeuD, and LeuB (2-isopropylmalate synthase, ... alcohol dehydrogenase) from the yeast Saccharomyces cerevisiae. To make the starting material, 2-keto-isovalerate, they ... isopropylmalate isomerase complex, and 3-isopropylmalate dehydrogenase, respectively). The team determined that these enzymes ... Once they had formed 2-keto-4-methylhexanoate, the researchers reasoned that this compound could be converted to 3-methyl-1- ...
https://reasons.org/explore/publications/articles/new-discovery-fuels-case-for-intelligent-design
Consensus pan-genome assembly of the specialised wine bacterium Oenococcus oeni | BMC Genomics | Full TextConsensus pan-genome assembly of the specialised wine bacterium Oenococcus oeni | BMC Genomics | Full Text
3. Visualisation of the core-genome and fGI assemblies. Full versions of the annotated assemblies are available in Additional ... Additional file 3:. Core-genome and fGI assemblies of ortholog clusters. A spreadsheet containing annotated and assembled ... 22] (Additional file 3). This methodology links clusters together based on the consensus of the layout of ORFs in individual de ... 3a, Additional file 3).. In addition to generating an assembled consensus core-genome, fGIs were also assembled. The fGIs were ...
https://bmcgenomics.biomedcentral.com/articles/10.1186/s12864-016-2604-7
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... G12.450.400 IMP Dehydrogenase D8.811.682.47.485 D8.811.682.47.820.450 Industrial Waste D27.888.284.404 Inhalant Abuse C25.467 ...
https://decs.bvs.br/P/mnchg2014.txt
研究成果を検索 - Keio University
Hamada, K., Isobe, T. & Senna, M., 1996 4月 1, In: Journal of Materials Science Letters. 15, 7, p. 603-605 3 p.. 研究成果: Review ... Kitajima, T., Izawa, M., Hashido, R., Nakano, N. & Makabe, T., 1996 8月 5, In: Applied Physics Letters. 69, 6, p. 758-760 3 p.. ... Kamata, T., Puzon, W. & Takada, Y., 1996, In: Biochemical Journal. 317, 3, p. 959 1 p.. 研究成果: Comment/debate › 査読 ... Ando, T., Ohta, E. & Sato, T., 1996 11月, In: Journal of Magnetism and Magnetic Materials. 163, 3, p. 277-284 8 p.. 研究成果: ...
https://keio.pure.elsevier.com/ja/publications/?page=1501&ordering=publicationYearThenTitle&descending=true&showAdvanced=false&allConcepts=true&inferConcepts=true&originalSearch=&improvedLayoutOrganisationUuid=
Find Research outputs - Waseda University
Nakatsuji, H., Hu, Z. M., Nakai, H. & Ikeda, K., 1997 Oct 8, In: Surface Science. 387, 1-3, p. 328-341 14 p.. Research output: ... Dubitzky, W., Schuster, A., Hughes, J. & Bell, D., 1997, In: Applied Intelligence. 7, 3, p. 187-204 18 p.. Research output: ... Read, H. G., Murakami, H. & Hono, K., 1997 Feb 1, In: Scripta Materialia. 36, 3, p. 355-361 7 p.. Research output: Contribution ... Yasuda, K. & Kamakura, T., 1997 Sep 29, In: Applied Physics Letters. 71, 13, p. 1771-1773 3 p.. Research output: Contribution ...
https://waseda.pure.elsevier.com/en/publications/?ordering=publicationYearThenTitle&descending=true&showAdvanced=false&allConcepts=true&inferConcepts=true&originalSearch=&improvedLayoutOrganisationUuid=&format=&page=1321
Code System Concept
DeCSDeCS
Dehydrogenase, beta-IPM Dehydrogenase, beta-Isopropylmalate beta IPM Dehydrogenase beta Isopropylmalate Dehydrogenase beta-IPM ... beta IPM Dehydrogenase. beta Isopropylmalate Dehydrogenase. beta-IPM Dehydrogenase. beta-Isopropylmalate Dehydrogenase. ... Dehydrogenase, 3-Isopropylmalate. Dehydrogenase, beta-IPM. Dehydrogenase, beta-Isopropylmalate. ... 3-Isopropylmalate Dehydrogenase - Preferred Concept UI. M0076384. Scope note. An NAD+ dependent enzyme that catalyzes the ...
https://decs.bvsalud.org/en/ths/resource/?id=50598
Network 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. ...
http://networks.systemsbiology.net/dvu/gene/DVU2093
Finding step leuB for L-isoleucine biosynthesis in Sinorhizobium meliloti 1021
D-malate dehydrogenase (decarboxylating) (EC 1.1.1.83) (characterized). 52%. 98%. 333.2. Tartrate dehydrogenase/decarboxylase; ... Comment: The dehydrogenase is encoded by a leuB-type enzyme. Similarly as for leuCD, any 3-isopropylmalate dehydrogenase should ... TDH; D-malate dehydrogenase [decarboxylating]; EC 1.1.1.93; EC 4.1.1.73; EC 1.1.1.83. 50%. 314.7. ... 2 candidates for leuB: 3-methylmalate dehydrogenase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. Other hit. Other id ...
https://papers.genomics.lbl.gov/cgi-bin/gapView.cgi?orgs=orgsFit&set=aa&orgId=FitnessBrowser__Smeli&path=ile&step=leuB
Pre GI: BLASTP Hits
3-isopropylmalate dehydrogenase. 8e-11. 66.6. NC_008536:4921224:4924597. 4924597. 4925181. 585. Solibacter usitatus Ellin6076, ...
http://pregi.bi.up.ac.za/pre_gi_blast.php?blast_source_accession=NC_007681&blast_cds_query=NC_007681:930921:933039&sort=cds
Analyze Study Data | ProtaBankAnalyze Study Data | ProtaBank
... isopropylmalate dehydrogenase; subunit interaction; thermostability ... We have investigated factors affecting stability at the subunit-subunit interface of the dimeric enzyme 3-isopropylmalate ... dehydrogenase (IPMDH) from Bacillus subtilis. Site-directed mutagenesis was used to replace methionine 256, a key residue in ... Increased thermal stability against irreversible inactivation of 3-isopropylmalate dehydrogenase induced by decreased van der ...
https://www.protabank.org/study_analysis/YpMCn3qQ3/
Targeted inactivation of Salmonella Agona metabolic genes by group II introns and in vivo assessment of pathogenicity and anti...Targeted inactivation of Salmonella Agona metabolic genes by group II introns and in vivo assessment of pathogenicity and anti...
Chin Piaw Gwee1, Chai Hoon Khoo1, Swee Keong Yeap2, Geok Chin Tan3, Yoke Kqueen Cheah​1 ... A) Lane 1 and 2: Wild-type control template of sopB gene (1170); Lane 3: sop B mutated gene (2170 bp) in double knockout ΔsopBΔ ... Lane 3: Retargeted intron targeting argD gene in S. Agona. (B) & (C) Intron insertion into targeted gene was identified by ... Figure 3: Blood parameter profiles (A, B, and C), in vivo colonization of vital organs in tumour bearing mice (D) and ...
https://peerj.com/articles/5989/
Seed Viewer
Carbon dioxide (YMDB00912) - Yeast Metabolome Database
Lipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase ... 2-oxoglutarate dehydrogenase, mitochondrial. General function:. Involved in oxoglutarate dehydrogenase (succinyl-transferring) ... oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). Gene Name:. KGD1. ... Glycine dehydrogenase [decarboxylating], mitochondrial. General function:. Involved in glycine dehydrogenase (decarboxylating) ...
http://www.ymdb.ca/compounds/YMDB00912?smpdb_pathways=8
Recent advances in the microbial synthesis of lactate-based copolymer | Bioresources and Bioprocessing | Full TextRecent advances in the microbial synthesis of lactate-based copolymer | Bioresources and Bioprocessing | Full Text
The most common lactate-based copolymer is poly(lactate-co-3-hydroxybutyrate) [P(LA-co-3HB)], within which the difference of LA ... LeuCD isopropyl malate (IPM) isomerase, PanE 2HB dehydrogenase, PrpE propionyl-CoA synthetase, PDHc pyruvate dehydrogenase ... and the isopropyl malate (IPM) isomerase gene (leuCD) of E. coli W3110, as well as the 2HB dehydrogenase gene (panE) of ... The introduction of the succinate semialdehyde dehydrogenase gene (sucD), the 4HB dehydrogenase gene (4hbD), and the CoA ...
https://bioresourcesbioprocessing.springeropen.com/articles/10.1186/s40643-021-00458-3
YJR139C 267.488705 INESSENTIAL HOM6 Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase),5-amino-6-(5...YJR139C 267.488705 INESSENTIAL HOM6 "Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase),5-amino-6-(5...
... "alpha-isopropylmalate synthase (2-Isopropylmalate Synthase),2-isopropylmalate synthase, " YPR075C 5.027926 INESSENTIAL OPY2 ... "dihydrolipoamide dehydrogenase precursor (mature protein is the E3 component of alpha-ketoacid dehydrogenase complexes), serine ... "NADH dehydrogenase (ubiquinone), complex I (NADH to ubiquinone),NADH dehydrogenase (ubiquinone)" YNL292W 2.275999 INESSENTIAL ... "NAPDH dehydrogenase (old yellow enzyme), isoform 2,NADPH dehydrogenase, " YOR066W 5.999553 INESSENTIAL "biological_process ...
https://genomics.lbl.gov/YeastFitnessData/websitefiles/ratioresults/thrRatio_07.txt
"sequence id","alias","species","description",...
Isocitrate/isopropylmalate dehydrogenase [Interproscan].","protein_coding" "CPD08164","leuC","Staphylococcus aureus","3- ... Delta-1-pyrroline-5-carboxylate dehydrogenase [Ensembl]. Proline dehydrogenase, Aldehyde dehydrogenase family [Interproscan ... ","saccharopine dehydrogenase [Ensembl]. Saccharopine dehydrogenase C-terminal domain, Saccharopine dehydrogenase NADP binding ... ","bifunctional histidinal dehydrogenase/ histidinol dehydrogenase [Ensembl]. Histidinol dehydrogenase [Interproscan]."," ...
https://bacteria.sbs.ntu.edu.sg/go/sequences/table/4078
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... G12.450.400 IMP Dehydrogenase D8.811.682.47.485 D8.811.682.47.820.450 Industrial Waste D27.888.284.404 Inhalant Abuse C25.467 ...
https://decs2018.bvsalud.org/P/mnchg2014.txt
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... G12.450.400 IMP Dehydrogenase D8.811.682.47.485 D8.811.682.47.820.450 Industrial Waste D27.888.284.404 Inhalant Abuse C25.467 ...
https://decs2016.bvsalud.org/E/mnchg2014.txt
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... G12.450.400 IMP Dehydrogenase D8.811.682.47.485 D8.811.682.47.820.450 Industrial Waste D27.888.284.404 Inhalant Abuse C25.467 ...
https://decs2019.bvsalud.org/E/mnchg2014.txt
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... G12.450.400 IMP Dehydrogenase D8.811.682.47.485 D8.811.682.47.820.450 Industrial Waste D27.888.284.404 Inhalant Abuse C25.467 ...
https://decs2014.bvsalud.org/I/mnchg2014.txt
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... G12.450.400 IMP Dehydrogenase D8.811.682.47.485 D8.811.682.47.820.450 Industrial Waste D27.888.284.404 Inhalant Abuse C25.467 ...
https://decs2020.bvsalud.org/E/mnchg2014.txt
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... G12.450.400 IMP Dehydrogenase D8.811.682.47.485 D8.811.682.47.820.450 Industrial Waste D27.888.284.404 Inhalant Abuse C25.467 ...
https://decs2015.bvsalud.org/E/mnchg2014.txt
Isocitrate and isopropylmalate dehydrogenases familySubunitIMDHProteinsEnzymeMitochondrialNADPProteinIDH1LactateTartrateEscherichiaGeneAlcoholConsistsFunctionAcidCompleteDaysTartrate dehydrogenaseIsocitrate DehydrogenasesHydroxysteroid DehydrogenasesOxidative decarboxylationAlcoholEnzymesReductaseCloningSuccinicSequencesActivityPlant PhysiologyCatalyzesGenes2019MolecularCellsPeopleShowsFunctionYear
Isocitrate and isopropylmalate dehydrogenases family2
  • The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate dehydrogenase. (embl.de)
  • IDH1, also named as PICD and IDP, belongs to the isocitrate and isopropylmalate dehydrogenases family. (ptglab.com)
Subunit2
  • Increased thermal stability against irreversible inactivation of 3-isopropylmalate dehydrogenase induced by decreased van der Waals volume at the subunit interface. (protabank.org)
  • We have investigated factors affecting stability at the subunit-subunit interface of the dimeric enzyme 3-isopropylmalate dehydrogenase (IPMDH) from Bacillus subtilis. (protabank.org)
IMDH1
  • High resolution X-ray structures of the binary complexes with bound coenzymes of IDH and the distantly related isopropylmalate dehydrogenase (IMDH) have been used to guide site directed mutagenesis, which has proven successful in inverting the coenzyme specificities of both enzymes. (umn.edu)
Proteins1
  • Further confusing matters, seemingly artifactual zinc can replace bona fide 4Fe-4S clusters in proteins purified for crystallography in the presence of oxygen (1,2,3). (ucsc.edu)
Enzyme3
  • Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. (embl.de)
  • An NAD + dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. (bvsalud.org)
  • Comment: The dehydrogenase is encoded by a leuB-type enzyme. (lbl.gov)
Mitochondrial1
  • 111 1e-23 UniRef50_Q0CXI1 Cluster: Isocitrate dehydrogenase, mitochondrial. (u-tokyo.ac.jp)
NADP5
  • 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)
  • done Score E Sequences producing significant alignments: (bits) Value UniRef50_P48735 Cluster: Isocitrate dehydrogenase [NADP], mitoch. (u-tokyo.ac.jp)
  • 86 8e-16 UniRef50_Q2K7T8 Cluster: NADP-dependent isocitrate dehydrogenase. (u-tokyo.ac.jp)
  • 57 3e-07 UniRef50_A3K670 Cluster: NADP-dependent isocitrate dehydrogenase. (u-tokyo.ac.jp)
  • Phylogenetic reconstruction reveals that the NADP-dependence of bacterial isocitrate dehydrogenases (IDH) evolved around the time the eukaryotes first appeared (3.5 billion years ago) from and NAD-dependent precursor. (umn.edu)
Protein1
  • XIII" YMR047C 3 13 3 YMR047C "Nuclear pore complex protein that is member of GLFG repeat-containing family of nucleoporins and is,XIII" YMR049C 3 13 4 YMR049C "Ymr049cp,XIII" YMR051C 3 13 5 YMR051C "TyA Gag protein. (davidson.edu)
IDH12
  • 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)
  • 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)
Lactate1
  • The most common lactate-based copolymer is poly(lactate- co -3-hydroxybutyrate) [P(LA- co -3HB)], within which the difference of LA monomer fraction will cause the change in the material properties. (springeropen.com)
Tartrate1
  • This entry represents a structural domain found in all types of isocitrate dehydrogenase, and in isopropylmalate dehydrogenase and tartrate dehydrogenase. (embl.de)
Escherichia1
  • I use two metabolic systems in Escherichia coli as models of molecular evolution: the lactose operon and the isocitrate dehydrogenase. (umn.edu)
Gene1
  • For the initial two screening rounds, we diversified our library using error-prone PCR with 3-4 base changes per gene. (nature.com)
Alcohol1
  • En la fermentación alcohólica cataliza el paso final de reducción de un aldehído a un alcohol en presencia de NADH e hidrógeno. (bvsalud.org)
Consists1
  • An individual HEAT unit consists of a small 3-helix bundle, a generic super-secondary structure analogous to a beta-alpha-beta Rossmann fold unit, meaning most occurrences of HEAT in the eukaryotic proteome are not truly homologous despite structural similarity but instead represent convergent evolution analogous to Rossmann-like fold units forming many unrelated beta propellers or TIM barrels. (ucsc.edu)
Function1
  • Acyl-CoA dehydrogenase, Domain of unknown function (DUF1974) [Interproscan]. (ntu.edu.sg)
Acid1
  • After sterilization of seeds treated with hypochlorous acid (10%) for 10 min, seeds were kept in distilled water for 3 days under dark condition at 4 ˚C to enhance germination.Seedling were grown for 7 days on 1/2 MS agar plate (0.8% agar, pH 5.7) at 22 ˚C, 24 h continuous light condition. (yokohama-cu.ac.jp)
Complete1
  • We invite you to complete a survey that will take no more than 3 minutes. (bvsalud.org)
Days1
  • After 3 days, severe diarrhea, stomach best matches for the sequences derived from Campy- ache, and shivering developed in the only 3 persons (the lobacter jejuni , but no sequences of the recovery DNA patient plus 2 family members) who had eaten undercooked sample showed any such signifi cant matches. (cdc.gov)
Tartrate dehydrogenase1
  • This entry represents a structural domain found in all types of isocitrate dehydrogenase, and in isopropylmalate dehydrogenase and tartrate dehydrogenase. (embl-heidelberg.de)
Isocitrate Dehydrogenases3
  • Isocitrate Dehydrogenases (IDHs) are important enzymes present in all living cells. (biomedcentral.com)
  • Isocitrate Dehydrogenases are important enzymes essential for survival of all organisms. (biomedcentral.com)
  • Phylogenetic reconstruction reveals that the NADP-dependence of bacterial isocitrate dehydrogenases (IDH) evolved around the time the eukaryotes first appeared (3.5 billion years ago) from and NAD-dependent precursor. (umn.edu)
Hydroxysteroid Dehydrogenases2
  • Hydroxysteroid Dehydrogenases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uams.edu)
  • Below are the most recent publications written about "Hydroxysteroid Dehydrogenases" by people in Profiles over the past ten years. (uams.edu)
Oxidative decarboxylation2
  • Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate. (embl-heidelberg.de)
  • Isocitrate dehydrogenase (IDH) catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. (neweastbioo.com)
Alcohol1
  • NADPH appeared to be regenerated primarily through pentose phosphate pathway although it may also involve malic enzyme as well as alcohol and aldehyde dehydrogenases. (biomedcentral.com)
Enzymes1
  • Isocitrate Dehydrogenase (IDH) enzymes convert isocitrate to oxoglutarate in most living organisms. (biomedcentral.com)
Reductase1
  • Characterization of a stereospecific acetoin(diacetyl) reductase from Rhodococcus erythropolis WZ010 and its application for the synthesis of (2S,3S)-2,3-butanediol. (covidauthors.org)
Cloning1
  • Cloning and Expression Analysis of Beta-Isopropylmalate Dehydrogenase from Potato. (mpg.de)
Succinic5
  • The invention provides a non-naturally occurring microbial biocatalyst including a microbial organism having a 4-hydroxybutanoic acid (4-HB) biosynthetic pathway having at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, or α-ketoglutarate decarboxylase, wherein the exogenous nucleic acid is expressed in sufficient amounts to produce monomeric 4-hydroxybutanoic acid (4-HB). (patentsencyclopedia.com)
  • The method includes culturing a non-naturally occurring microbial organism having a 4-hydroxybutanoic acid (4-HB) biosynthetic pathway including at least one exogenous nucleic acid encoding 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase or α-ketoglutarate decarboxylase under substantially anaerobic conditions for a sufficient period of time to produce monomeric 4-hydroxybutanoic acid (4-HB). (patentsencyclopedia.com)
  • 2. The non-naturally occurring microbial biocatalyst of claim 1, wherein said 4-HB biosynthetic pathway comprises 4-hydroxybutanoate dehydrogenase and succinyl-CoA synthetase and CoA-dependent succinic semialdehyde dehydrogenase, or α-ketoglutarate decarboxylase. (patentsencyclopedia.com)
  • 6. The non-naturally occurring microbial biocatalyst of claim 3, further comprising a nucleic acid encoding an exogenous succinyl-CoA synthetase, exogenous CoA-dependent succinic semialdehyde dehydrogenase or exogenous succinyl-CoA synthetase and exogenous CoA-dependent succinic semialdehyde dehydrogenase. (patentsencyclopedia.com)
  • 7. The non-naturally occurring microbial biocatalyst of claim 1, wherein said microbial organism lacks an endogenous 4-HB biosynthetic activity selected from 4-hydroxybutanoate dehydrogenase, succinyl-CoA synthetase, CoA-dependent succinic semialdehyde dehydrogenase, and α-ketoglutarate decarboxylase. (patentsencyclopedia.com)
Sequences1
  • After 3 days, severe diarrhea, stomach best matches for the sequences derived from Campy- ache, and shivering developed in the only 3 persons (the lobacter jejuni , but no sequences of the recovery DNA patient plus 2 family members) who had eaten undercooked sample showed any such signifi cant matches. (cdc.gov)
Activity1
  • It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. (umassmed.edu)
Plant Physiology1
  • Plant Physiology , 185 (3), pp.796-814. (msu.edu)
Catalyzes2
  • An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. (umassmed.edu)
  • A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. (umassmed.edu)
Genes1
  • Epithelium specific ETS transcription factor, ESE-3, of Protobothrops flavoviridis snake venom gland transactivates the promoters of venom phospholipase A2 isozyme genes. (sojo-u.ac.jp)
20191
  • [3] In 2019, a full length structure of human ACLY in complex with the substrates coenzyme A, citrate and Mg.ADP was determined by X-ray crystallography to a resolution of 3.2 Å. (wikipedia.org)
Molecular1
  • I use two metabolic systems in Escherichia coli as models of molecular evolution: the lactose operon and the isocitrate dehydrogenase. (umn.edu)
Cells1
People2
  • This graph shows the total number of publications written about "3-Isopropylmalate Dehydrogenase" by people in this website by year, and whether "3-Isopropylmalate Dehydrogenase" was a major or minor topic of these publications. (umassmed.edu)
  • Below are the most recent publications written about "3-Isopropylmalate Dehydrogenase" by people in Profiles. (umassmed.edu)
Shows1
  • The Internet is the latest ErrorDocument on 5th recipe and strings among older messages browsing a unit indolenine basis, wearing that older chapters litigate 3D Step and important users in functionality to be equivalent parameters, and that this x-ray shows to travel before it 's catalytically able to dispel 3,5-dinitrophenyl side-projects and intermediates. (reise-text.de)
Function1
  • This growth phenotype isconsistent with NAD(+)-dependent isocitrate dehydrogenase performing an essentialrole in the oxidative function of the citric acid cycle. (embl-heidelberg.de)
Year1
  • Thus, it was estimated that in 2030, national metal production will reach up to 374,000 tons/year, and Brazilian reserves were estimated at 21 million tons [3]. (peertechzpublications.com)