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)

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 ...
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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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 ...
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.
Nigeria ihanganye nibibazo bitoroshye byumutekano aho abantu barenga 13000 bishwe kuva aho umutwe wa Boko Haram ufatiye intwaro muri 2009.. Mbere yamatora yumukuru wigihugu ateganijwe kuwa 28 zukwezi kwa gatatu, BBC irabanyuriramo muri make uko umutekano wifashe muri icyo gihugu.. ...
Active Recombinant human FKBP12 protein is an Escherichia coli Full length protein, | 95% purity, | 1.000 Eu/µg endotoxin level and validated in FuncS, SDS-PAGE. Specific activity is | 300 nmoles/min…
Buy our Recombinant Human FKBP12 protein. Ab56524 is a full length protein produced in Escherichia coli and has been validated in WB, SDS-PAGE. Abcam provides…
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 - Mitochondria. T2 - FKBP38 and mitochondrial degradation. AU - Shirane, Michiko. AU - Nakayama, Keiichi. PY - 2014/1/1. Y1 - 2014/1/1. N2 - FK506-binding protein 38 (FKBP38) is a membrane chaperone that is localized predominantly to mitochondria and contains a COOH-terminal tail anchor. FKBP38 also harbors an FKBP domain that confers peptidyl-prolyl cis-trans isomerase activity, but it differs from other FKBP family members in that this activity is dependent on the binding of Ca2+-calmodulin. FKBP38 inhibits apoptosis by recruiting the anti-apoptotic proteins Bcl-2 and Bcl-xL to mitochondria. Mice deficient in FKBP38 die soon after birth manifesting a defect in neural tube closure that results in part from unrestrained apoptosis. We recently found that FKBP38 and Bcl-2 translocate from mitochondria to the endoplasmic reticulum during mitophagy, a form of autophagy responsible for the elimination of damaged mitochondria. FKBP38 and Bcl-2 thus escape the degradative fate of most ...
Monoclonal antibody to Trigger Factor (TF) molecular chaperone can be used for western blotting or immunoprecipitation of TF-tagged recombinant proteins
Monoclonal antibody to Trigger Factor (TF) molecular chaperone can be used for western blotting or immunoprecipitation of TF-tagged recombinant proteins
Escherichia coli synthesizes at least three [NiFe]-hydrogenase enzymes that catalyze the production or consumption of hydrogen gas and occupy a central place in cellular energy metabolism (4, 17). Multiple accessory proteins are required for the assembly of the bimetallic catalytic cluster of these enzymes, including the proteins encoded by the hyp genes and slyD (3, 7, 12). SlyD, which contributes to the insertion of nickel into the hydrogenase precursor proteins and cellular nickel accumulation (18), consists of a peptidyl-prolyl isomerase (PPIase) domain as well as a molecular chaperone domain and a C-terminal tail rich in metal-binding residues (10, 14, 15). A combination of in vitro and in vivo experiments demonstrated that both the metal-binding domain and the chaperone activity of SlyD are essential components of its function in hydrogenase production (13), but the role of SlyDs PPIase activity in the hydrogenase maturation pathway was unknown.. The crystal structure of Methanococcus ...
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 ...
A database search of the ASK1 sequence outside its kinase domain showed that a short amino acid sequence in the NH2-terminal part contains a motif for an FK506-binding protein (FKBP)-type peptidyl-prolyl cis-trans isomerase, of which the functional importance is unknown (Fig. 1A). The kinase domain of ASK1 has sequence similarity with members of the MAPKKK family including MEKK1 (30.0%) in mammal and SSK2 (32.3%) and STE11 (30.4%) in Saccharomyces cerevisiae. Phylogenetic comparison suggested that ASK1 is distantly related to RAF-1, KSR1, TAK1, and TPL-2 mammalian MAPKKKs but most closely related to the SSK2 or SSK22 family of yeast MAPKKKs, which are upstream regulators of yeast HOG1 MAPK (13).. Despite differences in the overall structures of ASK1 and SSK2 or SSK22 (13), it was of interest to examine whether ASK1 might act as a functional kinase in yeast and thereby complement the loss of SSK2 or SSK22. We used yeast strain TM257-H1 (ssk2Δ ssk22Δ sho1Δ) (13, 14), which grows in a normal YPD ...
1ID8: The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12).
(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.
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.
Knijnenburg AD, Tuin AW, Spalburg E, de Neeling AJ, Mars-Groenendijk RH, Noort D, Otero JM, Llamas-Saiz AL, van Raaij MJ, van der Marel GA, Overkleeft HS, Overhand ...
Tudey, uar wurld os follid woth fuud. Wholi sumi eri hielthy, ot siims loki tiinegirs eri muri fucasid un thi anhielthy fuuds. Yis, thiri eri ethlitoc prugrems; tiins eri stoll nut ietong thi roght fuuds thiy shuald bi. Thiy git thi sompli, iesy tu dipind un, luw cust fuuds whoch must lokily eri frum fest fuud ristearents. Tiinegirs uftin pock thi iesy chuoci, whoch os why thi ubisoty reti os rosong on uar steti, oncladong hiert ettecks end doebitis. Evin thuagh ot siims loki thi anhielthy chuocis eri muri dipindint whin yuari on e rash end niid e qaock boti tu iet, nut cerong ebuat thi natrotoun, tiinegirs dunt rielozi thet ot woll effict thim on thi lung ran, lotirelly ...
The Biodesign Institute at ASU addresses todays critical global challenges in healthcare, sustainability and security. Arizona State University, Tempe, AZ.
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 ...
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.
This family of proteins contain a 70 amino acid consensus sequence known as the J domain. The J domain of DnaJ interacts with ... This domain has disulphide isomerase activity.[8] The function of the C-terminal is chaperone and dimerization. ... which contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc ...
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 ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ...
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. ...
... 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, ...
... 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 ...
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- ...
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 ...
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, ...
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, ...
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. ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ...
Sternberg, M. J.; Thornton, J. M. (1978). "Prediction of protein structure from amino acid sequence". Nature. 271 (5640): 15-20 ... "An analysis of the structure of triose phosphate isomerase and its comparison with lactate dehydrogenase". Journal of Molecular ... a novel powerful method to predict the phenotypic effects of Single-nucleotide polymorphisms and other amino acid variants. ... Enhanced prediction of single amino acid variant (SAV) phenotype using network features". Journal of Molecular Biology. 426 (14 ...
One stream involves the shikimate pathway to produce the amino acid phenylalanine, (see phenylpropanoids) ... The chalcone is subsequently isomerized by the enzyme chalcone isomerase to the prototype pigment naringenin, ... UGT84A2 encodes sinapic acid: UDP-glucosyltransferase.[58] Genetic analysis[edit]. The phenolic metabolic pathways and enzymes ... may result from increased uric acid levels derived from the metabolism of the flavonoids in the food.[46] It is possible that ...
Proline is the only amino acid known to exist in both the cis and trans isomerization rate in vivo, and is often the rate- ... Peptidyl-prolyl cis-trans isomerase B is an enzyme that is encoded by the PPIB gene. As a member of the peptidyl-prolyl cis- ... PPIB is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of ... "Entrez Gene: PPIB peptidylprolyl isomerase B (cyclophilin B)". Ray P, Rialon-Guevara KL, Veras E, Sullenger BA, White RR (May ...
... though not in amino acid sequence. FKBPs have been identified in many eukaryotes from yeast to humans and function as protein ... FKBP, or FK506 binding protein, is a family of proteins that have prolyl isomerase activity and are related to the cyclophilins ... This therapeutic role is not related to prolyl isomerase activity. FKBP (FKBP1A) does not normally form a dimer but will ... "A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from ...
... 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, ...
The phenylpropanoid pathway begins from the amino acid phenylalanine, and an intermediate of the pathway, naringenin, is ... type II chalcone isomerase, and isoflavone synthase. Plants use isoflavones and their derivatives as phytoalexin compounds to ...
An isomerase converts 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 amino acids are produced. The ... Commercial syntheses of amino acids[edit]. The commercial production of amino acids usually relies on mutant bacteria that ...
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- ...
Its role in maintaining the balance of these aromatic amino acids in the cell is vital. This is the single known example of a ... This enzyme belongs to the family of isomerases, specifically those intramolecular transferases that transfer functional groups ... conversion of chorismate to prephenate is the first committed step in the pathway to the production of the aromatic amino acids ...
... isopropylmalate isomerase, isopropylmalate dehydrogenase, and aminotransferase - are necessary for the formation of leucine ... A branched-chain amino acid (BCAA) is an amino acid having an aliphatic side-chain with a branch (a central carbon atom bound ... Wikimedia Commons has media related to Branched-chain amino acids.. *Branched-chain+amino+acids at the US National Library of ... of the essential amino acids in muscle proteins and 40% of the preformed amino acids required by mammals.[2] Synthesis for ...
All the proteins have from 209 to 241 amino acid residues. The enzyme has a TIM barrel structure. The systematic name of this ... Phosphopentose Isomerase Phosphoribulose Kinase Pentose Phosphate Pathway TIM barrel RPE (human gene encoding Ribulose- ... However, amino acids positioned at the dimer interface - which are involved in many intermolecular interactions - are not ... The two aspartic acids mentioned above act as proton donors and acceptors. Asp37 and Asp175 are both hydrogen bonded to the ...
... 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 --- ...
The FAH gene is thought to be involved in the catabolism of the amino acid phenylalanine in human. The FAH gene is located on ... maleylacetoacetate isomerase (GSTZ1), fumarylacetoacetase (FAH) The protein has a number of conserved co-factor binding sites ... part of the overall biochemical process of amino acid degradation. Other proteins that are involved in the phenylalanine ... Nucleic Acids Res. 18 (7): 1887. doi:10.1093/nar/18.7.1887. PMC 330610 . PMID 2336361. "Entrez Gene: FAH fumarylacetoacetate ...
Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is ...
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, ...
... 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- ...
Their proteins have an N-terminal signal peptide consisting of 15-30 amino acids which are cleaved upon entry into the ... 35. Kaiser BK, Yim D, Chow IT, Gonzalez S, Dai Z, Mann HH, Strong RK, Groh V, Spies T. Disulphide-isomerase-enabled shedding of ... Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis. Mol Cells. 2007; 24:261-67. [PubMed] ... Protein disulfide isomerase (PDI) family consists of twenty-one members sharing a common structure (the TRX-like domain). ...
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 ...
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 ...
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 ...
... interconverting this structurally important amino acid between cis and trans isomers. Although there are 17 cyclophilins in the ...
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 ...
... J ... It has been proposed for ketosteroid isomerase and other enzymes that active site hydrogen bonding groups provide energetic ... It has also been proposed that the ketosteroid isomerase and other enzyme active sites provide electrostatic environments that ... To test these models, we substituted tyrosine with fluorotyrosines (F-Tyrs) in the ketosteroid isomerase (KSI) oxyanion hole ...
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 ...
Peptidyl-prolyl cis-trans isomerase HAdd BLAST. 176. Amino acid modifications. Feature key. Position(s). DescriptionActions. ... section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the ... The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, ... Peptidyl-prolyl cis-trans isomerase H (EC:5.2.1.8*Search proteins in UniProtKB for this EC number. ...
Protein disulfide-isomeraseAdd BLAST. 490. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ... p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. ... p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. ... p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. ...
... polypeptide chain containing 216 amino acids (21-236) and having a molecular mass of 23.5 kDa. ... Disulfide-Bond Isomerase Recombinant produced in E.Coli is a single, non-glycosylated, ... Disulfide-Bond Isomerase Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 216 amino ... Amino acid sequence. DDAAIQQTLA KMGIKSSDIQ PAPVAGMKTV LTNSGVLYIT DDGKHIIQGP MYDVSGTAPVNVTNKMLLKQ LNALEKEMIV YKAPQEKHVI ...
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 ...
245 amino acids (complete) Source: UniProtKB. Domains and repeats. None predicted. Structural features and predictions. * no ... Structures: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (B4RU63) ...
The removal of 41 N-terminal amino acids did not exhibit a significant effect on the enzyme activity however, the ... isomerase from hyperthermophilic achaeon thermococcus kodakaraensis implicates the necessity of its N-terminal amino acid ... Truncated type II isopentenyl diphosphate isomerase from hyperthermophilic achaeon thermoc Truncated type II isopentenyl ... The enzyme isopentenyl diphosphate isomerase [IDI, EC 5.3.3.2] interconverts isopentenyl diphosphate and dimethylallyl ...
Characterization of purified hP5 indicated that it has both isomerase and chaperone activities, but both activities are lower ... Amino Acid Motifs * Base Sequence * Citrate (si)-Synthase / metabolism * DNA Primers * Electrophoresis, Polyacrylamide Gel ... Functional analysis of human P5, a protein disulfide isomerase homologue J Biochem. 2002 Sep;132(3):451-5. doi: 10.1093/ ... Mutation of two thioredoxin-related motifs in hP5 revealed that the first motif is more important than the second for isomerase ...
Positional proteomics analysis identifies the cleavage of human peptidylprolyl isomerase H (PPIH; cyclophilin H) at amino acid ... PPIH peptidylprolyl isomerase H [Homo sapiens] PPIH peptidylprolyl isomerase H [Homo sapiens]. Gene ID:10465 ... peptidylprolyl isomerase Hprovided by HGNC. Primary source. HGNC:HGNC:14651 See related. Ensembl:ENSG00000171960 MIM:606095 ... Nucleic Acids Res, 2003 Aug 15. PMID 12907720, Free PMC Article * Crystal structure of the human U4/U6 small nuclear ...
... that were shown to provide xylose isomerase activity in yeast cells. The xylose isomerase activity can complete a xylose ... In one embodiment a heterologous nucleic acid molecule encoding a polypeptide having xylose isomerase activity and amino acid ... b) introducing a heterologous nucleic acid molecule encoding a polypeptide having xylose isomerase activity and amino acid ... nucleic acid molecule for encoding xylose isomerase and xylose isomerase encoded by the nucleic acid molecule ...
Modification of allosteric disulfide bonds by thiol isomerases is akin to cleavage of amino acid bonds by serine proteases of ... 7 PDI family thiol isomerases have an active site motif Cys-X-X-Cys (CXXC) where X is any amino acid. Duplication and evolution ... Depending on the context, thiol isomerases function as reductases, oxidases, or isomerases (Figure 3). Thiol isomerases can act ... Vascular thiol isomerases. A subset of thiol isomerases is found in the vasculature (Table 1)36,37 and some of these, including ...
Isomerases;. Racemases and epimerases;. Acting on amino acids and derivatives. Sysname. nocardicin-C epimerase. ... It catalyses the epimerization of the amino group at position 9 from (S)- configuration to (R)-. The enzyme can act on both ...
Isomerases;. Racemases and epimerases;. Acting on amino acids and derivatives. Sysname. penicillin-N 5-amino-5-carboxypentanoyl ... Epimerization at C-5 of the 5-amino-5-carboxypentanoyl group to form penicillin N is required to make a substrate for EC 1.14. ...
... isomerase; (ACIAC_1.PE1013). Keywords: Amino-acid biosynthesis; Complete proteome; Cytoplasm; Keywords: Histidine biosynthesis ... Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Keywords: Complete proteome; Isoleucine biosynthesis; ... ACIAC_1_PE1004 RecName: Full=Histidinol dehydrogenase; Short=HDH; EC=1.1.1 23; (ACIAC_1.PE1004). Keywords: Amino-acid ... Amino-acid biosynthesis; Complete proteome; Cytoplasm; Keywords: Histidine biosynthesis; Lyase. Organism: ACIDOVORAX CITRULLI ...
The EtPDIL cDNA contained 1129 nucleotides encoding 216 amino acids. The deduced EtPDIL protein belonged to thioredoxin-like ... Protein disulfide isomerase (PDI) and PDI-like proteins are members of the thioredoxin superfamily. They contain thioredoxin- ... Molecular characterization and analysis of a novel protein disulfide isomerase-like protein of Eimeria tenella.. [Hongyu Han, ...
An isomerase converts 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 amino acids are produced. The ... Commercial syntheses of amino acids[edit]. The commercial production of amino acids usually relies on mutant bacteria that ...
  • [eng] Cyclophilin-D (CyP-D) is a peptidyl prolyl cis/trans isomerase located in the mitochondrial matrix of mammalian cells. (uclouvain.be)
  • Their proteins have an N-terminal signal peptide consisting of 15-30 amino acids which are cleaved upon entry into the endoplasmic reticulum [ 10 ]. (aging-us.com)
  • 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)
  • 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. (kent.ac.uk)
  • Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. (kent.ac.uk)
  • 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. (kent.ac.uk)
  • 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. (kent.ac.uk)
  • 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 article discusses a computational approach that combines multiple sequence alignment, positive selection detection, and molecular docking to identify and design beneficial amino-acid mutations that further improve the intramolecular-cyclization activity of a chalcone-flavonone isomerase from Glycine max (GmCHI). (unt.edu)
  • Since thioredoxin motif mutants lacking isomerase activity retain chaperone activity with the substrate citrate synthase, the isomerase and chaperone activities of hP5 are probably independent, as was shown for PDI. (nih.gov)
  • In this study, we employed a comparative evolutionary approach to this question, focusing on differences in the structural properties of a protein, specifically the electric charge, encoded by fish-specific duplicated phosphoglucose isomerase ( Pgi ) genes. (biomedcentral.com)
  • In microbes, examples include 2-aminoisobutyric acid and lanthionine , which is a sulfide-bridged alanine dimer. (wikidoc.org)
  • In this study, we investigate the role of peptidyl-prolyl cis/trans isomerases (PPIases) on the activity of the S. aureus secreted virulence factor nuclease (Nuc). (asm.org)
  • As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to regulate many biological processes, including intracellular signaling, transcription, inflammation, and apoptosis. (wikipedia.org)
  • peptidylprolyl cis/trans isomerase, NIMA-in. (broadinstitute.org)
  • A homologue of the human site-specific prolyl cis/trans isomerase PIN1 was identified in Arabidopsis thaliana. (ugent.be)
  • We show by two-dimensional NMR spectroscopy that the PIN1At is a prolyl cis/trans isomerase with specificity for phosphoserine-proline bonds. (ugent.be)
  • Nonetheless, how a subfunctionalized protein can evolve into a more adaptive protein is poorly understood, mainly due to the limitations of current analytical methods, which can detect only strong selection for amino acid substitutions involved in adaptive molecular evolution. (biomedcentral.com)
  • Nonetheless, how a more adaptive or specialized protein property evolves after subfunctionalization is poorly understood, mainly due to the limited resolution power of current analytical methods, which seek to detect positive selection on individual amino acid substitutions involved in adaptive molecular evolution. (biomedcentral.com)
  • Although most of the activities of vascular thiol isomerases that contribute to thrombus formation are yet to be defined at the molecular level, allosteric disulfide bonds that are modified by thiol isomerases have been described in substrates such as αIIbβ3, α v β3, GPIbα, tissue factor, and thrombospondin. (bloodjournal.org)
  • However, these studies do not address the specific tissues and molecular mechanisms involved in amino acid stimulation of egg development. (pnas.org)
  • In biochemistry, amino acids having both the amine and the carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance. (wikipedia.org)
  • Amino acids are molecules which contain both a carboxylic acid and an amine group. (wikibooks.org)
  • In amino acid, the carboxyl group is more acidic than the carboxylic acid. (wikibooks.org)
  • An amino acid is in a zwitterionic state when the carboxylic acid group is deprotonated and the amino group is protonated, simultaneously. (wikibooks.org)
  • In solid state, the amine functionality deprotonates the carboxylic acid group, giving rise to the zwitterionic, dipolar entity. (wikibooks.org)
  • While in plants, 1-Aminocyclopropane-1-carboxylic acid is a small disubstituted cyclic amino acid that is a key intermediate in the production of the plant hormone ethylene . (wikidoc.org)
  • In contrast, for all other naturally occurring amino acids, steric hindrance between side chains precludes the cis form and overwhelmingly favors the trans form ( 2 ). (asm.org)
  • About 500 naturally occurring amino acids are known (though only 20 appear in the genetic code) and can be classified in many ways. (wikipedia.org)
  • The other product of transamidation is a keto acid that enters the citric acid cycle. (wikidoc.org)
  • Of the basic set of twenty amino acids (not counting selenocysteine ), humans cannot synthesize eight. (wikipedia.org)
  • These twenty amino acids are biosynthesized from other molecules, but organisms differ in which ones they can synthesize and which ones must be provided in their diet. (wikidoc.org)
  • Iodinated and brominated tyrosine are also amino acids found in species, but are not included in the 20 major amino acids because of their rarity: iodinated tyrosin is only found in thyroid hormones, and brominated tyrosine is only found in coral. (wikibooks.org)
  • A number of amino acids are essential for oogenesis and a steady infusion of a balanced mixture of amino acids into the hemolymph can stimulate egg development in a variety of mosquito species ( 9 ). (pnas.org)
  • Certain species of lactic acid bacteria produce and secrete bacteriocins, which are ribosomally synthesized antimicrobial peptides. (uio.no)
  • Manchenko, G. 2009-08-25 00:00:00 The isozyme patterns of glucose-6-phosphate isomerase (GPI) have been analyzed in ten species of polychaetes of the genera Polydora and Dipolydora (Polychaeta: Spionidae). (deepdyve.com)
  • This protein, which ranges in size from 232 to 251 amino acids, depending on the Legionella species ( 31 ), is an outer membrane protein important in the intracellular cycle of Legionella . (asm.org)
  • l-Arabinose isomerase (l-AI) catalyzes the isomerization of l-arabinose to l-ribulose and d-galactose to d-tagatose. (semanticscholar.org)
  • RPE65, which catalyzes isomerization of all- trans retinyl fatty acid esters to 11- cis -retinol (11 c ROL) in the visual cycle, controls the rhodopsin regeneration rate and photoreceptor susceptibility to light-induced degeneration. (jneurosci.org)