Amino Acid Isomerases: Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.Aldose-Ketose Isomerases: Enzymes that catalyze the interconversion of aldose and ketose compounds.Isomerases: A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.Carbon-Carbon Double Bond Isomerases: Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.Peptidylprolyl Isomerase: An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Carbohydrate Epimerases: Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.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.Protein Disulfide-Isomerases: Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.Steroid Isomerases: Enzymes that catalyze the transposition of double bond(s) in a steroid molecule. EC 5.3.3.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.Cyclophilins: A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.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.Immunophilins: Members of a family of highly conserved proteins which are all cis-trans peptidyl-prolyl isomerases (PEPTIDYLPROLYL ISOMERASE). They bind the immunosuppressant drugs CYCLOSPORINE; TACROLIMUS and SIROLIMUS. They possess rotamase activity, which is inhibited by the immunosuppressant drugs that bind to them.Tacrolimus Binding Proteins: A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-Dodecenoyl-CoA Isomerase: A carbon-carbon double bond isomerase that catalyzes the movement double bond from C3 to C2 of an unsaturated acyl-CoA. The enzyme plays a key role in allowing acyl-CoA substrates to re-enter the beta-oxidation pathway.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.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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Cyclophilin A: A 17-KDa cytoplasmic PEPTIDYLPROLYL ISOMERASE involved in immunoregulation. It is a member of the cyclophilin family of proteins that binds to CYCLOSPORINE.Ammonium Hydroxide: The hydroxy salt of ammonium ion. It is formed when AMMONIA reacts with water molecules in solution.Kinetics: The rate dynamics in chemical or physical systems.Sulfur-Sulfur Bond Isomerases: Enzymes that catalyze the transposition of a sulfur-sulfur bond. EC 5.3.4.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.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 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).Recombinant Proteins: Proteins prepared by recombinant DNA technology.Glucose-6-Phosphate Isomerase: An aldose-ketose isomerase that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate. In prokaryotic and eukaryotic organisms it plays an essential role in glycolytic and gluconeogenic pathways. In mammalian systems the enzyme is found in the cytoplasm and as a secreted protein. This secreted form of glucose-6-phosphate isomerase has been referred to as autocrine motility factor or neuroleukin, and acts as a cytokine which binds to the AUTOCRINE MOTILITY FACTOR RECEPTOR. Deficiency of the enzyme in humans is an autosomal recessive trait, which results in CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Pentoses: A class of carbohydrates that contains five carbon atoms.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Bacterial Proteins: Proteins found in any species of bacterium.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Genes, Bacterial: The functional hereditary units of BACTERIA.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Mannose-6-Phosphate Isomerase: An enzyme that catalyzes the reversible isomerization of D-mannose-6-phosphate to form D-fructose-6-phosphate, an important step in glycolysis. EC 5.3.1.8.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Triose-Phosphate Isomerase: An enzyme that catalyzes reversibly the conversion of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. A deficiency in humans causes nonspherocytic hemolytic disease (ANEMIA, HEMOLYTIC, CONGENITAL NONSPHEROCYTIC). EC 5.3.1.1.Molecular Weight: The sum of the weight of all the atoms in a molecule.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Amino Acids, Aromatic: Amino acids containing an aromatic side chain.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Amino Acids, SulfurCatalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Isomaltose: A disaccharide consisting of two glucose units in an alpha (1-6) glycosidic linkage.Proline: A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.XyloseEnzyme 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.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Metabolic Engineering: Methods and techniques used to genetically modify cells' biosynthetic product output and develop conditions for growing the cells as BIOREACTORS.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Bacillus: A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. (1/434)

In nonribosomal biosynthesis of peptide antibiotics by multimodular synthetases, amino acid monomers are activated by the adenylation domains of the synthetase and loaded onto the adjacent carrier protein domains as thioesters, then the formation of peptide bonds and translocation of the growing chain are effected by the synthetase's condensation domains. Whether the condensation domains have any editing function has been unknown. Synthesis of aminoacyl-coenzyme A (CoA) molecules and direct enzymatic transfer of aminoacyl-phosphopantetheine to the carrier domains allow the adenylation domain editing function to be bypassed. This method was used to demonstrate that the first condensation domain of tyrocidine synthetase shows low selectivity at the donor residue (D-phenylalanine) and higher selectivity at the acceptor residue (L-proline) in the formation of the chain-initiating D-Phe-L-Pro dipeptidyl-enzyme intermediate.  (+info)

Characterization of yrpC gene product of Bacillus subtilis IFO 3336 as glutamate racemase isozyme. (2/434)

Glr, the glutamate racemase of Bacillus subtilis (formerly Bacillus natto) IFO 3336 encoded by the glr gene, and YrpC, a protein encoded by the yrpC gene, which is located at a different locus from that of the glr gene in the B. subtilis genome, share a high sequence similarity. The yrpC gene complemented the D-glutamate auxotrophy of Escherichia coli WM335 cells defective in the glutamate racemase gene. Glutamate racemase activity was found in the extracts of E. coli WM335 clone cells harboring a plasmid, pYRPC1, carrying its gene. Thus, the yrpC gene encodes an isozyme of glutamate racemase of B. subtilis IFO 3336. YrpC is mostly found in an inactive inclusion body in E. coli JM109/pYRPC1 cells. YrpC was solubilized readily, but glutamate racemase activity was only slightly restored. We purified YrpC from the extracts of E. coli JM109/pYRPC2 cells using a Glutathione S-transferase Gene Fusion System to characterize it. YrpC is a monomeric protein and contains no cofactors, like Glr. Enzymological properties of YrpC, such as the substrate specificity and optimum pH, are also similar to those of Glr. The thermostability of YrpC, however, is considerably lower than that of Glr. In addition, YrpC showed higher affinity and lower catalytic efficiency for L-glutamate than Glr. This is the first example showing the occurrence and properties of a glutamate racemase isozyme.  (+info)

BimC motor protein KLP61F cycles between mitotic spindles and fusomes in Drosophila germ cells. (3/434)

KLP61F in Drosophila is a member of the BimC family of kinesins and, as for other family members [1], is required for spindle assembly [2] [3]. KLP61F is a bipolar homotetramer that cross-links spindle microtubules [4]. It is not known, however, whether the function of KLP61F is dedicated to mitosis or whether KLP61F interacts exclusively with microtubules. Previous work suggested that KLP61F functions during interphase in proliferating germ cells [3]. Cytokinesis is incomplete in germ cells and a branched cortical structure known as a fusome extrudes through intercellular bridges called ring canals. Here I show that, in germ cells, KLP61F cycles between spindles during mitosis and fusomes during interphase. Inspection of fusome-deficient hu-li tai shao (hts) mutants indicated that KLP61F gains fusome-dependent interactions near telophase that mediate its incorporation into these structures. KLP61F proved to be maintained in fusomes by microtubule-independent, detergent-resistant interactions. Inspection of KLP61F mutants indicated that KLP61F is required to recruit fusome material to spindle midbodies near telophase and for normal fusome organization. These observations suggest that KLP61F is bifunctional in germ cells, with microtubule-dependent functions in spindle assembly and microtubule-independent functions in fusome organization. Cytological analyses with antibodies against phosphorylated Eg5 peptide [4] suggest that cycling of KLP61F might reflect phosphorylation.  (+info)

Occurrence of free D-amino acids and aspartate racemases in hyperthermophilic archaea. (4/434)

The occurrence of free D-amino acids and aspartate racemases in several hyperthermophilic archaea was investigated. Aspartic acid in all the hyperthermophilic archaea was highly racemized. The ratio of D-aspartic acid to total aspartic acid was in the range of 43.0 to 49.1%. The crude extracts of the hyperthermophiles exhibited aspartate racemase activity at 70 degrees C, and aspartate racemase homologous genes in them were identified by PCR. D-Enantiomers of other amino acids (alanine, leucine, phenylalanine, and lysine) in Thermococcus strains were also detected. Some of them might be by-products of aspartate racemase. It is proven that D-amino acids are produced in some hyperthermophilic archaea, although their function is unknown.  (+info)

Active site titration of gramicidin S synthetase 2: evidence for misactivation and editing in non-ribosomal peptide biosynthesis. (5/434)

The catalytic competence of gramicidin S synthetase 2 (GS2) was determined by following the kinetics of PP(i) generation using active site titration measurements with [gamma-(32)P]ATP. The initial 'burst' of product formation can be correlated to the generation of the aminoacyl adenylate:enzyme complexes at the four amino acid activation domains and the subsequent aminoacylation of carrier domains, followed by a slow linear turnover of substrate due to breakdown of the intermediate. Simultaneous activation of all four amino acid substrates at a saturating concentration displayed a consumption of 8.3 ATP/GS2. In the presence of single amino acids, a binding stoichiometry higher than the anticipated two ATP per active site was obtained, implying misactivation at non-cognate domains. Breakdown of acyladenylate intermediates reflects a possible corrective mechanism by which the enzyme controls the fidelity of product formation.  (+info)

Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains. (6/434)

BACKGROUND: Nonribosomal peptide synthetases (NRPSs) are large modular proteins that selectively bind, activate and condense amino acids in an ordered manner. Substrate recognition and activation occurs by reaction with ATP within the adenylation (A) domain of each module. Recently, the crystal structure of the A domain from the gramicidin synthetase (GrsA) with L-phenylalanine and adenosine monophosphate bound has been determined. RESULTS: Critical residues in all known NRPS A domains have been identified that align with eight binding-pocket residues in the GrsA A domain and define sets of remarkably conserved recognition templates. Phylogenetic relationships among these sets and the likely specificity determinants for polar and nonpolar amino acids were determined in light of extensive published biochemical data for these enzymes. The binding specificity of greater than 80% of the known NRPS A domains has been correlated with more than 30 amino acid substrates. CONCLUSIONS: The analysis presented allows the specificity of A domains of unknown function (e.g. from polymerase chain reaction amplification or genome sequencing) to be predicted. Furthermore, it provides a rational framework for altering of A domain specificity by site-directed mutagenesis, which has significant potential for engineering the biosynthesis of novel natural products.  (+info)

Purification and properties of ornithine racemase from Clostridium sticklandii. (7/434)

Ornithine racemase has been purified to homogeneity from Clostridium sticklandii, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This is the first racemase known to be highly specific to ornithine. This PLP-dependent enzyme has an M(r) of 92, 000, with a K(m) for L-ornithine of 0.77 +/- 0.05 mM and a k(cat) of 980 +/- 20 s(-1).  (+info)

Differences in genotypes of Helicobacter pylori from different human populations. (8/434)

DNA motifs at several informative loci in more than 500 strains of Helicobacter pylori from five continents were studied by PCR and sequencing to gain insights into the evolution of this gastric pathogen. Five types of deletion, insertion, and substitution motifs were found at the right end of the H. pylori cag pathogenicity island. Of the three most common motifs, type I predominated in Spaniards, native Peruvians, and Guatemalan Ladinos (mixed Amerindian-European ancestry) and also in native Africans and U.S. residents; type II predominated among Japanese and Chinese; and type III predominated in Indians from Calcutta. Sequences in the cagA gene and in vacAm1 type alleles of the vacuolating cytotoxin gene (vacA) of strains from native Peruvians were also more like those from Spaniards than those from Asians. These indications of relatedness of Latin American and Spanish strains, despite the closer genetic relatedness of Amerindian and Asian people themselves, lead us to suggest that H. pylori may have been brought to the New World by European conquerors and colonists about 500 years ago. This thinking, in turn, suggests that H. pylori infection might have become widespread in people quite recently in human evolution.  (+info)

*Xylose isomerase

Both share an acid residue Glutamic acid 216 of the enzyme that bridges the two cations. Two basic amino acids surround the ... The isomerase has now been observed in nearly a hundred species of bacteria. Xylose-isomerases are also commonly called ... Other names in common use include D-xylose isomerase, D-xylose ketoisomerase, and D-xylose ketol-isomerase. The activity of D- ... and the xylose isomerase was found to be thermally stable to about 60 degrees Celsius Xylose isomerase has a structure that is ...

*Dermorphin

... appears to be made in these through an unusual posttranslational modification carried out by an amino acid isomerase ... "Posttranslational amino acid epimerization: enzyme-catalyzed isomerization of amino acid residues in peptide chains". Proc. ... This unusual process is needed because the D-alanine in this peptide is not among the 20 amino acids coded for in the genetic ... Dermorphin is not found in humans or other mammals and similar D-amino acid peptides have only been found in bacteria, ...

*Steroid Delta-isomerase

"Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site". ... steroid isomerase, Δ5-ketosteroid isomerase, Δ5(or Δ4)-3-keto steroid isomerase, Δ5-steroid isomerase, 3-oxosteroid isomerase, ... "A Critical Test of the Electrostatic Contribution to Catalysis with Noncanonical Amino Acids in Ketosteroid Isomerase". Journal ... The interface between the two monomers is narrow and well defined, consisting of neutral or apolar amino acids, suggesting the ...

*TPI1

Daar IO, Artymiuk PJ, Phillips DC, Maquat LE (Oct 1986). "Human triose-phosphate isomerase deficiency: a single amino acid ... In each chain, nonpolar amino acids pointing inward from the beta strands contribute to the hydrophobic core of the structure. ... and fatty acid biosynthesis. Triosephosphate isomerase deficiency is a disorder characterized by a shortage of red blood cells ... and each subunit contains 247 amino acids. Each TPI1 monomer contains the full set of catalytic residues, but the enzyme is ...

*Arginine racemase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ...

*Diaminopimelate epimerase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... The lysine/diaminopimelic acid branch of the aspartate pathway produces the essential amino acid lysine via the intermediate ... Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids - lysine, threonine, methionine and isoleucine ... Members of the animal kingdom do not possess this pathway and must therefore acquire these essential amino acids through their ...

*Methionine racemase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... McElroy, W.D. and Glass, H.B. (Eds.), A Symposium on Amino Acid Metabolism, A Symposium on Amino Acid Metabolism, Baltimore, ...

*Aspartate racemase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... phosphate-independent amino acid racemase". J. Biol. Chem. 267 (26): 18361-4. PMID 1526977. Liu L, Iwata K, Kita A, ...

*Alanine racemase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... Normally in PLP reactions an acidic amino acid residue such as a carboxylic acid group, with a pKa of about 5, protonates the ... found no amino acid residues or water molecules, other than the carboxylate group of PLP-Ala, to be close enough (within 4.5A) ... Wood WA (1955). "Amino acid racemases". Methods Enzymol. Methods in Enzymology. 2: 212-217. doi:10.1016/S0076-6879(55)02189-7. ...

*4-hydroxyproline epimerase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ...

*Protein-serine epimerase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... Katayama K, Kuwada M (1995). "Isolation and characterization of a peptide isomerase from funnel web spider venom". J. Biol. ...

*2-aminohexano-6-lactam racemase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... This enzyme is also called alpha-amino-epsilon-caprolactam racemase. Ahmed SA, Esaki N, Tanaka H, Soda K (1984). "L-alpha-Amino ... doi:10.1016/0014-5793(84)81081-9. Ahmed SA, Esaki N, Tanaka H, Soda K (1986). "Mechanism of alpha-amino-epsilon-caprolactam ... thio-epsilon-caprolactam, a new sulfur-containing substrate for alpha-amino-epsilon-caprolactam racemase". FEBS Lett. 174: 76- ...

*Protein domain

... of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid ... Domains vary in length from between about 25 amino acids up to 500 amino acids in length[citation needed]. The shortest domains ... As the procedure does not consider the protein as a continuous chain of amino acids there are no problems in treating ... A key feature of the PTP-C2 superdomain is amino acid residue conservation in the domain interface. Protein folding - the ...

*List of MeSH codes (D08)

... amino acid isomerases MeSH D08.811.399.894.200.200 --- alanine racemase MeSH D08.811.399.894.500 --- carbohydrate epimerases ... amino acid oxidoreductases MeSH D08.811.682.664.500.062 --- alanine dehydrogenase MeSH D08.811.682.664.500.125 --- d-amino-acid ... l-amino acid oxidase MeSH D08.811.682.664.500.724 --- leucine dehydrogenase MeSH D08.811.682.664.500.772 --- nitric oxide ... aromatic-L-amino-acid decarboxylase MeSH D08.811.520.224.125.100.500 --- dopa decarboxylase MeSH D08.811.520.224.125.250 --- ...

*Agatoxin

... contain one or more D-amino acids which are produced from L-amino acids through the action of peptide isomerases. Alpha- ... consisting of 35-37 amino acids and are constrained by four intramolecular disulfide bonds. Omega-agatoxins in turn are ... venom peptide isomerase". Biosci. Biotechnol. Biochem. 62 (6): 1211-5. doi:10.1271/bbb.62.1211. PMID 9692206. Doering CJ, ...

*Peptidylprolyl isomerase A

PPIA is an 18 kDa, 165-amino acid long cytosolic protein. Like other cyclophilins, PPIA forms a β-barrel structure with a ... Peptidylprolyl isomerase A (PPIA), also known as cyclophilin A (CypA) or rotamase A is an enzyme that in humans is encoded by ... As a result, PPIA contributes to viral diseases such as AIDS, hepatitis C, measles, and influenza A. Peptidylprolyl isomerase A ... This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans ...

*Amino acid

Kivirikko KI, Pihlajaniemi T (1998). "Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4- ... Only 837 D-amino acids were found in Swiss-Prot database (187 million amino acids analysed). The 20 amino acids that are ... part of amino acid catabolism (see below). A rare exception to the dominance of α-amino acids in biology is the β-amino acid ... "N-alkylated alpha-amino acid". The α-carboxylic acid group of amino acids is a weak acid, meaning that it releases a hydron ( ...

*Amino acid synthesis

An isomerase then isomerizes α-isopropylmalate to β-isopropylmalate. The third step is the NAD+-dependent oxidation of β- ... Amino acids that must be obtained from the diet are called essential amino acids. Nonessential amino acids are produced in the ... Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced ... Most amino acids are synthesized from α-ketoacids, and later transaminated from another amino acid, usually glutamate. The ...

*Amino-acid racemase

L-amino acid, and one product, D-amino acid. This enzyme belongs to the family of isomerases, specifically those racemases and ... In enzymology, an amino-acid racemase (EC 5.1.1.10) is an enzyme that catalyzes the chemical reaction an L-amino acid ⇌ {\ ... The systematic name of this enzyme class is amino-acid racemase. This enzyme is also called L-amino acid racemase. This enzyme ... Soda K, Osumi T (1969). "Crystalline amino acid racemase with low substrate specificity". Biochem. Biophys. Res. Commun. 35 (3 ...

*Mannose phosphate isomerase

MPI is composed of 440 Amino Acid residues, with one active site and one zinc ion (Zn2+) ligand. Amino acids GLN 111A, HIS 113A ... Mannose-6 phosphate isomerase (MPI), alternately phosphomannose isomerase (PMI) (EC 5.3.1.8) is an enzyme which facilitates the ... Anomeric Form used by Phosphomannose Isomerase and Its 1-Epimerization by Phosphoglucose Isomerase". The Journal of Biological ... "Structural Basis for Phosphomannose Isomerase Activity in Phosphoglucose Isomerase from Pyrobaculum Aerophilum: A Subtle ...

*Glutamate racemase

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... Glaser L (1960). "Glutamic acid racemase from Lactobacillus arabinosus". J. Biol. Chem. 235: 2095-8. PMID 13828348. Molecular ... Nucleic Acids Res. 34 (19): 5567-76. doi:10.1093/nar/gkl704. PMC 1635304 . PMID 17020913. Sengupta S, Nagaraja V (February 2008 ... the bound water molecule that interacts with glutamate amino group) would prevent binding of the substrate; or 4-substituted D- ...

*Branched-chain amino acid aminotransferase

BCATs have been found to interact with protein disulfide isomerases, a class of enzymes that regulate cellular repair and ... Branched-chain amino acids (BCAA) are ubiquitous in many organisms, comprising 35% of all proteins and 40% of the amino acids ... The branched-chain amino acid aminotransferases help to produce compounds like isovaleric acid, isobutyric acid, 2- and 3- ... Branched-chain amino acid aminotransferase (BCAT), also known as branched-chain amino acid transaminase, is an aminotransferase ...

*Enoyl CoA isomerase

... there is little overlap among their amino acid sequences. For example, only 40 out of 302 amino acid sequences (13%) are the ... isomerase, 3,2-trans-enoyl-CoA isomerase, ∆3(cis),∆2(trans)-enoyl-CoA isomerase, or acetylene-allene isomerase, (EC 5.3.3.8) is ... Analysis of Amino Acid Sequence Identities among Families of Acyl: Adenyl Ligases, Enoyl-CoA Hydratases/Isomerases, and Acyl- ... "Amino Acid Sequence Similarities of the Mitochondrial Short Chain delta3,delta2-Enoyl-CoA Isomerase and Peroxisomal ...

*Triosephosphate isomerase

Triose phosphate isomerase is a dimer of identical subunits, each of which is made up of about 250 amino acid residues. The ... but mutants with a different positively charged amino acid retain some function. TIM barrel Triose Phosphate Isomerase ... most include the mutation of glutamic acid at position 104 to aspartic acid. Triose phosphate isomerase is a highly efficient ... Besides the precisely placed glutamate and histidine residues to form the enediol, a ten- or eleven-amino acid chain of TPI ...

*Isopentenyl-diphosphate delta isomerase

IPP isomerase also requires a divalent cation to fold into its active conformation. The enzyme contains several amino acids, ... Isopentenyl pyrophosphate isomerase (IPP isomerase), also known as Isopentenyl-diphosphate delta isomerase, is an isomerase ... The active site of IPP isomerase is deeply buried within the enzyme and consists of a glutamic acid residue and a cysteine ... suggesting that the isomerase may play a role in this disease. "IDI1 - Isopentenyl-diphosphate Delta-isomerase - Saccharomyces ...

*Prostaglandin-endoperoxide synthase 2

... the membrane-binding domain consists of a series of amphipathic α helices with several hydrophobic amino acids exposed to a ... or thromboxane A2 by tissue-specific isomerases.(Figure 2) While metabolizing arachidonic acid primarily to PGG2, COX-2 also ... Arachidonic acid can bind to E-cat and E-allo, but the affinity of AA for E-allo is 25 times that for Ecat. Palmitic acid, an ... However, oxygenation of 10,10-difluoroarachidonic acid to 11-(S )-hydroxyeicosa-5,8,12,14-tetraenoic acid is not consistent ...

*Prolyl isomerase

... although larger proteins can also contain prolyl isomerase domains. Proline is unique among the natural amino acids in having a ... Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but ... Prolyl isomerase (also known as peptidylprolyl isomerase or PPIase) is an enzyme (EC 5.2.1.8) found in both prokaryotes and ... The addition of a potential prolyl isomerase will accelerate this latter reaction phase if it has true prolyl isomerase ...
Gramicidin S or Gramicidin Soviet is an antibiotic that is effective against some gram-positive and gram-negative bacteria as well as some fungi. It is a derivative of gramicidin, produced by the gram-positive bacterium Bacillus brevis. Gramicidin S is a cyclodecapeptide, constructed as two identical pentapeptides joined head to tail, formally written as cyclo(-Val-Orn-Leu-D-Phe-Pro-)2. That is to say, it forms a ring structure composed of five different amino acids, each one used twice within the structure. Another interesting point is that it utilizes two amino acids uncommon in peptides: ornithine as well as the atypical stereoisomer of phenylalanine. It is synthesized by gramicidin S synthetase. Gramicidin S biosynthetic pathway consists of two-enzyme of nonribosomal peptide synthases (NRPSs), gramicidin S synthetase I (GrsA) and gramicidin S synthetase II (GrsB), to give a product as a cyclic decapeptide. Within the biosynthetic pathway, there are total of five modules that specifically ...
It is generally agreed that many proteins are structurally dynamic; sampling many conformations while in solution and also adopting new conformations upon complexation with a ligand. Many of these flexible enzymes are of biological interest, and hindering their function via binding of competitive inhibitors would open up valuable therapeutic avenues. Unfortunately due to the conformation-dependent nature of ligand binding, the act of discovering a new small molecule that will bind these particular proteins is analogous to aiming at a moving target. The following work focuses on one particular enzyme, glutamate racemase. Glutamate racemase is an essential and non-redundant enzyme in all species of bacteria, and inhibition of this enzyme results in cell wall degradation, followed by imminent cell death. Inhibitors of glutamate racemase could act as novel antibiotics against a target to which there are no current antibiotics, and thus no known resistance. My studies focus on three interdependent ...
Lien vers Pubmed [PMID] - 23613764. PLoS ONE 2013;8(4):e60955. Chagas disease is caused by Trypanosoma cruzi, a protozoan transmitted to humans by blood-feeding insects, blood transfusion or congenitally. Previous research led us to discover a parasite proline racemase (TcPRAC) and to establish its validity as a target for the design of new chemotherapies against the disease, including its chronic form. A known inhibitor of proline racemases, 2-pyrrolecarboxylic acid (PYC), is water-insoluble. We synthesized soluble pyrazole derivatives, but they proved weak or inactive TcPRAC inhibitors. TcPRAC catalytic site is too small and constrained when bound to PYC to allow efficient search for new inhibitors by virtual screening. Forty-nine intermediate conformations between the opened enzyme structure and the closed liganded one were built by calculating a transition path with a method we developed. A wider range of chemical compounds could dock in the partially opened intermediate active site models ...
Professor Rudnick is a graduate of Antioch College, where he received a B.S. in Chemistry in 1968. He performed graduate studies in the enzymology of amino acid racemases in the laboratory of Robert H. Abeles in the Graduate Department of Biochemistry at Brandeis University, receiving a Ph.D. in Biochemistry in 1974. His graduate studies led to an understanding of the structure and mechanism of proline racemase that was confirmed by the crystal structure of a homologous protein in 2006. From 1973-1975, Professor Rudnick performed postdoctoral research on lactose permease with H. Ronald Kaback at the Roche Institute of Molecular Biology. This work provided a greater understanding of binding and transport reactions using photoaffinity reagents and substrate analogs. In 1975, he left Roche to become an Assistant Professor in the Department of Pharmacology at Yale, and was promoted to Associate Professor in 1980 and Professor in 1991 ...
Amino Acid Isomerases: Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
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ppiase, cyp37, peptidyl-prolyl, cis-trans, isomerase, cyp37, chloroplastic, PPIase CYP37 | peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic, P82869, ABF57273.1, AS10 1589
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Intracellular pH must be kept close to neutrality to be compatible with cellular functions, but the mechanisms of pH homeostasis and the responses to intracellular acidification are mostly unknown. In the plant Arabidopsis thaliana, we found that intracellular acid stress generated by weak organic acids at normal external pH induces expression of several chaperone genes, including ROF2, which encodes a peptidyl-prolyl cis-trans isomerase of the FK506-binding protein class. Loss of function of ROF2, and especially double mutation of ROF2 and the closely related gene ROF1, results in acid sensitivity. Over-expression of ROF2 confers tolerance to intracellular acidification by increasing proton extrusion from cells. The activation of the plasma membrane proton pump (H+-ATPase) is indirect: over-expression of ROF2 activates K+ uptake, causing depolarization of the plasma membrane, which activates the electrogenic H+ pump. The depolarization of ROF2 over-expressing plants explains their tolerance to ...
Cyclophilin A (CypA) is the main member of the immunophilin superfamily that has peptidyl-prolyl cis-trans isomerase activity. CypA participates in protein folding, cell signaling, inflammation and tumorigenesis. Further, CypA plays critical roles in the replication of several viruses. Upon influenza virus infection, CypA inhibits viral replication by interacting with the M1 protein. In addition, CypA is incorporated into the influenza virus virions. Finally, Cyclosporin A (CsA), the main inhibitor of CypA, inhibits influenza virus replication through CypA-dependent and -independent pathways. This review briefly summarizes recent advances in understanding the roles of CypA during influenza virus infection.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
cytoplasm, nucleus, FK506 binding, peptidyl-prolyl cis-trans isomerase activity, protein dimerization activity, chaperone-mediated protein folding, protein folding
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It is thought to mediate calcineurin inhibition. It also interacts functionally with mature hetero-oligomeric progesterone receptor complexes along with the 90 kDa heat shock protein and P23 protein. This gene has been found to have multiple polyadenylation sites. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Mar 2009 ...
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It is thought to function as an ER chaperone and may also act as a component of membrane cytoskeletal scaffolds. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Sep 2008 ...
PPIases accelerate the folding of proteins. Substrate specificity investigated with Suc-Ala-Xaa-Pro-Phe-4-nitroanilide where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln.
This project is supported by the Canadian Institutes of Health Research (award #111062), Alberta Innovates - Health Solutions, and by The Metabolomics Innovation Centre (TMIC), a nationally-funded research and core facility that supports a wide range of cutting-edge metabolomic studies. TMIC is funded by Genome Alberta, Genome British Columbia, and Genome Canada, a not-for-profit organization that is leading Canadas national genomics strategy with funding from the federal government. Maintenance, support, and commercial licensing is provided by OMx Personal Health Analytics, Inc. Designed by Educe Design & Innovation Inc. ...
Professor Rudnick is a graduate of Antioch College, where he received a B.S. in Chemistry in 1968. He performed graduate studies in the enzymology of amino acid racemases in the laboratory of Robert H. Abeles in the Graduate Department of Biochemistry at Brandeis University, receiving a Ph.D. in Biochemistry in 1974. His graduate studies led to an understanding of the structure and mechanism of proline racemase that was confirmed by the crystal structure of a homologous protein in 2006. From 1973-1975, Professor Rudnick performed postdoctoral research on lactose permease with H. Ronald Kaback at the Roche Institute of Molecular Biology. This work provided a greater understanding of binding and transport reactions using photoaffinity reagents and substrate analogs. In 1975, he left Roche to become an Assistant Professor in the Department of Pharmacology at Yale, and was promoted to Associate Professor in 1980 and Professor in 1991 ...
Accepted name: alanine racemase. Reaction: L-alanine = D-alanine. Other name(s): L-alanine racemase. Systematic name: alanine racemase. Comments: A pyridoxal-phosphate protein.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9024-06-0. References:. 1. Marr, A.G. and Wilson, P.W. The alanine racemase of Brucella abortus. Arch. Biochem. Biophys. 49 (1954) 424-433.. 2. Wood, W.A. Amino acid racemases. Methods Enzymol. 2 (1955) 212-217.. 3. Wood, W.A. and Gunsalus, I.C. D-Alanine formation: a racemase in Streptococcus faecalis. J. Biol. Chem. 190 (1951) 403-416.. ...
PIN1 was recently identified as a peptidyl-prolyl cis-trans isomerase (PPIase). It binds to and isomerizes specific pSer/Thr-Pro motifs and catalytically induces conformational changes after phosphorylation. PIN1 plays an important role in several ce
Cyclophilin antibody for detecting human peptidyl-prolyl cis-trans isomerase A. Validated on up to 12 cell lysates for western blotting. Try a trial size today.
Peptidyl-prolyl Cis-trans Isomerase (cyclophilin); Catalyzes The Cis-trans Isomerization Of Peptide Bonds N-terminal To Proline Residues; Plays A Role In Determining Prion Variants; Binds To Hsp82p And Contributes To Chaperone Activity; Protein Abundance Increases In Response To DNA Replication Stress
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Although the precise molecular composition of the MPTP is currently undergoing investigation, its core components are thought to be the adenine nucleotide translocase (ANT) located in the inner mitochondrial membrane and cyclophilin D, a peptidyl prolyl cis-trans isomerase that interacts with ANT.129 Other components may include VDAC and the peripheral benzodiazepine receptor, which are located in the outer mitochondrial membrane. In healthy mitochondria, the close association of VDAC and ANT create a macromolecular complex that shuttles adenine nucleotides between the ATP-producing matrix and ATP-consuming cytosol. MPTP opening can be triggered under stress conditions, however, by increases in Ca2+, oxidative stress, depletion of adenine nucleotides, increases in inorganic phosphate, and depolarization of the inner mitochondrial membrane, stimuli that operate during ischemia-reperfusion.129 Although proapoptotic (Bax and Bak) and antiapoptotic (Bcl-2 and Bcl-xL) Bcl-2 proteins have been ...
Peptidyl-prolyl isomerases (PPIases) are a well conserved class of enzymes found throughout nature in microorganisms, plants and animals. They are characterized by their ability to catalyze the conversion of cis- and trans- peptidyl-proline bonds in proteins and consequently are able to exert control over target protein structure and function.
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Human FKBP5 qPCR primer pairs, confirmed in positive organizations; screened the primer with high specificity and high sensitivity.
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One of the rate-limiting steps in protein folding has been shown to be the cis-trans isomerization of proline residues, which is catalyzed by a range of peptidylprolyl cis-trans isomerases. To characterize the interaction between model peptides and the periplasmic peptidylprolyl cis-trans isomerase SurA from E. coli, we employed a chemical cross-linking strategy that has been used previously to elucidate the interaction of substrates with other folding catalysts. The interaction between purified SurA and model peptides was significant in that it showed saturation and was abolished by denaturation of SurA; however the interaction was independent of the presence of proline residues in the model peptides. From results obtained by limited proteolysis we conclude that an N-terminal fragment of SurA, comprising 150 amino acids that do not contain the active sites involved in the peptidylprolyl cis-trans isomerization, is essential for the binding of peptides by SurA. This was confirmed by probing the ...
TY - JOUR. T1 - Is cyclophilin involved in the immunosuppressive and nephrotoxic mechanism of action of cyclosporin A?. AU - Sigal, N. H.. AU - Dumont, F.. AU - Durette, P.. AU - Siekierka, John. AU - Peterson, L.. AU - Rich, D. H.. AU - Dunlap, B. E.. AU - Staruch, M. J.. AU - Melino, M. R.. AU - Koprak, S. L.. AU - Williams, D.. AU - Witzel, B.. AU - Pisano, J. M.. PY - 1991/1/1. Y1 - 1991/1/1. N2 - In this report we have approached two questions relating to the mechanism of action of cyclosporin A (CsA). First, we address whether the major cytosolic protein for CsA, cyclophilin, is directly involved in mediating the immunosuppressive activity of this drug, and, in particular, whether inhibition of this proteins peptidyl-prolyl cis-trans isomerase (PPIase) activity results in inhibition of murine T cell activation. Second, we ask whether the nephrotoxicity observed with CsA is related to inhibition of PPIase-dependent pathways in cells other than lymphocytes. Using a series of 61 cyclosporin ...
Staphylococcus aureus is a Gram-positive bacterium causing many kinds of infections from mild respiratory tract infections to life-threatening states as sepsis. It produces many toxins and has a remarkable ability to acquire resistance to antimicrobial drugs. Many S. aureus strains have acquired resistance to commonly used antibiotics and some strains are becoming multi-resistant. Methicillin-resistant strain of Staphylococcus aureus (MRSA) is the principal cause of severe nosocomial infections which can be fatal to compromised patients. Whole genome sequencing of two MRSA strains in 2001 was regarded as a way to find targets for novel antibiotics against infections caused by MRSA [1].. PrsA protein is found ubiquitously in Gram-positive bacteria, including S. aureus [Swiss-Prot:P60747], but not in Gram-negative ones [2, 3]. By sequence homology PrsA contains a parvulin-type peptidyl-prolyl cis-trans isomerase (PPIase) domain and flanking N- and C-terminal domains. PPIases are enzymes that ...
TRCDSEMBL:AE014001_10 gene: "fkpA"; product: "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase)"; Yersinia pestis KIM section 401 of 415 of the complete genome ...
The first data to link PPI function to transcriptional control were those implicating a cyclophilin in the regulation of the cMyb protein. Intramolecular interactions between the N‐terminal DNA‐binding and C‐terminal regulatory domains of cMyb suppress its DNA binding. In vitro studies of this inhibition of DNA‐binding showed it to require the cyclophilin Cyp‐40, and suggested that it involves PPI activity, as inhibition could be blocked by CsA. Provocatively, the oncogenic vMyb protein, which harbours point mutations in its DNA‐binding domain, was not bound by Cyp‐40 and escaped inhibition, lending circumstantial support to the idea that cyclophilins can influence transcriptional events by causing changes in protein conformation (Leverson and Ness, 1998). At least one FKBP has also been linked to transcriptional events. Association of interferon regulatory factor 4 (IRF‐4) with FKBP52 was found to block DNA‐binding and transcriptional activation by the PU.1‐IRF‐4 complex, ...
(2,2-L-Serine)-gramicidin S | C48H84N12O12 | CID 195883 - structure, chemical names, physical and chemical properties, classification, patents, literature, biological activities, safety/hazards/toxicity information, supplier lists, and more.
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Author Summary Cyclophilins are proteins that catalyze the isomerization of prolines, interconverting this structurally important amino acid between cis and trans isomers. Although there are 17 cyclophilins in the human genome, the function of most cyclophilin isoforms is unknown. At least some members of this protein family are of interest for clinically relevant drug design, as they are targets of the drug cyclosporin, which is used as an immunosuppressant to treat patients following organ transplantation. The absence of a comprehensive picture of the similarities and differences between the different members of this protein family precludes effective and specific drug design, however. In the current study we undertake such a global structure∶function analysis. Using biochemical, structural, and computational methods we characterize the human cyclophilin family in detail and suggest that there is a previously overlooked region of these enzymes that contributes significantly to isoform diversity. We
Author Summary Cyclophilins are proteins that catalyze the isomerization of prolines, interconverting this structurally important amino acid between cis and trans isomers. Although there are 17 cyclophilins in the human genome, the function of most cyclophilin isoforms is unknown. At least some members of this protein family are of interest for clinically relevant drug design, as they are targets of the drug cyclosporin, which is used as an immunosuppressant to treat patients following organ transplantation. The absence of a comprehensive picture of the similarities and differences between the different members of this protein family precludes effective and specific drug design, however. In the current study we undertake such a global structure∶function analysis. Using biochemical, structural, and computational methods we characterize the human cyclophilin family in detail and suggest that there is a previously overlooked region of these enzymes that contributes significantly to isoform diversity. We
A variety of transcription factors and protein kinases involved in signal transduction are recovered from cells in heterocomplexes containing the abundant protein chaperone hsp90. Genetic studies in yeast have demonstrated that binding of steroid receptors, the dioxin receptor, and some protein kinases to hsp90 is critical for their signal transducing function in vivo. These heterocomplexes are formed by a multiprotein chaperone machinery consisting of at least four ubiquitous proteins--hsp90, hsp70, p60 and p23. Four high-molecular-weight immunophilins have been discovered as components of steroid receptor or other transcription factor complexes with hsp90. The immunophilins, protein chaperones with prolyl isomerase activity, bind the immunosuppressant drugs FK506 or CyP-40. These immunophilins all bind via tetratricopeptide repeat (TPR) domains to a single TPR binding site on each hsp90 dimer, and multiple heterocomplexes exist for each protein chaperoned by hsp90 according to the immunophilin ...
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A critical role of Cyclophilins, mostly Cyclophilin A (CyPA), in the replication of HCV is supported by a growing body of in vitro and in vivo evidence. CyPA probably interacts directly with nonstructural protein 5A to exert its effect, through its peptidyl-prolyl isomerase activity, on maintaining the proper structure and function of the HCV replicase. The major proline substrates are located in domain II of NS5A, centered around a
Cyclophilin B, 0.1 ml. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Cyclophilin H / PPIH, 0.5 mg. Cyclophilin H (also known as peptidylpropyl isomerase H, PPIH) is a member of peptidyl-propyl cis-trans isomerase (PPIase) family, which catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
A validated positive silencing control targeting the Cyclophilin B (PPIB) gene in human, mouse, or rat cell lines. Useful for determination of optimal RNAi experimental conditions
BioAssay record AID 561638 submitted by ChEMBL: Inhibition of MurI in flaA mutant Helicobacter pylori Hp80.2 overexpressing MurI gene assessed as microbial growth inhibition by CLSI M100-S13 method.
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Prolycopene isomerase, chloroplastic ; Carotene cis-trans-isomerase that converts 7,9,9-tri- cis-neurosporene to 9-cis-neurosporene and 7,9,9,7-tetra-cis- lycopene (also known as prolycopene) into all-trans-lycopene. Isomerization requires redox-active components, suggesting that isomerization is achieved by a reversible redox reaction acting at specific double bonds. Isomerizes adjacent cis-double bonds at C7 and C9 pairwise into the trans-configuration, but is incapable of isomerizing single cis-double bonds at C9 and C9 (615 aa ...
One such discovery cut across the grain of scientific thought of the day. Noelle explains it: "If you took whole blood from the donor prior to [a kidney transplant] and transfused it into the host, it facilitated the longevity of the transplant. That observation is counterintuitive, because one would think that if you immunized the host with blood prior to the transplant, you would facilitate graft rejection. However, the procedure came to be known as donor-specific transfusion (DST), and it was widely used at the time.". Then the powerful immunosuppressive drug cyclosporin was discovered, and the field of organ transplantation was revolutionized. DST was abandoned, and it became one of those oddities of science that was never adequately explained.. Since then, knowledge of immunology has grown exponentially. It is now known, for example, that tens or even hundreds of millions of a bodys cells turn over every day. The body has to have a way of recognizing the new cells as part of "self" so the ...
d-Glutamate cyclase (DGLUCY) is a unique enzyme that reversibly converts free d-glutamate to 5-oxo-d-proline and H2O. Mammalian DGLUCY is highly expressed in the mitochondrial matrix in the heart, and its downregulation disrupts d-glutamate and/or 5-oxo-d-proline levels, contributing to the onset and/or exacerbation of heart failure. However, detailed characterisation of DGLUCY has not yet been pe ...
Conformational Differences of an Immunosuppressant Peptolide in a Single Crystal and in a Crystal Complex with Human Cyclophilin A ...
prw:PsycPRwf_0782 K01775 alanine racemase [EC:5.1.1.1] , (GenBank) alanine racemase (A) MRSASIILDSKALTHNLNCVIDTVPDTTKVLAMVKADAYGHGIAHCLPALKDADGLGVAC FTEAQHIRELGWDKILVLIEGVFSETEWQQSIEAQCQSIIHHQDQVQWALNHLPPENSPC RTVWLKLNTGMNRLGFESDELGDVAQSLVDAGYELILTSHFANADAPNHPSNAKQIDTFT QALQQLREQVDPSIKASLCNSAGILNFKACHFDWVRPGIMLYGSSPVEGVSAQMLKLKPV MSFKASLMAIHNIAAGTSVGYGSRFVANRPIVKGIVSIGYGDGYPRVVDGSAWVSVQLAG EHSSYKCPVIGRVAMDMIAIDLTDVPNPKVGSQVMLWGDPELGAPSVDEIAESAHTLGYE LLCRVTQRPLREVL ...
kdi:Krodi_1313 K01775 alanine racemase [EC:5.1.1.1] , (GenBank) alanine racemase (A) MAITRLEIDLAALRHNYSYLRKKVAPSVKMMAVVKAFGYGSDAGAVAQELEMLGVDYFAV AYVSEGIALRDAGITTPILVLHPQPDTFDELIERCLEPSIYSIRMMELFTAFAKGKGQEN YPIHLKFNTGLNRLGFLNTDVSWILDRLRENVSVKVASLFSHLVASEDPAEEEFTLNQIL QFTNISKELLQALDYVPFMHMTNTSGVINYHRAHFDCVRIGIGLYGYGNSKEDTKKLKPV ARLKSVISQIHHIKPGQSIGYNRAYKATEEIVTATLPIGHADGISRSLGNGVGYVMIAGQ KAPIVGNVCMDMLMVDITGISCKEGDDVEVFGETTSAETLAGEMQSISYELLTAIGQRVK RVILR ...
Human FKBP6 full-length ORF ( AAH36817.1, 1 a.a. - 327 a.a.) recombinant protein with GST-tag at N-terminal. (H00008468-P02) - Products - Abnova
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FK 1012: consists of two FK-506 covalently bonded molecules; can bind two immunophilins at the same time thereby starting a part of the signal cascade that avtivates T-cells
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ウサギ・ポリクローナル抗体 ab3562 交差種: Ms,Rat,Rb,Chk,Cow,Hu,NHuPrm 適用: WB,IP,IHC-P,IHC-Fr,ICC,Flow Cyt,ICC/IF…Cyclophilin…
Little is known about the nature of post mortem degradation of proteins and peptides on a global level, the so-called degradome. This is especially true for nonneural tissues. Degradome properties in relation to sampling procedures on different tissues are of great importance for the studies of, for instance, post translational modifications and/or the establishment of clinical biobanks. Here, snap freezing of fresh(, 2 min post mortem time) mouse liver and pancreas tissue is compared with rapid heat stabilization with regard to effects on the proteome (using two-dimensional differential in-gel electrophoresis) and peptidome (using label free liquid chromatography). We report several proteins and peptides that exhibit heightened degradation sensitivity, for instance superoxide dismutase in liver, and peptidyl-prolyl cis-trans isomerase and insulin C-peptides in pancreas. Tissue sampling based on snap freezing produces a greater amount of degradation products and lower levels of endogenous ...
Native DadB and Alr alanine racemases (M/sub r/ 39,000) from Salmonella typhimurium are proteolyzed at homologous positions by ..cap alpha..-chymotrypsin, trypsin, and subtilisin to generate in all cases two nonoverlapping polypeptides of M/sub r/ 28,000 and 11,000. Under nondenaturing conditions, chymotryptic digest results in an associated form of the two fragments which possesses 3% of the original catalytic activity, incorporates 0.76 equiv of the mechanism-based inactivator ..beta..-chloro-(/sup 14/C)-D-alanine, and exhibits a UV circular dichroism profile identical with that of native enzyme. Protein sequence analysis of the denatured chymotryptic fragments indicates the presence of a tetrapeptide interdomain hinge (DadB, residues 254-257; Alr, residues 256-259) that is attacked at both ends during proteolysis. Under the previously employed digest conditions, NaB/sup 3/H/sub 4/-reduced DadB holoenzyme is resistant to ..cap alpha..-chymotrypsin and trypsin and is labile only toward ...
Autori: Bogdan Bancia Editorial: 2009.. Rezumat:. The three-dimensional structure determination of proteins represents an important step towards understanding their biological function and thus their roles in living organisms. Using a combination of multidimensional NMR techniques three different biomolecules were analyzed in the present study, E. coli peptidyl - prolyl cis-trans isomerase PpiB, proinsulin connecting peptide and DnaG-C. 15N-HSQC spectra were recorded of PpiB which had been expressed without further purification in a cell-free expression system with amino acid selective isotope labelling. Comparison of spectra before and after ultrafiltration indicated that labelled metabolic by-products are of low molecular weight. Therefore, the labelled protein signals are easily distinguished from those of metabolites. The structure analysis of the proinsulin connecting peptide included the assignment of 1H, 13C and 15N NMR resonances using 2D NMR, measurement of T1 (1H) relaxation times and ...
Looking for online definition of Cis-trans isomerism in the Medical Dictionary? Cis-trans isomerism explanation free. What is Cis-trans isomerism? Meaning of Cis-trans isomerism medical term. What does Cis-trans isomerism mean?
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PPIL1 antibody [N1C3] (peptidylprolyl isomerase (cyclophilin)-like 1) for ICC/IF, WB. Anti-PPIL1 pAb (GTX118126) is tested in Human samples. 100% Ab-Assurance.
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The trigger factor is an abundant soluble protein of Escherichia coli with a Mr of 48 kDa. It was discovered originally by Wickner and co‐workers in 1987 when they searched for cytosolic components which are involved in the export of secretory proteins (Crooke and Wickner, 1987; Lill et al., 1988). They found that the trigger factor interacted with the export‐competent form of a precursor protein, proOmpA, and that it bound to the large subunit of the ribosome (Crooke et al., 1988).. Recently, the trigger factor was rediscovered by three groups, which used different experimental approaches to investigate early processes in cellular protein maturation. The groups of Bukau (Hesterkamp et al., 1996) and Luirink (Valent et al., 1995) incorporated photoactivatable chemical crosslinkers into nascent proteins and, after arresting translation, searched for proteins which possibly bind to and are crosslinked with these newly formed protein chains, while they are still associated with the ribosome. ...
Cyclophilin (Cyp) A has been reported to be overexpressed in the majority of cancer cells, including hepatocellular carcinoma (HCC). However, the biological functions of CypA in HCC are far from being understood. To determine the biological functions of CypA in HCC, the present study screened human fetal liver complementary DNA for proteins interacting with CypA using the yeast two-hybrid system. A nuclear protein, serine/arginine-rich (SR)-25, was isolated as a novel CypA-binding protein that is distinct from those previously described in the literature. Binding assays and co-immunoprecipitation confirmed the physical association between CypA and SR-25. The present study demonstrated that CypA may interact with SR-25 through its peptidyl-prolyl isomerase domain. In addition, CypA may induce the expression of SR-25 in Hep3B cells. The messenger RNA levels of CypA and SR-25 in HCC indicated that there was a significant correlation between the expression of CypA and the expression of SR-25 in HCC. It can
NOVEL RNAi THERAPEUTIC FOR TREATMENT OF HEPATITIS C INFECTION - Small interfering RNAs (siRNAs) or small hairpin RNA (shRNAs) and compositions comprising same are provided that specifically target human cyclophilin A (CyPA) to effectively inhibit Hepatitis C(HCV) infection in a cell. Such siRNA and shRNAs may have a length of from about 19 to about 29 contiguous nucleotides corresponding to a specific region of human cyclophilin A (CyPA) cDNA of from about nucleotide 155 to about nucleotide 183 having particular potency against CyPA and HCV. Such siRNA and shRNAs may be formulated as naked compositions or as pharmaceutical compositions. DNA polynucleotides, plasmids, and viral or non-viral vectors are also provided that encode siRNA or shRNA molecules, which may be delivered directly to cells or in combination with known delivery agents, such as lipids, polymers, encapsulated lipid particles, such as liposomes. Methods for treating, managing inhibiting, preventing, etc., HCV infection using such ...
Isomerases são ENZIMAS que realizam reações de interconversão entre isômeros óticos ou geométricos - Epimerases. A determinação do nome das enzimas é normatizada por um comitê especializado , o Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). EC5.1 - Racemases e epimerases EC5.2 - Isomerases cis-trans EC5.3 - Oxirredutases intramoleculares EC5.4 - Transferases intramoleculares EC5.5 - Liases intramoleculares EC5.99 - Outras isomerases Enzimas do grupo EC.5 (em inglês ...
Spectrophotometric determination of the ionophore compounds and mass spectrometry of the biosynthesis products revealed that the cells of Streptomyces chrysomallus subsp. macrotetrolidi during the lag phase permanently contained practically constant though insignificant (about 20 to 40 nmol/mg of protein) amounts of biosynthetic precursors of macrotetrolides, oligomers of nactinic acids. The oligomers of nactinic acids had antibiotic activity and in an amount of 2.5 micrograms/ml inhibited the growth of Bacillus mycoides. The oligomers of nactinic acids had ionophore properties and were highly labile with respect to inorganic cations. The presence of sodium in the extragent stabilized the calcium monomer, a trimer of nonactinic acid, and promoted washing off the substances of the nactinic nature from the cells. The cations of ammonia and possibly potassium stabilized the dimer and tetramer of nonactinic acid forming a more hydrophobic complex by comparison with the initial compounds.
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Polyclonal antibody for Cyclophilin B/PPIB detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. Cyclophilin B/PPIB information: Molecular Weight: 23743 MW; Subcellular Localization: Endoplasmic reticulum lumen. Me
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Rabbit monoclonal antibody raised against a human FKBP8 peptide using ARM Technology. A synthetic peptide of human FKBP8 is used for rabbit immunization.Customer or Abnova will decide on the preferred peptide sequence. (H00023770-K) - Products - Abnova
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Calcineurin B兔多克隆抗体(ab94535)可与人样本反应并经WB实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
The physiological roles of immunophilins are unclear, but many possess peptidyl-prolyl isomerase (PPIase) activity, and they have been found in all organisms examined to date, implying that they are involved in fundamental, protein-folding processes. The chloroplast thylakoid lumen of the higher plant Arabidopsis thaliana contains up to 16 immunophilins (five cyclophilins and 11 FKBPs), but only two of them, AtCYP20-2 and AtFKBP13, have been found to be active PPIases, indicating that the other immunophilins in this cellular compartment may have lost their putative PPIase activities. To assess this possibility, we characterized two independent Arabidopsis knockout lines lacking AtCYP20-2 in enzymological and quantitative proteomic analyses. The PPIase activity in thylakoid lumen preparations of both mutants was equal to that of corresponding wild-type preparations, and comparative two-dimensional difference gel electrophoresis analyses of the lumenal proteins of the mutants and wild type showed ...
Looking for online definition of peptidylprolyl isomerase D in the Medical Dictionary? peptidylprolyl isomerase D explanation free. What is peptidylprolyl isomerase D? Meaning of peptidylprolyl isomerase D medical term. What does peptidylprolyl isomerase D mean?
You are viewing an interactive 3D depiction of the molecule n-[4-({[(6r)-2-amino-5-methyl-4-oxo-3,4,5,6,7,8-hexahydro-6-pteridinyl]methyl}amino)benzoyl]-d-glutamic acid (C20H26N7O6+) from the PQR.
Active site of A. baumannii alanine racemase. (a) 2Fo− Fc electron-density map of the active site contoured at 1.0σ with isomesh map shown (1.6 Å carve).
The SCOP classification for the Alanine racemase C-terminal domain-like superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
Sigma-Aldrich offers Sigma-C7696, Cyclophilin A from calf thymus for your research needs. Find product specific information including CAS, MSDS, protocols and references.
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Detail záznamu - Inhibition of Human Serine Racemase, an Emerging Target for Medicinal Chemistry - Detail záznamu - Knihovna Akademie věd České republiky
Sigma-Aldrich offers abstracts and full-text articles by [J Marsolier, M Perichon, J D DeBarry, B O Villoutreix, J Chluba, T Lopez, C Garrido, X Z Zhou, K P Lu, L Fritsch, S Ait-Si-Ali, M Mhadhbi, S Medjkane, J B Weitzman].
FKBP52小鼠单克隆抗体[Hi52C](ab59460)可与小鼠, 大鼠, 仓鼠, 狗, 人样本反应并经WB, IP, IHC, Flow Cyt, ICC/IF实验严格验证。所有产品均提供质保服务,中国75%以上现货。
Recombinant Peptidylprolyl Isomerase B (Cyclophilin B) (PPIB) Peptide. Species: Human. Source: Escherichia coli (E. coli). Order product ABIN934947.
Numerous mechanisms have been suggested for how bacterial toxins kill susceptible mammalian cells. Several recent studies demonstrated the importance of mitochondrial targeting of toxins produced by H. pylori, C. difficile, and S. aureus to mitochondria (56). In these cases toxin-mediated cell death was caspase independent and did not result in typical PTPs in the MOM (14, 18).. Previously, we reported that M. haemolytica LKT induces apoptosis of BL-3 cells in a caspase-9-dependent manner and that in mitochondria isolated from LKT-intoxicated BL-3 cells there was gross damage to the MOM (4). Based on these observations, we hypothesized that LKT is transported into the cell and binds directly to mitochondria. In the present study, we first demonstrated that full-length LKT protein could be identified in purified mitochondrial lysates from LKT-treated BL-3 cells (Fig. 1A). Transfection of anti-LKT antibodies into BL-3 cells prevented binding of LKT to mitochondria. Confocal microscopy and flow ...
Accepted name: (S)-2-methylmalate dehydratase. Reaction: (S)-2-methylmalate = 2-methylfumarate + H2O. Other name(s): mesaconate hydratase; (+)-citramalate hydro-lyase; L-citramalate hydrolase; citramalate dehydratase; (+)-citramalic hydro-lyase; mesaconate mesaconase; mesaconase; (S)-2-methylmalate hydro-lyase. Systematic name: (S)-2-methylmalate hydro-lyase (2-methylfumarate-forming). Comments: Also hydrates fumarate to (S)-malate.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9027-94-5. References:. 1. Blair, A.H. and Barker, H.A. Assay and purification of (+)-citramalate hydro-lyase components from Clostridium tetanomorphum. J. Biol. Chem. 241 (1966) 400-408. [PMID: 5903732]. 2. Wang, C.C. and Barker, H.A. Purification and properties of L-citramalate hydrolyase. J. Biol. Chem. 244 (1969) 2516-2526. [PMID: 5769987]. ...
Gramicidin S, a membrane-active antibiotic, was crystallized from solvent containing water, methanol, trifluoroacetic acid and hydrochloric acid. The structure was refined at 0.95 Å resolution and contains 1.5 molecules of gramicidin S, two trifluoracetic acid molecules and ten water molecules in the crystallographic asymmetric unit. In the crystals, the gramicidin S molecules line up into helical channels that differ from those observed previously ...
Looking for Bacillus brevis? Find out information about Bacillus brevis. any rod-shaped bacterium or, more particularly, a rod-shaped bacterium of the genus Bacillus. Some bacterium in the genus cause disease, for example B.... Explanation of Bacillus brevis
An anti-Brucella vaccine candidate which comprises of purified Brucella lipopolysaccharide and cocktail of four Salmonella Typhimurium (ST)-Brucella vectors was reported earlier. Each vector constitutively express highly conserved Brucella antigens (rB), viz. lumazine synthase (BLS), proline racemase subunit A (PrpA), outer membrane protein-19 (Omp19), and Cu-Zn superoxide dismutase (SOD). The present study determined relative level of protection conferred by each single strain. Upon virulent challenge, the challenge strain was recovered most abundantly in non-immunized control mice and the ST-Omp19, ST-BLS, LPS, and ST-SOD immunized mice groups showed much less burden. Indirect ELISA based assay also confirmed the induction of antigen specific IgG for each antigen delivered. In route-wise comparison of the combined vaccine candidate, intraperitoneal (IP), intramuscular (IM), and subcutaneous (SC) immunizations revealed an indication of highly efficient routes for the protection. Splenocytes of ...
Background Proline racemase (PRAC) enzymes of Trypanosoma cruzi (TcPRAC), the agent of Chagas disease, and Trypanosoma vivax (TvPRAC), the agent of livestock trypanosomosis, have been implicated in the B-cells polyclonal activation contributing to immunosuppression and the evasion of host defences. The similarity to prokaryotic PRAC and the absence in Trypanosoma brucei andTrypanosoma congolense have raised many questions about the origin, evolution, and functions of trypanosome PRAC (TryPRAC) enzymes. Findings We identified TryPRAC homologs as single copy genes per haploid genome in 12 of 15Trypanosoma species, including T. cruzi and T. cruzi marinkellei, T. dionisii, T. erneyi, T. rangeli, T. conorhini and T. lewisi, all parasites of mammals. Polymorphisms in TcPRAC genes matched T. cruzi genotypes: TcI-TcIV and Tcbat have unique genes, while the hybrids TcV and TcVI containTcPRACA and TcPRACB from parental TcII and TcIII, respectively. PRAC homologs were identified in trypanosomes from anurans,

Recombinant Human Triosephosphate isomerase protein (ab88134)Recombinant Human Triosephosphate isomerase protein (ab88134)

Buy our Recombinant Human Triosephosphate isomerase protein. Ab88134 is a full length protein produced in Saccharomyces ... Amino Acid Sequence. * Species. Human. * Sequence. MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPP TAY ... Recombinant Human Triosephosphate isomerase protein. See all Triosephosphate isomerase proteins and peptides. ... Triosephosphate isomerase (TIM) catalyses the reversible interconversion of G3P and DHAP. Only G3P can be used in glycolysis, ...
more infohttp://www.abcam.com/recombinant-human-triosephosphate-isomerase-protein-ab88134.html

Fungal protein disulfide isomerase - Patent # 6346244 - PatentGeniusFungal protein disulfide isomerase - Patent # 6346244 - PatentGenius

... encoded by a nucleic acid sequence which hybridizes with (i) the DNA sequence of SEQ ID NO:1 or (ii) the DNA sequence of SEQ ID ... The present invention also relates to DNA sequences encoding the protein disulfide isomerases, compositions comprising said ... protein disulfide isomerases and methods of use thereof. ... The present invention relates to protein disulfide isomerases ... C.for 30 minutes; and (b) has an amino acid sequence that is at least 80% homologous to the amino acid sequence of SEQ ID NO:3. ...
more infohttp://www.patentgenius.com/patent/6346244.html

PPIase CYP37 | peptidyl-prolyl cis-trans isomerase CYP37, chlorPPIase CYP37 | peptidyl-prolyl cis-trans isomerase CYP37, chlor

... peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic, P82869, ABF57273.1, AS10 1589 ... Synthetic peptide (amino acids 277 - 290) specific for chloroplast cyclophilin from Arabidopsis thaliana (At3g15520) (P82869). ... Home / Plant/Algal antibodies / Photosynthesis / Proteases / PPIase CYP37 , peptidyl-prolyl cis-trans isomerase CYP37, chlor ... AS10 1595 , Anti-PPIase CYP37 , peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic, large pack size. AS10 1607 , Anti- ...
more infohttp://www.agrisera.com/en/artiklar/plantalgal-cell-biology/photosynthesis-/proteases/ppiase-cyp37-peptidyl-prolyl-cis-trans-isomerase-cyp37-chloroplastic-.html

Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id...Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id...

From results obtained by limited proteolysis we conclude that an N-terminal fragment of SurA, comprising 150 amino acids that ... Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id ... To characterize the interaction between model peptides and the periplasmic peptidylprolyl cis-trans isomerase SurA from E. coli ... Hence we propose that, similar to protein disulfide isomerase and other folding catalysts, SurA exhibits a modular architecture ...
more infohttps://kar.kent.ac.uk/45/

The intriguing Cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding | BMC...The intriguing Cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding | BMC...

Synthetic Vpr1-20(A), Vpr21-40 (B), Vpr25-40 (C), Vpr1-40(D) and synthetic mutants carrying Pro to Asn exchanges at amino acid ... To confirm that CypA interacts with Pro-35 of s Vpr21-40 and Pro-35 of s Vpr25-40 as a prolyl cis/trans isomerase, an excess of ... The 96 amino acid virion-associated multifunctional viral protein R (Vpr) [1, 2] is encoded by primate lentiviruses, the human ... each comprising four residues containing only one Pro residue preceded by a variety of different amino acids, Harrison and ...
more infohttps://bmcstructbiol.biomedcentral.com/articles/10.1186/1472-6807-10-31

Characterization of the redox state of human cyclophilin-D and its interactions with peroxiredoxin 5

 | DIAL.pr - BOREALCharacterization of the redox state of human cyclophilin-D and its interactions with peroxiredoxin 5 | DIAL.pr - BOREAL

We showed that the 16 first amino acid of the presequence are necessary and sufficient to form a functional presequence and to ... eng] Cyclophilin-D (CyP-D) is a peptidyl prolyl cis/trans isomerase located in the mitochondrial matrix of mammalian cells. The ...
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Amino Acid Isomerases
     Summary Report | CureHunterAmino Acid Isomerases Summary Report | CureHunter

Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1. ... Amino Acid Racemases; Acid Isomerases, Amino; Acid Racemases, Amino; Isomerases, Amino Acid; Racemases, Amino Acid ... Amino Acid Isomerases. Subscribe to New Research on Amino Acid Isomerases Enzymes that catalyze either the racemization or ... Isomerases: 29*Racemases and Epimerases: 4*Amino Acid Isomerases*Alanine Racemase: 10 ...
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Plant triose phosphate isomerase isozymes : purification, immunological and structural characterization, and partial amino Acid...Plant triose phosphate isomerase isozymes : purification, immunological and structural characterization, and partial amino Acid...

Partial amino acid sequences from the N-terminus were also obtained for both lettuce TPIs. Nine of the 13 positions sequenced ... The overall similarity of the two isozymes and the high similarity of their partial amino acid sequences to those of several ... The two isozymes, purified from lettuce, had closely similar amino acid compositions with the exception of methionine which was ... in the two proteins had identical amino acid residues. The partial sequences of the plant proteins showed high similarity to ...
more infohttps://www.semanticscholar.org/paper/Plant-triose-phosphate-isomerase-isozymes-%3A-and-and-Pichersky-Gottlieb/988b811b3890bd93757144ff90c79106fa9d8afb

Post-duplication charge evolution of phosphoglucose isomerases in teleost fishes through weak selection on many amino acid...Post-duplication charge evolution of phosphoglucose isomerases in teleost fishes through weak selection on many amino acid...

The difference in net protein charge was attributable not to specific amino acid sites but to the sum of various amino acid ... but rather was driven by weak selection on a large number of amino acid sites and consequently by steady directional and/or ... which can detect only strong selection for amino acid substitutions involved in adaptive molecular evolution. In this study, we ... finding suggests that the surface charge evolution of PGI proteins was not driven by strong selection on individual amino acid ...
more infohttps://bmcevolbiol.biomedcentral.com/articles/10.1186/1471-2148-7-204

Emeritus Professor Philip Kuchel - The University of SydneyEmeritus Professor Philip Kuchel - The University of Sydney

Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom. Amino Acids, 32(1), 63-68. [More ... Characterization and isolation of L-to-D-amino-acid-residue isomerase from Platypus venom. Amino Acids, 32(1), 63-68. [More ... Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom. Amino Acids, 32(1), 63-68. [More ... Characterization and isolation of L-to-D-amino-acid-residue isomerase from Platypus venom. Amino Acids, 32(1), 63-68. [More ...
more infohttps://sydney.edu.au/science/people/philip.kuchel.php

Professor Katherine Belov - The University of SydneyProfessor Katherine Belov - The University of Sydney

Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom. Amino Acids, 32(1), 63-68. [More ... Characterization and isolation of L-to-D-amino-acid-residue isomerase from Platypus venom. Amino Acids, 32(1), 63-68. [More ... Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom. Amino Acids, 32(1), 63-68. [More ... Characterization and isolation of L-to-D-amino-acid-residue isomerase from Platypus venom. Amino Acids, 32(1), 63-68. [More ...
more infohttp://sydney.edu.au/science/people/kathy.belov.php

Allosteric inhibitors of Helicobacter pylori glutamate  | Open-iAllosteric inhibitors of Helicobacter pylori glutamate | Open-i

Amino Acid Isomerases/antagonists & inhibitors*/chemistry/genetics/metabolism. *Bacteria/chemistry/drug effects/enzymology*/ ... Amino Acid Isomerases/antagonists & inhibitors*/chemistry/genetics/metabolism. *Bacteria/chemistry/drug effects/enzymology*/ ... Bottom Line: Glutamate racemase, a member of the cofactor-independent, two-thiol-based family of amino acid racemases, has been ... Bottom Line: Glutamate racemase, a member of the cofactor-independent, two-thiol-based family of amino acid racemases, has been ...
more infohttps://openi.nlm.nih.gov/detailedresult.php?img=PMC3815242_mbt0001-0345-f5&req=4

Plus itPlus it

... it has some amino acid homology with yeast sterol isomerases ( 4). The σ1 receptors are transmembrane proteins that are ... is adjacent to one of the amino acid residues (D172) found to be obligatory for ligand binding ( 11). However, other amino ... Also shown are amino acid residues known to be obligatory for σ1 receptor drug binding and the splice sites of a non-drug ... B, σ1 receptor amino acid sequence contains several CBD motifs of the structure L/V-X1-5-Y-X1-5-K/R. The sequences VEYGR ( ...
more infohttp://cancerres.aacrjournals.org/content/67/23/11166

Publications by Lynne Elizabeth Maquat, Ph.D. -  University of Rochester Medical CenterPublications by Lynne Elizabeth Maquat, Ph.D. - University of Rochester Medical Center

"Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme." Proceedings of ... "Nucleotide sequence of murine triosephosphate isomerase cDNA." Nucleic acids research.. 1990 Jul 25; 18(14):4261. ... "Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man." The ... "A beta zero-thalassemic beta-globin RNA that is labile in bone marrow cells is relatively stable in HeLa cells." Nucleic acids ...
more infohttps://www.urmc.rochester.edu/people/23074170-lynne-elizabeth-maquat/publications

Search Results -   - 41 Results - Digital LibrarySearch Results - - 41 Results - Digital Library

Computational Identification of Amino-Acid Mutations that Further Improve the Activity of a Chalcone-Flavonone Isomerase from ... beneficial amino-acid mutations that further improve the intramolecular-cyclization activity of a chalcone-flavonone isomerase ... signals and details the recently discovered role of lysine catabolite pipecolic acid (Pip) in defense amplification and priming ...
more infohttps://digital.library.unt.edu/search/?sort=title&src=ark&q3=&searchType=advanced&t3=untl_agent&fq=str_month:02_feb&fq=untl_institution:UNTCAS&fq=str_degree_department:Biological%20Sciences

SCOPe 2.07: Structural Classification of Proteins - extendedSCOPe 2.07: Structural Classification of Proteins - extended

Keywords: Rossmann fold, Branched-chain amino acid biosynthesis, Knotted protein, NADPH, Isomerase, OXIDOREDUCTASE. Deposited ... Compound: Putative ketol-acid reductoisomerase (Os05g0573700 protein). Species: Oryza sativa Japonica Group [TaxId:39947]. Gene ... Compound: Putative ketol-acid reductoisomerase (Os05g0573700 protein). Species: Oryza sativa Japonica Group [TaxId:39947]. Gene ...
more infohttp://scop.berkeley.edu/pdb/code=3fr8

Heidi J Imker - Research Output
     - University of Illinois at Urbana-ChampaignHeidi J Imker - Research Output - University of Illinois at Urbana-Champaign

Prediction and assignment of function for a divergent N-succinyl amino acid racemase. Song, L., Kalyanaraman, C., Fedorov, A. A ... The Pseudomonas aeruginosa antimetabolite L -2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two ...
more infohttps://experts.illinois.edu/en/persons/heidi-j-imker/publications/

SWISS-MODEL Template Library | 4tve.1SWISS-MODEL Template Library | 4tve.1

Biran, S. et al., The eps1p protein disulfide isomerase conserves classic thioredoxin superfamily amino Acid motifs but not ...
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Search Articles | University of Toronto LibrariesSearch Articles | University of Toronto Libraries

amino acid isomerases - antagonists & inhibitors (66) 66 Filter by. Remove filter. carrier proteins - antagonists & inhibitors ... AMINO-ACID-SEQUENCE , CIS-TRANS-ISOMERASE , LEGIONELLA-PNEUMOPHILA-MIP , MICROBIOLOGY , INDEPENDENT CHAPERONE FUNCTION , ... nima-interacting peptidylprolyl isomerase - metabolism (24) 24 Filter by. Remove filter. peptidylprolyl isomerase - physiology ... peptidylprolyl isomerase - antagonists & inhibitors (200) 200 Filter by. Remove filter. peptidylprolyl isomerase - metabolism ( ...
more infohttps://query.library.utoronto.ca/index.php/search/q?kw=SubjectTerms:Peptidylprolyl%20Isomerase%20-%20antagonists%20&%20inhibitors

Arthritogenic T cell epitope in glucose-6-phosphate isomerase-induced arthritis | Arthritis Research & Therapy | Full TextArthritogenic T cell epitope in glucose-6-phosphate isomerase-induced arthritis | Arthritis Research & Therapy | Full Text

We selected 32 types of peptides as core sequences from the human GPI 558 amino acid sequence, which binds the binding motif, ... from DBA/1 mice was identified from the amino acid sequence of T cell epitopes and candidate peptides of T cell epitopes in GPI ... Arthritis induced by immunisation with glucose-6-phosphate isomerase (GPI) in DBA/1 mice was proven to be T helper (Th) 17 ... has 13/15 amino acids homology to mGPI325-339 (IWYINCYGCETHALL) while hGPI544-558 (GLINFIKQQREARVQ) has only 9/15 amino acids ...
more infohttps://arthritis-research.biomedcentral.com/articles/10.1186/ar2545

Dermorphin - WikipediaDermorphin - Wikipedia

Dermorphin appears to be made in these through an unusual posttranslational modification carried out by an amino acid isomerase ... "Posttranslational amino acid epimerization: enzyme-catalyzed isomerization of amino acid residues in peptide chains". Proc. ... This unusual process is needed because the D-alanine in this peptide is not among the 20 amino acids coded for in the genetic ... Dermorphin is not found in humans or other mammals and similar D-amino acid peptides have only been found in bacteria, ...
more infohttps://en.wikipedia.org/wiki/Dermorphin

Gstz1 - Maleylacetoacetate isomerase - Rattus norvegicus (Rat) - Gstz1 gene & proteinGstz1 - Maleylacetoacetate isomerase - Rattus norvegicus (Rat) - Gstz1 gene & protein

Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. ... 3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with t-butyl and cumene ... Probable bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2- ... Maleylacetoacetate isomeraseAdd BLAST. 216. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ...
more infohttp://www.uniprot.org/uniprot/P57113

Autosomal Recessive Congenital Ichthyosis - GeneReviews® - NCBI BookshelfAutosomal Recessive Congenital Ichthyosis - GeneReviews® - NCBI Bookshelf

Normal gene product. The protein product of ALOXE3, hydroperoxide isomerase ALOXE3 (eLOX-3), has 711 amino acid residues. Both ... has 701 amino acid residues and catalyzes the conversion of arachidonic acid to 12R-hydroxyeicosatetraenoic acid (12R-HETE). ... The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones ... Normal gene product. The ABCA12 cDNA encodes a protein of 2,595 amino acids that belongs to a subfamily of ATP-binding cassette ...
more infohttps://www.ncbi.nlm.nih.gov/books/NBK1420/
  • NMR data at atomic resolution indicate prolyl cis / trans isomerisation of the highly conserved proline residues Pro-5, -10, -14 and -35 of Vpr are catalyzed by human CypA and require only very low concentrations of the isomerase relative to that of the peptide substrates. (biomedcentral.com)
  • Arthritis induced by immunisation with glucose-6-phosphate isomerase (GPI) in DBA/1 mice was proven to be T helper (Th) 17 dependent. (biomedcentral.com)
  • In addition, the amino acids arginine , cysteine , glycine , glutamine , histidine , proline , serine , and tyrosine are considered conditionally essential , meaning they are not normally required in the diet but must be supplied exogenously to specific populations that do not synthesize it in adequate amounts. (wikipedia.org)
  • This unusual process is needed because the D-alanine in this peptide is not among the 20 amino acids coded for in the genetic code and thus the peptide cannot be synthesized in the usual way from the encodings in the genome of an organism. (wikipedia.org)
  • Most amino acids are synthesized from α- ketoacids , and later transaminated from another amino acid, usually glutamate . (wikipedia.org)
  • The α-ketoglutarate family of amino acid synthesis (synthesis of glutamate, glutamine, proline and arginine) begins with α-ketoglutarate, an intermediate in the Citric Acid Cycle. (wikipedia.org)
  • The regulation of the synthesis of glutamate from α-ketoglutarate is subject to regulatory control of the Citric Acid Cycle as well as mass action dependent on the concentrations of reactants involved due to the reversible nature of the transamination and glutamate dehydrogenase reactions. (wikipedia.org)
  • 6 , 7 PDI family thiol isomerases have an active site motif Cys-X-X-Cys (CXXC) where X is any amino acid. (bloodjournal.org)
  • Duplication and evolution of the thioredoxin-like fold 8 resulted in multidomain thiol isomerases of the PDI family that contain both catalytic domains (termed a, a′, or a 0 by convention), which contain the CXXC motif, and substrate-binding domains (termed b or b′ by convention). (bloodjournal.org)
  • Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. (uniprot.org)
  • In E. coli citrate synthase, the enzyme involved in the condensation reaction initiating the Citric Acid Cycle is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP. (wikipedia.org)
  • The interface between the two monomers is narrow and well defined, consisting of neutral or apolar amino acids, suggesting the hydrophobic interaction is important for dimerization. (wikipedia.org)
  • In addition, the loss of AIM1 alters the fatty acid composition of the mature adult plant. (plantcell.org)
  • Despite our rudimentary understanding of the mechanisms by which thiol isomerases control vascular function, the clinical utility of targeting them in thrombotic disorders is already being explored in clinical trials. (bloodjournal.org)
  • This is one of the initial regulations of the α-ketoglutarate family of amino acid synthesis. (wikipedia.org)
  • This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. (wikipedia.org)
  • All thiol isomerases, of which now there are 21 in the PDI family, have evolved from an ancestral thioredoxin found in primitive unicellular organisms. (bloodjournal.org)
  • Probable bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1, 3-diazole and maleylacetoacetate isomerase activity. (uniprot.org)