Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
Enzymes that catalyze the interconversion of aldose and ketose compounds.
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.
Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.
An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
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.
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.
Enzymes that catalyze the transposition of double bond(s) in a steroid molecule. EC 5.3.3.
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.
A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-
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.
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.
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.
A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
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.
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.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A 17-KDa cytoplasmic PEPTIDYLPROLYL ISOMERASE involved in immunoregulation. It is a member of the cyclophilin family of proteins that binds to CYCLOSPORINE.
The hydroxy salt of ammonium ion. It is formed when AMMONIA reacts with water molecules in solution.
The rate dynamics in chemical or physical systems.
Enzymes that catalyze the transposition of a sulfur-sulfur bond. EC 5.3.4.
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.
Cellular proteins and protein complexes that transport amino acids across biological membranes.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
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).
Proteins prepared by recombinant DNA technology.
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.
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.
A class of carbohydrates that contains five carbon atoms.
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.
Proteins found in any species of bacterium.
Transport proteins that carry specific substances in the blood or across cell membranes.
The functional hereditary units of BACTERIA.
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.
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.
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.
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.
The sum of the weight of all the atoms in a molecule.
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.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
Amino acids containing an aromatic side chain.
The relationships of groups of organisms as reflected by their genetic makeup.
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 which have a branched carbon chain.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
An essential branched-chain amino acid important for hemoglobin formation.
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.
A disaccharide consisting of two glucose units in an alpha (1-6) glycosidic linkage.
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.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
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.
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).
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.
Methods and techniques used to genetically modify cells' biosynthetic product output and develop conditions for growing the cells as BIOREACTORS.
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.
Established cell cultures that have the potential to propagate indefinitely.
A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.
Proteins obtained from ESCHERICHIA COLI.
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 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.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
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
PTM-dependent Induction (Phosphorylation of T329 on Alpha-globin transcription factor CP2 (Tcfcp2)) of the Alpha-globin transcription factor CP2 (Tcfcp2) DOC_WW_Pin1_4 motif - Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) WW domain ...
PTM-dependent Induction (Phosphorylation of S213 on Mothers against decapentaplegic homolog 3 (SMAD3)) of the Mothers against decapentaplegic homolog 3 (SMAD3) DOC_WW_Pin1_4 motif - Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) WW domain ...
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 ...
TY - JOUR. T1 - The immunosuppressive and toxic effects of FK-506 are mechanistically related. T2 - Pharmacology of a novel antagonist of FK-506 and rapamycin. AU - Dumont, Francis J.. AU - Staruch, Mary Jo. AU - Koprak, Samuel L.. AU - Siekierka, John J.. AU - Lin, C. Shirley. AU - Harrison, Richard. AU - Sewell, Tonya. AU - Kindt, Victoria M.. AU - Beattie, Thomas R.. AU - Wyvratt, Matthew. AU - Sigal, Nolan H.. PY - 1992/9/1. Y1 - 1992/9/1. N2 - FK-506 inhibits Ca2+-dependent transcription of lymphokine genes in T cells, and thereby acts as a powerful immunosuppressant. However, its potential therapeutic applications may be seriously limited by several side effects, including nephrotoxicity and neurotoxicity. At present, it is unclear whether these immunosuppressive and toxic effects result from interference with rehted biochemical processes. FK-506 is known to interact with FK-binding protein-12 (FKBP-12), an abundant cytosolic protein with cis.trans peptidyl-prolyl isomerase activity ...
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.
SWISS-MODEL Repository entry for A1T7U8 (DAPF_MYCVP), Diaminopimelate epimerase. Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / NRRL B-24157 /PYR-1) (Mycobacterium vanbaalenii)
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.
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
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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 ...
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).
Dr. Muganga yize muri Kaminuza ya Havard no mu ya Alberta muri Canada ari naho yakuye Impamyabumenyi yIkirenga.. Inzego zumutekano zimushinja ibyaha birimo ubugambanyi, ariko abasanzwe bakurikirana politiki ya Uganda, bakemeza ko itabwa muri yombi rye rifitanye isano nibikorwa amazemo iminsi byo gushaka ko izina ryubwoko bwe bwa Banyarwanda rihinduka, rikaba Abavandimwe.. Uyu mwarimu afite inkomoko mu Rwanda nubwo yavukiye muri Uganda. Umuryango we wari warahungiye muri Uganda mu myaka ya 1950 aba ari naho avukira.. Uyu mugabo yari aherutse gutangiza ubukangurambaga bwo guhindura izina ryubwoko bwabo. Icyo gihe yavuze ko impamvu ari uko kwitwa Abanyarwanda bituma dufatwa nkabanyamahanga, tukimwa ibyangombwa birimo indangamuntu, ndetse no kugira ngo abana bacu binjire mu nzego zumutekano bikaba bitoroshye.. Bivugwa ko Dr. Muganga yari umuntu ufitanye imikoranire nabantu barwanya ubutegetsi bwu Rwanda aho yabaga muri Canada.. ...
(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.
The structurally unrelated drugs cyclosporin A (CsA) and FK-506 are powerful immunosuppressants, used prophylactically following transplant surgery to prev
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 ...
Finalmente se conocieron las causas del fallecimiento de Carrie Fisher, la actriz conocida por interpretar a la princesa Leia en la saga Star Wars ...
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.
z roke dečkove je božji volek odletel pa na polja pisani je cvetki obsedel. čuri muri, božji volek, tam je domek tvoj, zdaj pa zleti in pokaži, kje je domek moj! poletel je božji volek k soncu pod nebo, dolgo je za njim strmelo dečkovo oko. ...
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 ...
... of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid ... TIM barrels contain 200-250 amino acid residues, folded into 8 α-helices and 8 β-strands. The β-strands are arranged into a ... A deep mutational scanning approach and a competition assay was used to determine the fitness of all possible amino acid ... TIM barrels contain two distinct buried regions, where amino acid residues are completely enveloped by their neighbors and lack ...
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 ... 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 ... 1955). A Symposium on Amino Acid Metabolism, A Symposium on Amino Acid Metabolism. Baltimore. pp. 616-634. Biology portal v t e ...
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 ...
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 ... In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. 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 ...
... in presence of amino acids, the maillard reaction. In addition, various organic acids can be biotechnologically produced from ... Glucose can also be converted from bacterial xylose isomerase to fructose. In addition, glucose metabolites produce all ... nonessential amino acids, sugar alcohols such as mannitol and sorbitol, fatty acids, cholesterol and nucleic acids. Finally, ... Gluconeogenesis allows the organism to build up glucose from other metabolites, including lactate or certain amino acids, while ...
Similar to aspartic acid, the amino acid proline has the rare property of being able to occupy both cis and trans isomers of ... Peptidyl-prolyl isomerase, or PPIase, is an enzyme very commonly associated with proline isomerization due to their ability to ... As an amino acid, proline is present in many proteins. This aids in the multitude of effects that isomerization of proline can ... The specific amino acid that precedes the prolyl peptide bond also can have an effect on which conformation the bond assumes. ...
... a novel powerful method to predict the phenotypic effects of Single-nucleotide polymorphisms and other amino acid variants. ... "An analysis of the structure of triose phosphate isomerase and its comparison with lactate dehydrogenase". Journal of Molecular ... "Prediction of protein structure from amino acid sequence". Nature. 271 (5640): 15-20. Bibcode:1978Natur.271...15S. doi:10.1038/ ... Enhanced prediction of single amino acid variant (SAV) phenotype using network features". Journal of Molecular Biology. 426 (14 ...
... contain one or more D-amino acids which are produced from L-amino acids through the action of peptide isomerases. Alpha- ... The ω‎-agatoxins are approximately 100 amino acids in length and are antagonists of voltage-sensitive calcium channels and also ... 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, ...
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. Biology ... 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- ...
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 ... Overview of all the structural information available in the PDB for UniProt: P23284 (Peptidyl-prolyl cis-trans isomerase B) at ...
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 ...
... that catalyze the interconversion between the cis and trans isomers of peptide bonds containing the amino acid proline (Pro). ... FKBP-12 and cyclophilins both share common peptide-prolyl isomerase activity. While the majority of the Peptide bonds within ... Immunophilins, with their prolyl isomerase activity, thus function as protein-folding chaperones. FKBP12 FKBP4 (FKBP52) FKBP5 ( ... In molecular biology, immunophilins are endogenous cytosolic peptidyl-prolyl isomerases (PPI) ...
The mammalian σ1 receptor is an integral membrane protein with 223 amino acids. It shows no homology to other mammalian ... which is a C 8-C7 sterol isomerase in the ergosterol biosynthetic pathway. Hydropathy analysis of the σ1 receptor indicates ... and sterol Δ8-Δ7 isomerase sites". Journal of Medicinal Chemistry. 46 (11): 2117-24. doi:10.1021/jm021014d. PMID 12747784. ...
... protein disulfide isomerases, natriuretic peptides, hyaluronidases, phospholipases, L-amino acid oxidase (LAAO), vascular ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and ... The systematic name of this enzyme class is penicillin N 5-amino-5-carboxypentanoyl-epimerase. This enzyme participates in ...
... amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH D08.811.399.894.500 - carbohydrate epimerases MeSH ... 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 synthase ... aromatic-L-amino-acid decarboxylase MeSH D08.811.520.224.125.100.500 - dopa decarboxylase MeSH D08.811.520.224.125.250 - ...
D-aspartate This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids ... one face of the amino acid while another protonated base concertedly donates its hydrogen onto the other face of the amino acid ... Amino acid racemization is carried out by two dominant mechanisms: one-base mechanisms and two-base mechanisms. In one-base ... D-amino acids are common within the peptidoglycan of bacteria. In Bifidobacterium bifidum, D-aspartate is formed from L- ...
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 aspartic acids are the acid/base catalysts. Lastly, once the ligand is attached to the active site, a series of methionines ...
Par17, which carries a 25 residue N-terminal extension, shares the complete successive amino acid sequence with Par14. In ... Par17, a member of the parvulin family of peptidyl-prolyl-cis/trans-isomerases (PPIases), is an isoform of parvulin 14 (Par14) ... "Parvulin 17 Promotes Microtubule Assembly by Its Peptidyl-Prolyl Cis/Trans Isomerase Activity". Journal of Molecular Biology. ...
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 ...
... though not in amino acid sequence. FKBPs have been identified in many eukaryotes, ranging from yeast to humans, and function as ... 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 ... "Gene group: FKBP prolyl isomerases (FKBP)". HUGO Gene Nomenclature Committee. "Symbol report for FKBP1C". HUGO Gene ...
... 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 ...
Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is ...
Branched-chain amino acid aminotransferase. *Alanine-glyoxylate transaminase *AGXT. 2.6.3: Oximinotransferases. * ...
... encodes a 51.2 kDa protein that is composed of 474 amino acids; 124 peptides have been observed through mass spectrometry ... fatty acid metabolic process. • metabolism. • cardiolipin acyl-chain remodeling. • fatty acid beta-oxidation. ... transferase activity, transferring acyl groups other than amino-acyl groups. • enoyl-CoA hydratase activity. • long-chain-3- ... 2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A acetyltransferase ...
The glycogen phosphorylase monomer is a large protein, composed of 842 amino acids with a mass of 97.434 kDa in muscle cells. ...
... results in an amino acid switch: valine to methionine exchange at codon 66, Val66Met, which is in the prodomain of BDNF.[39][38 ... Glucose-6-phosphate isomerase (GPI; PGI, PHI, AMF). *Glia maturation factor (GMF) ... as the amino acid change occurs on the portion of the prodomain where sortilin binds; and sortilin is essential for normal ... neurotrophic factor regulates the expression and synaptic delivery of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid ...
... as all ingested SOD is broken down into amino acids before being absorbed. However, ingestion of SOD bound to wheat proteins ... and their active sites contain the same type and arrangement of amino acid side-chains. They are usually dimers, but ... superoxide inactivates the citric acid cycle enzyme aconitase, can poison energy metabolism, and releases potentially toxic ...
The DCXR gene encodes a membrane protein that is approximately 34 kDa in size and composed of 224 amino acids. The protein is ...
... is a pegylated anti-vascular endothelial growth factor (VEGF) aptamer, a single strand of nucleic acid that binds ... amino]carbonyl]-3,13-dioxa-5,11-diaza-1,15-pentadecanediyl]bis[ω-methoxypoly(oxy-1,2-ethanediyl)], sodium salt[1] ... Glucose-6-phosphate isomerase (GPI; PGI, PHI, AMF). *Glia maturation factor (GMF) ... It was found that using poly(lactic-co-glycolic) acid (PLGA) microspheres, which encapsulated the drug, the minimum dosing ...
"Mutation of three critical amino acids of the N-terminal domain of IGF-binding protein-3 essential for high affinity IGF ... Glucose-6-phosphate isomerase (GPI; PGI, PHI, AMF). *Glia maturation factor (GMF) ... "Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit" ...
cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". The Journal of Biological Chemistry. 264 (16 ... AKR1B1 consists of 316 amino acid residues and weighs 35853Da. It does not possess the traditional dinucleotide binding fold. ... "Nucleic Acids Research. 17 (20): 8368. doi:10.1093/nar/17.20.8368. PMC 334974. PMID 2510130.. ... 2nvc: Human Aldose Reductase complexed with novel naphtho[1,2-d]isothiazole acetic acid derivative (3) ...
Bovine rhodopsin contains 348 amino acid residues. The retinal chromophore binds at Lys296. ... "Role of LRAT on the Retinoid Isomerase Activity and Membrane Association of Rpe65". Journal of Biological Chemistry. 282 (29 ... retinal + NAD+ + H2O → retinoic acid + NADH + H+ (catalyzed by RALDH). retinal + O2 + H2O → retinoic acid + H2O2 (catalyzed by ... Retinoic acid, sometimes called vitamin A acid, is an important signaling molecule and hormone in vertebrate animals. ...
... beyond the twenty canonical amino acids found in nature, to include an unnatural amino acid as well. The unnatural amino acid ... the tRNA with the amino acid. Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing ... and redox-active amino acids.[14] Another use is introducing amino acids bearing reactive functional groups for chemically ... the cavity that holds the amino acid can be mutated and modified to carry unnatural amino acids synthesized in the lab, and to ...
McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY, Weinstein B (June 1983). "Complete amino acid sequence of the ... 2fzz: Factor Xa in complex with the inhibitor 1-(3-amino-1,2-benzisoxazol-5-yl)-6-(2'-(((3r)-3-hydroxy-1-pyrrolidinyl)methyl)-4 ... 1mq6: Crystal Structure of 3-chloro-N-[4-chloro-2-[[(5-chloro-2-pyridinyl)amino]carbonyl]-6-methoxyphenyl]-4-[[(4,5-dihydro-2- ... 1xka: FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S)-(3'-AMIDINO-3-BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID ...
The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino ... Three possible representations of the three-dimensional structure of the protein triose phosphate isomerase. Left: All-atom ... amino acids. All proteinogenic amino acids possess common structural features, including an α-carbon to which an amino group, a ... If amino acids are present in the environment, microorganisms can conserve energy by taking up the amino acids from their ...
The opines are amino acid derivatives used by the bacterium as a source of carbon and energy. This natural process of ... Another selection system that can be employed is usage of metabolic markers such as phospho-mannose isomerase. Agrobacterium is ... CS1 maint: Multiple names: authors list (link) Ben-Amar, Anis; Daldoul, Samia; Reustle, Götz M.; Krczal, Gabriele; Mliki, Ahmed ... Todd, Rebecca; Tague, Brian W. (2001-12-01). "Phosphomannose isomerase: A versatile selectable marker forArabidopsis thaliana ...
L-α-Amino acids (incl. L-arginine, L-lysine, L-ornithine). *Osteocalcin ... Δ4-abiraterone by 3β-hydroxysteroid dehydrogenase/Δ5-4 isomerase; and Δ4-abiraterone to 3-keto-5α-abiraterone by 5α-reductase.[ ...
"Exogenous γ-aminobutyric acid treatment affects citrate and amino acid accumulation to improve fruit quality and storage ... Glutamic acid decarboxylase is the rate-limiting enzyme in the synthesis of γ-aminobutyric acid (GABA), and impaired function ... Glutamate decarboxylase or glutamic acid decarboxylase (GAD) is an enzyme that catalyzes the decarboxylation of glutamate to ... Wei J, Davis KM, Wu H, Wu JY (May 2004). "Protein phosphorylation of human brain glutamic acid decarboxylase (GAD)65 and GAD67 ...
... that appears to be associated with binding the incoming amino acid. The conserved sequence motifs found in the four Mur enzymes ... 1) formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc). ... N-acetylmuramic acid. All four Mur ligases are topologically similar to one another, even though they display low sequence ...
The amino acid side-chains of the active site are bent into positions so the enzyme does its catalytic work. In some cases, ... Isomerases: A -, B where B is an isomer of A. *Ligases: join two large molecules: Ab + C -, A-C + b ... They break down other enzymes and proteins back into amino acids.[3] Nucleases are enzymes that cut DNA or RNA, often in ... For example, fatty acids are synthesized by one set of enzymes in the cytosol, endoplasmic reticulum and Golgi apparatus. Then ...
Besides ascorbate, medically important conditional pro-oxidants include uric acid and sulfhydryl amino acids such as ... which can be catalysed by protein disulfide isomerase and glutaredoxins.[100][101] Ascorbic acid is a redox catalyst which can ... Uric acid[edit]. Uric acid is by far the highest concentration antioxidant in human blood. Uric acid (UA) is an antioxidant ... which is made from amino acids. As any glutathione in the gut is broken down to free cysteine, glycine and glutamic acid before ...
The complete amino acid sequence". European Journal of Biochemistry. 169 (3): 547-53. doi:10.1111/j.1432-1033.1987.tb13644.x. ... The complete amino acid sequence". European Journal of Biochemistry. 169 (3): 547-53. doi:10.1111/j.1432-1033.1987.tb13644.x. ... sialic acid, and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C1 complex". ...
... s (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring ... a 110-amino acid module that recognizes acetylated lysine residues and is functionally linked to the co-activators in the ... The number of amino acid residues in each HAT is indicated at the right in each example. ... The basic mechanism catalyzed by HATs involves the transfer of an acetyl group from acetyl-CoA to the ε-amino group of a target ...
In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent ... Taylor RK, LaPointe CF (2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". J. Biol. ... While a number of different mechanisms for aspartyl proteases have been proposed, the most widely accepted is a general acid- ... Jarrell KF, Bardy SL (2003). "Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in ...
Amino Acids. 44 (1): 111-8. doi:10.1007/s00726-011-1081-1. PMID 21938398. S2CID 16143202.. ... tTG also presents PDI (Protein Disulfide Isomerase) activity.[33][34] Based on its PDI activity, tTG plays an important role in ... Transcription is increased by retinoic acid. Among its many supposed functions, it appears to play a role in wound healing, ... amino group of a lysine residue and a γ-carboxamide group of glutamine residue, creating an inter- or intramolecular bond that ...
Of the twenty common naturally occurring amino acids, only proline is likely to adopt the cis isomer of the peptide bond, ... this interconversion may be catalyzed by specific isomerases known as prolyl isomerases or PPIases. The interconversion between ... However, peptide bonds that replace proline with another N-substituted amino acid (such as sarcosine) are also likely to adopt ... The PPII backbone dihedral angles (-75°, 150°) are observed frequently in proteins, even for amino acids other than proline.[2] ...
The LDHBx protein is seven amino acids longer than the LDHB (LDH-H) protein. This amino acid extension is generated by ... This leads to the addition of seven amino acid acids to the normal LDH-H protein. The extension contains a peroxisomal ... Glucose isomerase. *Phosphofructokinase 1 (Liver, Muscle, Platelet)→/Fructose 1,6-bisphosphatase←. *Fructose-bisphosphate ... LDHBx is generated by translation of the LDHB mRNA, but the stop codon is interpreted as an amino acid-encoding codon. In ...
Where C is cysteine, G is glycine, R is arginine, and X represents any amino acid.[14] ... Glucose-6-phosphate isomerase (GPI; PGI, PHI, AMF). *Glia maturation factor (GMF) ... Human EGF is 6-kDa[5] and has 53 amino acid residues and three intramolecular disulfide bonds.[6] ... stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids ...
These residues can broadly be classified as surface- and interior-allosteric amino acids. Allosteric sites at the surface ... that is not itself an amino acid. For instance, many enzymes require sodium binding to ensure proper function. However, the ... "Nucleic Acids Res. 39: D663-669. doi:10.1093/nar/gkq1022. PMC 3013650 . PMID 21051350.. CS1 maint: Explicit use of et al. (link ... For example, the GABAA receptor has two active sites that the neurotransmitter gamma-aminobutyric acid (GABA) binds, but also ...
"Hydrophobic amino acids". Amino Acid Properties and Consequences of Substitutions, In: Bioinformatics for Geneticists. Wiley. ... Protein disulfide isomerases catalyze the proper formation of disulfide bonds; the cell transfers dehydroascorbic acid to the ... and glutamic acid. While glutamic acid is usually sufficient because amino acid nitrogen is recycled through glutamate as an ... Cysteine (symbol Cys or C;[3] /ˈsɪstiiːn/)[4] is a semiessential[5] proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH ...
The amino terminal ~150 amino acids make up a regulatory domain, thought to control access of substrates to the active site.[17 ... amino acid binding. • monooxygenase activity. • protein domain specific binding. Cellular component. • cytoplasm. • cytosol. • ... aromatic amino acid family metabolic process. • response to lipopolysaccharide. • cerebral cortex development. • response to ... Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L- ...
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. ...
Recombinant Human Triosephosphate isomerase protein is an Escherichia coli Full length protein 1 to 249 aa range, , 95% purity ... Amino acids. 1 to 249. * Tags. His tag N-Terminus. Associated products. ... 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, ...
... 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 ...
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, ...
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. ...
The remainder of the OH groups hydrogen bond with neighboring amino acid side chains. A detailed mechanism for D-xylose ... The crystal structure of recombinant Streptomyces rubiginosus D-xylose isomerase (D-xylose keto-isomerase, EC 5.3.1.5) solved ... The crystal structure of recombinant Streptomyces rubiginosus D-xylose isomerase (D-xylose keto-isomerase, EC 5.3.1.5) solved ... XYLOSE ISOMERASE. A. 387. Streptomyces rubiginosus. Mutation(s): 0 Gene Names: xylA. EC: 5.3.1.5. ...
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase; KW Methionine biosynthesis; Nucleus; Reference proteome. SQ ... CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; L-methionine from S-methyl-5-thio- ... 3, Last annotation update) DE RecName: Full=Methylthioribose-1-phosphate isomerase; Short=M1Pi; DE Short=MTR-1-P isomerase; EC= ... DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:EC. DR GO; GO:0009086; P:methionine biosynthetic ...
... putative methylthioribose-1-phosphate isomerase; KW Amino-acid biosynthesis; Complete proteome; Isomerase; KW Methionine ... 3, Last annotation update) DE RecName: Full=Putative methylthioribose-1-phosphate isomerase; DE Short=M1Pi; Short=MTR-1-P ... isomerase; (AEPER1_1.PE483). GN OrderedLocusNames=APE_0686; OS AEROPYRUM PERNIX K1. OC Archaea; Crenarchaeota; Thermoprotei; ... S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:EC. DR GO; GO:0009086; P:methionine biosynthetic process; IEA: ...
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, ...
The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate ... Triosephosphate isomerase Chain: A Molecule details › Chain: A. Length: 251 amino acids. Theoretical weight: 27.21 KDa. Source ... Triosephosphate isomerase. > Triosephosphate isomerase * Occurring in:. *Triosephosphate isomerase. > Aldolase-type TIM ... of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase. ...
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 ...
Protein disulphide isomerase (PDI) is a disulphide bond-modulating ER chaperone, which can also facilitate the ER-associated ... Protein disulphide isomerase (PDI) is a disulfide bond-modulating ER chaperone, which can also facilitate the ER-associated ... 2003). An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell 11, 619-633 ... 2005). Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J. Biol. Chem. ...
X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed ... Xylose isomerase Chain: A Molecule details › Chain: A. Length: 388 amino acids. Theoretical weight: 43.25 KDa. Source organism: ... Xylose isomerase. > Xylose isomerase-like, TIM barrel domain * Occurring in:. *Xylose isomerase. > Xylose isomerase-like ... Sequence domains: Xylose isomerase-like TIM barrel Structure domains: Divalent-metal-dependent TIM barrel enzymes ...
Amino acid numbers are provided below, indicating the positions of each domain within the protein. ... for all other naturally occurring amino acids, steric hindrance between side chains precludes the cis form and overwhelmingly ... Effect of prolyl isomerase on the folding reactions of staphylococcal nuclease. Biochemistry 36:15134-15139. doi:10.1021/ ... Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell Mol Life Sci 55:423-436. doi:10.1007/ ...
The deduced amino acid sequence is 560 amino acids long, the same as the A. thaliana PgiC gene. Based on a single L. crassa ... the amino acid identity for these two species is 93.6%, showing that the cDNA sequence corresponds to cytosolic PgiC, rather ... Phosphoglucose isomerase (PGI; E.C. 5.3.1.9) catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6- ... 1987 Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156- ...
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 ...
A novel chloroplastic isopentenyl diphosphate isomerase gene from Jatropha curcas: cloning, characterization and subcellular ... A novel chloroplastic isopentenyl diphosphate isomerase gene from Jatropha curcas: cloning, characterization and subcellular ... A novel chloroplastic isopentenyl diphosphate isomerase gene from Jatropha curcas: cloning, characterization and subcellular ... It encoded a protein of 305 amino acids. Analysis of deduced amino acid sequence predicted the presence of conserved active ...
enzymes - glucose isomerase Antibiotics - penicillen food additives - amino acids. alcohol - ethanol. chemicals - citric acid ... Actinomycetes - antibiotics and amino acids. Cyanobacteria - potential renewable food stuffs in future. Proteobacteria. Fungal ...
  • Characterization of purified hP5 indicated that it has both isomerase and chaperone activities, but both activities are lower than those of human protein disulfide isomerase (PDI). (nih.gov)
  • Several thiol isomerases including protein disulfide isomerase, ERp57, and ERp5 are secreted by and localize to the membranes of platelets and endothelial cells. (bloodjournal.org)
  • Molecular characterization and analysis of a novel protein disulfide isomerase-like protein of Eimeria tenella. (sigmaaldrich.com)
  • Protein disulfide isomerase (PDI) and PDI-like proteins are members of the thioredoxin superfamily. (sigmaaldrich.com)
  • Here, we demonstrate that the reticulon family of proteins is a novel regulator of the ER chaperone protein disulfide isomerase (PDI), and that through PDI, reticulon-4A (Nogo-A) can protect mice against the neurodegeneration that characterizes ALS. (jneurosci.org)
  • Protein disulfide isomerase (PDI), an ER resident chaperone, may protect against this process. (jneurosci.org)
  • Disulfides are created in the presence of enzymes in the protein disulfide isomerase (PDI) family. (wikibooks.org)
  • This subunit forms a heterodimer along with the protein disulfide isomerase. (cags.org.ae)
  • The eps1p protein disulfide isomerase conserves classic thioredoxin superfamily amino Acid motifs but not their functional geometries. (expasy.org)
  • The third enzyme, glucose-isomerase, converts glucose to a mixture of about 42 percent fructose and 50-52 percent glucose with some other sugars mixed in. (drmirkin.com)
  • While alpha-amylase and glucoamylase are added directly to the slurry, pricey glucose-isomerase is packed into columns and the sugar mixture is then passed over it. (drmirkin.com)
  • Inexpensive alpha-amylase and glucoamylase are used only once, glucose-isomerase is reused until it loses most of its activity. (drmirkin.com)
  • Two of the enzymes used, alpha-amylase and glucose-isomerase, are genetically modified to make them more stable. (drmirkin.com)
  • It has also been proposed that the ketosteroid isomerase and other enzyme active sites provide electrostatic environments that result in larger energetic responses (i.e., greater "sensitivity") to ground-state to transition-state charge rearrangement, relative to aqueous solution, thereby providing catalysis relative to the corresponding reaction in water. (nih.gov)
  • DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones. (prospecbio.com)
  • The enzyme isopentenyl diphosphate isomerase [IDI, EC 5.3.3.2] interconverts isopentenyl diphosphate and dimethylallyl diphosphate. (bvsalud.org)
  • The removal of 41 N-terminal amino acids did not exhibit a significant effect on the enzyme activity however, the thermostability of the enzyme decreased. (bvsalud.org)
  • The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the monolactam antibiotic nocardicin A. It catalyses the epimerization of the amino group at position 9' from (S)- configuration to (R)-. The enzyme can act on both isonocardicin A and isonocardicin C, but the in vivo substrate appears to be the latter [3]. (genome.jp)
  • 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)
  • Peptidylprolyl isomerase A (PPIA), also known as cyclophilin A (CypA) or rotamase A is an enzyme that in humans is encoded by the PPIA gene on chromosome 7. (wikipedia.org)
  • Aromatic L -amino acid decarboxylase ( AADC or AAAD ), also known as DOPA decarboxylase ( DDC ), tryptophan decarboxylase , and 5-hydroxytryptophan decarboxylase , is a lyase enzyme ( EC 4.1.1.28 ). (wikidoc.org)
  • In enzymology, an isopenicillin N epimerase is an enzyme that catalyzes the chemical reaction: Isopenicillin N \rightleftharpoons penicillin N. Hence, this enzyme has one substrate, isopenicillin N, and one product, penicillin N. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. (morebooks.de)
  • The systematic name of this enzyme class is penicillin N 5-amino-5-carboxypentanoyl-epimerase. (morebooks.de)
  • The TPI1 gene provides instructions for making an enzyme called triosephosphate isomerase 1. (medlineplus.gov)
  • The triosephosphate isomerase 1 enzyme carries out a specific reaction during glycolysis: the conversion of a molecule called dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate. (medlineplus.gov)
  • This conversion can go both ways, meaning that the triosephosphate isomerase 1 enzyme can also convert glyceraldehyde 3-phosphate back into DHAP. (medlineplus.gov)
  • For the triosephosphate isomerase 1 enzyme to be turned on (active), it has to attach (bind) to another triosephosphate isomerase 1 enzyme, forming a two-enzyme complex called a dimer. (medlineplus.gov)
  • This change replaces the protein building block (amino acid) glutamic acid with the amino acid aspartic acid at position 104 in the triosephosphate isomerase 1 enzyme (written as Glu104Asp or E104D). (medlineplus.gov)
  • Without functional triosephosphate isomerase 1 enzyme to convert DHAP to glyceraldehyde 3-phosphate, red blood cells accumulate DHAP, which is toxic in large quantities. (medlineplus.gov)
  • The EBP gene provides instructions for making an enzyme called 3β-hydroxysteroid-Δ8,Δ7-isomerase. (medlineplus.gov)
  • Some of the mutations responsible for this condition in females insert or delete a small amount of genetic material from the EBP gene, while others change single protein building blocks (amino acids) in the 3β-hydroxysteroid-Δ8,Δ7-isomerase enzyme. (medlineplus.gov)
  • These cases result from changes involving single amino acids in the 3β-hydroxysteroid-Δ8,Δ7-isomerase enzyme. (medlineplus.gov)
  • Glucosephosphate isomerase, another glycolytic enzyme, displays similar activity and, conversely, depletion of PGM or glucosephosphate isomerase with short interfering RNA triggers premature senescence. (aacrjournals.org)
  • An example of a dimeric enzyme is glucose-phosphate isomerase. (encyclopedia.com)
  • An enzyme which catalyses this slow rotation was found and called peptidyl prolyl cis-trans isomerase (PPIase) (1). (bioscience.org)
  • Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. (curehunter.com)
  • It has been proposed for ketosteroid isomerase and other enzymes that active site hydrogen bonding groups provide energetic stabilization via "short, strong" or "low-barrier" hydrogen bonds that are formed due to matching of their pKa or proton affinity to that of the transition state. (nih.gov)
  • Thiol isomerases are multifunctional enzymes that influence protein structure via their oxidoreductase, isomerase, and chaperone activities. (bloodjournal.org)
  • Consequently, the action of peptidyl-prolyl cis/trans isomerases (PPIases), enzymes that catalyze the isomerization of proline peptide bonds between the cis and trans forms, is required to facilitate timely folding and subsequent protein activity ( 4 ). (asm.org)
  • Three classes of enzymes possessing phosphomannose-isomerase activity have been identified in bacteria and lower eukaryotes. (epfl.ch)
  • Based on amino acid sequence identity we propose a classification system for enzymes with phosphomannose-isomerase activity. (epfl.ch)
  • Cyclophilin (CyP) is one of the enzymes that act as peptidylprolyl cis-trans isomerases (EC 5.2.1.8). (apsnet.org)
  • The identity between amino acid sequences of functionally related enzymes of the three operons varied between 50.6 and 75.7%, with the tcbCDEF and tfdCDEF pair being the least similar of the three. (asm.org)
  • Acyl-CoA thioesterases (ACOTs) are a family of enzymes that catalyze the hydrolysis of the CoA esters of various lipids to the free acids and coenzyme A, thereby regulating levels of these compounds. (hmdb.ca)
  • Enzymes are large proteins and through genetic modification specific amino acids in the enzymes are changed or replaced so the enzyme's "backbone" won't break down or unfold. (drmirkin.com)
  • The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. (nih.gov)
  • To test the theoretical prediction that highly inbreeding populations should have low neutral genetic diversity relative to closely related outcrossing populations, we sequenced portions of the cytosolic phosphoglucose isomerase ( PgiC ) gene in the plant genus Leavenworthia, which includes both self-incompatible and inbreeding taxa. (genetics.org)
  • The aim of the work described here is to compare sequence polymorphism at the DNA level in a phosphoglucose isomerase gene between species with different outcrossing rates. (genetics.org)
  • The present investigation describes the cloning, characterization and subcellular localization of isopentenyl diphosphate isomerase (IPI) gene from J. curcas . (ejbiotechnology.info)
  • The characterization of gene mutations for human glucose phosphate isomerase deficiency associated with chronic hemolytic anemia. (jci.org)
  • TY - JOUR T1 - The effects of disruption of phosphoglucose isomerase gene on carbon utilisation and cellulase production in Trichoderma reesei Rut-C30. (unboundmedicine.com)
  • The cDNA, under the control of the GAL1 promoter, was expressed in a Saccharomyces cerevisiae strain from which the native gene encoding phosphomannose isomerase had been deleted. (epfl.ch)
  • The precise amino acid content, and the sequence of those amino acids, of a specific protein, is determined by the sequence of the bases in the gene that encodes that protein. (wikibooks.org)
  • At least 12 mutations in the TPI1 gene have been found to cause triosephosphate isomerase deficiency. (medlineplus.gov)
  • One TPI1 gene mutation accounts for approximately 80 percent of triosephosphate isomerase deficiency cases. (medlineplus.gov)
  • Here, we report that amino acid signaling through the nutrient-sensitive target of rapamycin (TOR) pathway is essential for the activation of YPP gene expression. (pnas.org)
  • An increase in extracellular amino acid levels, similar to the increase observed after a blood meal, is critical for 20E stimulation of YPP gene expression. (pnas.org)
  • Mutations in this gene are associated with triosephosphate isomerase deficiency. (genetex.com)
  • The PIN1At gene encodes a protein of 119 amino acids that is 53% identical with the catalytic domain of the human PIN1 parvulin. (ugent.be)
  • A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease. (ebi.ac.uk)
  • If the protein's amino acid residues, specifically cysteines, are close to one another they will form a disulfide bond even if it is not properly folded. (wikibooks.org)
  • The phosphorylation of proteins on the serine or threonine residues that immediately precede proline (pSer/Thr-Pro) is specifically catalyzed by the prolyl isomerase Pin1 and is a key signaling mechanism in cell proliferation and transformation. (aacrjournals.org)
  • Amino acid biosynthesis overview. (wikipedia.org)
  • The pathways for the biosynthesis of essential amino acids are much more complex than those for the nonessential ones. (wikipedia.org)
  • Ct 's major active pathways are glycolysis, gluconeogenesis, glycerol-phospholipid (GPL) biosynthesis (support from host acetyl-CoA) and pentose phosphate pathway (PPP), while its incomplete TCA and fatty acid biosynthesis are less active. (frontiersin.org)
  • Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:190450]. (abcam.com)
  • Nerve cells in the part of the brain involved in coordinating movements (the cerebellum) are particularly affected in people with triosephosphate isomerase deficiency. (medlineplus.gov)
  • Death of red and white blood cells, nerve cells in the brain, and cardiac muscle cells leads to the signs and symptoms of triosephosphate isomerase deficiency. (medlineplus.gov)
  • Rodríguez-Almazán C, Arreola R, Rodríguez-Larrea D, Aguirre-López B, de Gómez-Puyou MT, Pérez-Montfort R, Costas M, Gómez-Puyou A, Torres-Larios A. Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. (medlineplus.gov)
  • Each dgt mutation reduced or nullified the peptidyl-prolyl isomerase activity of the GST-LeCYP1 fusion proteins in vitro. (rti.org)
  • Objective- The Pin1 prolyl isomerase acts in concert with proline-directed protein kinases to regulate function of protein substrates through isomerization of peptide bonds that link phosphoserine or phosphothreonine to proline. (ahajournals.org)
  • This mechanism involves phosphorylation-dependent conformational changes that are induced by the Pin1 prolyl isomerase. (ahajournals.org)
  • We investigated how calcineurin caused spine pathology and found that the cis-trans prolyl isomerase Pin1 was a critical downstream target of Aβ 42 -calcineurin signaling. (sciencemag.org)
  • One protein whose dysfunction is implicated in both spine physiology and AD pathogenesis is the peptidyl-prolyl isomerase Pin1 ( 3 ). (sciencemag.org)
  • Analysis of deduced amino acid sequence predicted the presence of conserved active sites, metal binding sites and the NUDIX motif, which were consistent with other IPIs. (ejbiotechnology.info)
  • The deduced amino acid sequence of the characterized open reading frame shows approximately 80% homology with cytosolic CyP from other organisms. (apsnet.org)
  • The deduced amino acid sequence of an arsenate-resistant clone, PV4-8, had cDNA highly homologous to plant cytosolic triosephosphate isomerases (cTPI). (deepdyve.com)
  • The EtPDIL cDNA contained 1129 nucleotides encoding 216 amino acids. (sigmaaldrich.com)
  • Through unbiased expression screening of a bovine retinal pigment epithelium (RPE) cDNA library, we have identified elongation of very long-chain fatty acids-like 1 (ELOVL1) and fatty acid transport protein 4 (FATP4), which each have very long-chain fatty acid acyl-CoA synthetase (VLCFA-ACS) activity, as negative regulators of RPE65. (jneurosci.org)
  • Protein sequence information obtained from internal fragments of the protein was used to design degenerate oligonucleotides which were used to amplify a fragment of a human phosphomannose-isomerase cDNA. (epfl.ch)
  • The cDNA encoded a protein with significant sequence identity to fungal and some bacterial phosphomannose isomerases but was unrelated to those from other bacteria. (epfl.ch)
  • Mutation of two thioredoxin-related motifs in hP5 revealed that the first motif is more important than the second for isomerase activity and that the first cysteine in each motif is necessary for isomerase activity. (nih.gov)
  • 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)
  • The central domain is a cysteine -rich region, which contains four repeats of the motif CXXCXGXG where X is any amino acid. (wikipedia.org)
  • In proteins, these bonds form between the thiol groups of two cysteine amino acids. (wikibooks.org)
  • Most of the cross-linkages are from disulfide bonds formed by the oxidation of two cysteine amino acids. (wikibooks.org)
  • The cysteine amino acid group is the only amino acid capable of forming disulfide bonds, and thus can only do so with other cysteine groups. (wikibooks.org)
  • O2 directly regulates two transcription factors, genes linked to carbon and amino acid metabolism and abiotic stress resistance. (plantcell.org)
  • RB utilizes energy -rich compounds to generate ATP in nucleic acid metabolism. (frontiersin.org)
  • Amino acids play central roles both as building blocks of proteins and as intermediates in metabolism. (wikibooks.org)
  • B6 plays a particularly important role in neurotransmitter, sulfur amino acids metabolism and in niacin synthesis from tryptophan. (aquaplantscare.uk)
  • Triosephosphate isomerase (TIM) catalyses the reversible interconversion of G3P and DHAP. (abcam.com)
  • Phosphomannose isomerase catalyses the interconversion of fructose-6-P and mannose-6-P and has a critical role in the supply of D-mannose derivatives required for many eukaryotic glycosylation reactions. (epfl.ch)
  • The most important role is in processes of oxidising and reduction and in processes of amino acids (it catalyses them into carbohydrates and fats) and lipids syntheses. (aquaplantscare.uk)
  • Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability. (uni-regensburg.de)
  • To this end the crystal structure of dimeric phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima (tPRAI) was determined using phases derived from the isomorphous replacement method and was refined at 2.0 A resolution. (uni-regensburg.de)
  • Amino acid composition and sequence analyses of the protein products of T.maritima trpC (indoleglycerol phosphate synthase), trpF (phosphoribosyl anthranilate isomerase) and trpA (alpha-subunit of tryptophan synthase) suggest that these thermostable (beta alpha)8-barrel proteins may be stabilized by additional salt bridges, compared with the mesostable forms. (uni-regensburg.de)
  • 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)
  • Pin1, a recently identified peptidyl-prolyl cis/trans isomerase (PPIase), has two domains: a PPIase domain at its COOH terminus responsible for isomerization and a WW domain at the NH 2 terminus, which functions as a binding element specific to pSer/Thre-Pro motifs ( 18 - 20 ). (aacrjournals.org)
  • A homologue of the human site-specific prolyl cis/trans isomerase PIN1 was identified in Arabidopsis thaliana. (ugent.be)
  • In dendritic spines, Pin1 interacted with and was dephosphorylated by calcineurin, which rapidly suppressed its isomerase activity. (sciencemag.org)
  • Alleles dgt(1-1)and dgt(1-2) contain single nucleotide point mutations that generate an amino acid change (G137R) and a stop codon (W128stop), respectively, while dgt(dp) has an amino acid change (W128CDelta129-133) preceding a 15 bp deletion. (rti.org)
  • 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)
  • It has been previously shown that bacterial mutants lacking phosphoglucose isomerase (PGI) produce more nucleotide precursors and amino acids. (unboundmedicine.com)
  • It can be modulated by the alteration of fatty acids that build membrane phospholipids. (hindawi.com)
  • Thiamin in organisms plays 3 main roles: participates in energy processes (in mitochondria), in chemical reactions leading to nucleic and fatty acids synthesis as well as in neurophysiological processes (plays a role in the synthesis of neurotransmitters). (aquaplantscare.uk)
  • More complex classification schemes have been proposed ( 26 , 38 ), the most successful being one based on the range and proportion of cellular fatty acids and ubiquinones ( 21 , 22 , 40 , 43 ). (asm.org)
  • The inclusion of hydroxylated fatty acids has improved discrimination, but it requires the analysis of both mono- and dihydroxylated fatty acids, and individual patterns are complex, making analysis difficult ( 21 ). (asm.org)
  • Plant triose phosphate isomerase isozymes : purification, immunological and structural characterization, and partial amino Acid sequences. (semanticscholar.org)
  • The plastid isoform of triose phosphate isomerase is required for the postgerminative transition from heterotrophic to autotrophic growth in Arabidopsis. (semanticscholar.org)
  • Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5A resolution using amino acid sequence data. (nii.ac.jp)
  • It was shown to have the same amino-acid sequence with that of bovine cyclophilin (CyP), a target protein for an immunosuppressant, cyclosporin A (CsA) (2, 3). (bioscience.org)
  • Characterization of an l-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH. (semanticscholar.org)
  • Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain. (semanticscholar.org)
  • Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum. (semanticscholar.org)
  • Disulfide-Bond Isomerase Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 216 amino acids (21-236) and having a molecular mass of 23.5 kDa. (prospecbio.com)
  • The crystal structure of recombinant Streptomyces rubiginosus D-xylose isomerase (D-xylose keto-isomerase, EC 5.3.1.5) solved by the multiple isomorphous replacement technique has been refined to R = 0.16 at 1.64 A resolution. (rcsb.org)
  • Cell-free extracts of PV4-8 had 3-fold higher level of triosephosphate isomerase (TPI) specific activities than that found in E. coli XL-1 Blue and had a 42 kD fusion protein immunoreactive to polyclonal antibodies raised against recombinant Solanum chacoense cTPI. (deepdyve.com)
  • Recombinant fusion protein containing a sequence corresponding to amino acids 1-249 of human TPI1 (NP_000356.1). (genetex.com)
  • 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)
  • 259: 3230-3236, 1984), xylose isomerase is a tetramer composed of four identical subunits. (rcsb.org)
  • A detailed mechanism for D-xylose isomerase is proposed. (rcsb.org)
  • Upon binding of cyclic alpha-D-xylose to xylose isomerase, His-54 acts as the catalytic base in a ring opening reaction. (rcsb.org)
  • D-xylose isomerase (XI) is capable of sugar isomerization and slow conversion of some monosaccharides into their C2-epimers. (rcsb.org)
  • Protein disulphide isomerase (PDI) is a disulphide bond-modulating ER chaperone, which can also facilitate the ER-associated degradation (ERAD) of misfolded proteins. (frontiersin.org)
  • This domain has disulphide isomerase activity. (wikipedia.org)
  • MD-FEP simulations indicate that amino acid substitutions in a hydrophobic pocket near C5 of L-arabinose can enhance sugar binding. (rcsb.org)
  • Amino acids can be broadly hydrophobic and hydrophilic , depending on the chemical properties of the R group side chain. (wikibooks.org)
  • In an aqueous environment, the hydrophobic amino acids are unable to participate in hydrogen bonding. (wikibooks.org)
  • The difference in net protein charge was attributable not to specific amino acid sites but to the sum of various amino acid sites located on the surface of the PGI molecule. (biomedcentral.com)
  • Transferases speed along the transfer of groups of atoms, such as methyl, acetyl or amino groups, from one molecule to another molecule. (pharmiweb.com)
  • The formation of a dipeptide from two amino acids is accompanied by the loss of a water molecule. (wikibooks.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)
  • The reduced thiol isomerase aligns with a substrate that contains a disulfide bond such that the free thiolate forms an 180° angle with the vector of the disulfide. (bloodjournal.org)
  • In recent years, identification of proteins participating in cross-linked structures in epidermis and appendages has benefited from the approach of peptide generation with enzymatic fragmentation followed by separation and amino acid sequencing of the peptides. (mcponline.org)
  • Interleukins (IL-1a, IL-1ß, IL-2, IL-4, IL-6, TNFa), immunophylin and ubiquitin as well as proline rich peptides, comprised of 10-15 amino acids are being produced in N. Supraopticus and N. Paraventricularis and then secreted into neurohypophysis. (springer.com)
  • Certain species of lactic acid bacteria produce and secrete bacteriocins, which are ribosomally synthesized antimicrobial peptides. (uio.no)
  • Amino acids that must be obtained from the diet are called essential amino acids . (wikipedia.org)
  • More than 500 amino acids exist in nature, but the proteins in all species, from bacteria to humans, consist mainly of only 20 called the essential amino acids. (wikibooks.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)
  • 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)
  • Protein disulfide isomerases are redox chaperones from the thioredoxin superfamily, with crucial functions in redox protein folding at the endoplasmic reticulum (ER). (nature.com)
  • To test these models, we substituted tyrosine with fluorotyrosines (F-Tyr's) in the ketosteroid isomerase (KSI) oxyanion hole to systematically vary the proton affinity of an active site hydrogen bond donor while minimizing steric or structural effects. (nih.gov)
  • Tyrosine is synthesized by the hydroxylation of phenylalanine , an essential amino acid. (wikipedia.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)
  • The Interaction of DCA and/or Tyrosine Breakdown Products and Maleylacetoacetate Isomerase (MAAI) in Vivo. (clinicaltrials.gov)
  • Subjects are administered an infusion of the amino acids leucine and tyrosine. (clinicaltrials.gov)
  • Given the infusion of the above amino acids and DCA administration the inhibition of tyrosine will be measured in the KRT haplotype and non KRT haplotype. (clinicaltrials.gov)
  • Soon after this discovery, a target protein for FK506 (FKBP: FK506 binding protein), a macrolide immunosuppressant, was also shown to be a PPIase, while amino-acid sequence homology between them was low (4). (bioscience.org)
  • 4 PDI, present in the endoplasmic reticulum, is the prototype thiol isomerase and has been extensively studied. (bloodjournal.org)
  • Protein disulfide isomerases (PDIs) support endoplasmic reticulum redox protein folding and cell-surface thiol-redox control of thrombosis and vascular remodeling. (nature.com)
  • and tcbF, which encodes a putative trans-dienelactone isomerase (37.5 kDa). (asm.org)
  • MTTP encodes a 97 kDa large subunit that is 894 amino acids long. (cags.org.ae)
  • In a variety of other eukaryotic systems, amino acid signaling is transduced through the target of rapamycin (TOR) signaling pathway ( 16 , 17 ). (pnas.org)
  • This family of proteins contain a 70 amino acid consensus sequence known as the J domain. (wikipedia.org)
  • In addition, proteins contain within their amino acid sequences the necessary information to determine how that protein will fold into a three dimensional structure, and the stability of the resulting structure. (wikibooks.org)
  • however, it has some amino acid homology with yeast sterol isomerases ( 4 ). (aacrjournals.org)
  • Nucleic Acids Res, 2003 Aug 15. (nih.gov)
  • Nucleic acids research. (rochester.edu)
  • This affords an unproven, but logically consistent explanation for the fact that contemporary proteins are assembled by a ribozyme and contemporary nucleic acids are made by a protein polymerase. (mdpi.com)
  • Is it possible to understand the molecular structure and function of proteins and nucleic acids in enough detail to make accurate predictions about structure and function? (stanford.edu)
  • p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. (uniprot.org)
  • Questions we are trying to answer include: How can a protein be stabilized by a single amino acid change? (stanford.edu)
  • Most amino acids are synthesized from α- ketoacids , and later transaminated from another amino acid, usually glutamate . (wikipedia.org)
  • Proteins are linear polymers formed by linking the a-carboxyl group of one amino acid to the a-amino group of another amino acid. (wikibooks.org)
  • 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)
  • The different amino acid substitutions have been mapped on to the recently determined crystal structure of GSTZ1-1 to evaluate and explain their influence on function. (labome.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)
  • peptidylprolyl cis/trans isomerase, NIMA-in. (broadinstitute.org)
  • They are peptidyl-prolyl-cis-trans-isomerases. (springer.com)
  • We show by two-dimensional NMR spectroscopy that the PIN1At is a prolyl cis/trans isomerase with specificity for phosphoserine-proline bonds. (ugent.be)
  • 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)
  • Succinyl-CoA is an important intermediate in the citric acid cycle, where it is synthesized from α-Ketoglutarate by α-ketoglutarate dehydrogenase (EC 1.2.4.2) through decarboxylation, and is converted into succinate through the hydrolytic release of coenzyme A by succinyl-CoA synthetase (EC 6.2.1.5). (hmdb.ca)
  • In the mid-1990s, ADM was the object of an FBI probe into price fixing of three products-HFCS, citric acid and lysine-and consumers. (drmirkin.com)
  • GSTZ1d: a new allele of glutathione transferase zeta and maleylacetoacetate isomerase. (labome.org)