ATP Synthetase Complexes
Amino Acyl-tRNA Synthetases
Multienzyme Complexes
Dicyclohexylcarbodiimide
Phosphotransferases
Aspartate-tRNA Ligase
Methionine-tRNA Ligase
Adenosine Diphosphate
Adenosine Triphosphatases
Fatty Acid Synthases
Glutamate-tRNA Ligase
RNA, Transfer, Glu
RNA, Transfer, Amino Acyl
Glutamate-Ammonia Ligase
2',5'-Oligoadenylate Synthetase
Adenosine Triphosphate
Macromolecular Substances
Escherichia coli
Reticulocytes
Chromatography, Gel
Molecular Sequence Data
Amino Acid Sequence
Detergents
Liver
Peptide Synthases
Protein Conformation
Electrophoresis, Polyacrylamide Gel
Ligases
Tryptophan-tRNA Ligase
Carbon-Nitrogen Ligases
MedlinePlus
Health Records, Personal
Genetic Diseases, Inborn
Genetic Counseling
Genetic Testing
Williams Syndrome
F0 complex of the Escherichia coli ATP synthase. Not all monomers of the subunit c oligomer are involved in F1 interaction. (1/160)
The antigenic determinants of mAbs against subunit c of the Escherichia coli ATP synthase were mapped by ELISA using overlapping synthetic heptapeptides. All epitopes recognized are located in the hydrophilic loop region and are as follows: 31-LGGKFLE-37, 35-FLEGAAR-41, 36-LEGAAR-41 and 36-LEGAARQ-42. Binding studies with membrane vesicles of different orientation revealed that all mAbs bind to everted membrane vesicles independent of the presence or absence of the F1 part. Although the hydrophilic region of subunit c and particularly the highly conserved residues A40, R41, Q42 and P43 are known to interact with subunits gamma and epsilon of the F1 part, the mAb molecules have no effect on the function of F0. Furthermore, it could be demonstrated that the F1 part and the mAb molecule(s) are bound simultaneously to the F0 complex suggesting that not all c subunits are involved in F1 interaction. From the results obtained, it can be concluded that this interaction is fixed, which means that subunits gamma and epsilon do not switch between the c subunits during catalysis and furthermore, a complete rotation of the subunit c oligomer modified with mAb(s) along the stator of the F1F0 complex, proposed to be composed of at least subunits b and delta, seems to be unlikely. (+info)Chemical mechanism of ATP synthase. Magnesium plays a pivotal role in formation of the transition state where ATP is synthesized from ADP and inorganic phosphate. (2/160)
The chemical mechanism by which ATP synthases catalyze the synthesis of ATP remains unknown despite the recent elucidation of the three-dimensional structures of two forms of the F(1) catalytic sector (subunit stoichiometry, alpha(3)beta(3)gammadeltaepsilon). Lacking is critical information about the chemical events taking place at the catalytic site of each beta-subunit in the transition state. In an earlier report (Ko, Y. H., Bianchet, M. A., Amzel, L.M., and Pedersen, P. L. (1997) J. Biol. Chem. 272, 18875-18881), we provided evidence for transition state formation in the presence of Mg(2+), ADP, and orthovanadate (V(i)), a photoreactive phosphate analog with a trigonal bipyramidal geometry resembling that of the gamma-P of ATP in the transition state of enzymes like myosin. In the presence of ultraviolet light and O(2,) the MgADP.V(i)-F(1) complex was cleaved within the P-loop (GGAGVGKT) of a single beta-subunit at alanine 158, implicating this residue as within contact distance of the gamma-P of ATP in the transition state. Here, we report that ADP, although facilitating transition state formation, is not essential. In the presence of Mg(2+) and V(i) alone the catalytic activity of the resultant MgV(i)-F(1) complex is inhibited to nearly the same extent as that observed for the MgADP. V(i)-F(1) complex. Inhibition is not observed with ADP, Mg(2+), or V(i) alone. Significantly, in the presence of ultraviolet light and O(2,) the MgV(i)-F(1) complex is cleaved also within the P-loop of a single beta-subunit at alanine 158 as confirmed by Western blot analyses with two different antibodies, by N-terminal sequence analyses, and by quantification of the amount of unreacted beta-subunits. These novel findings indicate that Mg(2+) plays a pivotal role in transition state formation during ATP synthesis catalyzed by ATP synthases, a role that involves both its preferential coordination with P(i) and the repositioning of the P-loop to bring the nonpolar alanine 158 into the catalytic pocket. A reaction scheme for ATP synthases depicting a role for Mg(2+) in transition state formation is proposed here for the first time. (+info)Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase 6 gene encoding subunit a. (3/160)
We investigated the biochemical phenotype of the mtDNA T8993G point mutation in the ATPase 6 gene, associated with neurogenic muscle weakness, ataxia, and retinitis pigmentosa (NARP), in three patients from two unrelated families. All three carried >80% mutant genome in platelets and were manifesting clinically various degrees of the NARP phenotype. Coupled submitochondrial particles prepared from platelets capable of succinate-sustained ATP synthesis were studied using very sensitive and rapid luminometric and fluorescence methods. A sharp decrease (>95%) in the succinate-sustained ATP synthesis rate of the particles was found, but both the ATP hydrolysis rate and ATP-driven proton translocation (when the protons flow from the matrix to the cytosol) were minimally affected. The T8993G mutation changes the highly conserved residue Leu(156) to Arg in the ATPase 6 subunit (subunit a). This subunit, together with subunit c, is thought to cooperatively catalyze proton translocation and rotate, one with respect to the other, during the catalytic cycle of the F(1)F(0) complex. Our results suggest that the T8993G mutation induces a structural defect in human F(1)F(0)-ATPase that causes a severe impairment of ATP synthesis. This is possibly due to a defect in either the vectorial proton transport from the cytosol to the mitochondrial matrix or the coupling of proton flow through F(0) to ATP synthesis in F(1). Whatever mechanism is involved, this leads to impaired ATP synthesis. On the other hand, ATP hydrolysis that involves proton flow from the matrix to the cytosol is essentially unaffected. (+info)Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. (4/160)
Around 30-40 years after the first isolation of the five complexes of oxidative phosphorylation from mammalian mitochondria, we present data that fundamentally change the paradigm of how the yeast and mammalian system of oxidative phosphorylation is organized. The complexes are not randomly distributed within the inner mitochondrial membrane, but assemble into supramolecular structures. We show that all cytochrome c oxidase (complex IV) of Saccharomyces cerevisiae is bound to cytochrome c reductase (complex III), which exists in three forms: the free dimer, and two supercomplexes comprising an additional one or two complex IV monomers. The distribution between these forms varies with growth conditions. In mammalian mitochondria, almost all complex I is assembled into supercomplexes comprising complexes I and III and up to four copies of complex IV, which guided us to present a model for a network of respiratory chain complexes: a 'respirasome'. A fraction of total bovine ATP synthase (complex V) was isolated in dimeric form, suggesting that a dimeric state is not limited to S.cerevisiae, but also exists in mammalian mitochondria. (+info)Differential regulation of exonic regulatory elements for muscle-specific alternative splicing during myogenesis and cardiogenesis. (5/160)
Muscle-specific isoform of the mitochondrial ATP synthase gamma subunit (F(1)gamma) was generated by alternative splicing, and exon 9 of the gene was found to be lacking particularly in skeletal muscle and heart tissue. Recently, we reported that alternative splicing of exon 9 was induced by low serum or acidic media in mouse myoblasts, and that this splicing required de novo protein synthesis of a negative regulatory factor (Ichida, M., Endo, H., Ikeda, U., Matsuda, C., Ueno, E., Shimada, K., and Kagawa, Y. (1998) J. Biol. Chem. 273, 8492-8501; Hayakawa, M., Endo, H., Hamamoto, T., and Kagawa, Y. (1998) Biochem. Biophys. Res. Commun. 251, 603-608). In the present report, we identified a cis-acting element on the muscle-specific alternatively spliced exon of F(1)gamma gene by an in vivo splicing system using cultured cells and transgenic mice. We constructed a F(1)gamma wild-type minigene, containing the full-length gene from exon 8 to exon 10, and two mutants; one mutant involved a pyrimidine-rich substitution on exon 9, whereas the other was a purine-rich substitution, abbreviated as F(1)gamma Pu-del and F(1)gamma Pu-rich mutants, respectively. Based on an in vivo splicing assay using low serum- or acid-stimulated splicing induction system in mouse myoblasts, Pu-del mutation inhibited exon inclusion, indicating that a Pu-del mutation would disrupt an exonic splicing enhancer. On the other hand, the Pu-rich mutation blocked muscle-specific exon exclusion following both inductions. Next, we produced transgenic mice bearing both mutant minigenes and analyzed their splicing patterns in tissues. Based on an analysis of F(1)gamma Pu-del minigene transgenic mice, the purine nucleotide of this element was shown to be necessary for exon inclusion in non-muscle tissue. In contrast, analysis of F(1)gamma Pu-rich minigene mice revealed that the F(1)gamma Pu-rich mutant exon had been excluded from heart and skeletal muscle of these transgenic mice, despite the fact mutation of the exon inhibited muscle-specific exon exclusion in myotubes of early embryonic stage. These results suggested that the splicing regulatory mechanism underlying F(1)gamma pre-mRNA differed between myotubes and myofibers during myogenesis and cardiogenesis. (+info)Catalytic site forms and controls in ATP synthase catalysis. (6/160)
A suggested minimal scheme for substrate binding by and interconversion of three forms of the catalytic sites of the ATP synthase is presented. Each binding change, that drives simultaneous interchange of the three catalytic site forms, requires a 120 degrees rotation of the gamma with respect to the beta subunits. The binding of substrate(s) at two catalytic sites is regarded as sufficing for near maximal catalytic rates to be attained. Although three sites do not need to be filled for rapid catalysis, during rapid bisite catalysis some enzyme may be transiently present with three sites filled. Forms with preferential binding for ADP and P(i) or for ATP are considered to arise from the transition state and participate in other steps of the catalysis. Intermediate forms and steps that may be involved are evaluated. Experimental evidence for energy-dependent steps and for control of coupling to proton translocation and transition state forms are reviewed. Impact of relevant past data on present understanding of catalytic events is considered. In synthesis a key step is suggested in which proton translocation begins to deform an open site so as to increase the affinity for ADP and P(i), that then bind and pass through the transition state, and yield tightly bound ATP in one binding change. ADP binding appears to be a key parameter controlling rotation during synthesis. In hydrolysis ATP binding to a loose site likely precedes any proton translocation, with proton movement occurring as the tight site form develops. Aspects needing further study are noted. Characteristics of the related MgADP inhibition of the F(1) ATPases that have undermined many observations are summarized, and relations of three-site filling to catalysis are assessed. (+info)The epsilon subunit of bacterial and chloroplast F(1)F(0) ATPases. Structure, arrangement, and role of the epsilon subunit in energy coupling within the complex. (7/160)
Recent studies show that the epsilon subunit of bacterial and chloroplast F(1)F(0) ATPases is a component of the central stalk that links the F(1) and F(0) parts. This subunit interacts with alpha, beta and gamma subunits of F(1) and the c subunit ring of F(0). Along with the gamma subunit, epsilon is a part of the rotor that couples events at the three catalytic sites sequentially with proton translocation through the F(0) part. Structural data on the epsilon subunit when separated from the complex and in situ are reviewed, and the functioning of this polypeptide in coupling within the ATP synthase is considered. (+info)The rotary binding change mechanism of ATP synthases. (8/160)
The F(0)F(1) ATP synthase functions as a rotary motor where subunit rotation driven by a current of protons flowing through F(0) drives the binding changes in F(1) that are required for net ATP synthesis. Recent work that has led to the identification of components of the rotor and stator is reviewed. In addition, a model is proposed to describe the transmission of energy from four proton transport steps to the synthesis of one ATP. Finally, some of the requirements for efficient energy coupling by a rotary binding change mechanism are considered. (+info)These disorders are caused by changes in specific genes that fail to function properly, leading to a cascade of effects that can damage cells and tissues throughout the body. Some inherited diseases are the result of single gene mutations, while others are caused by multiple genetic changes.
Inherited diseases can be diagnosed through various methods, including:
1. Genetic testing: This involves analyzing a person's DNA to identify specific genetic changes that may be causing the disease.
2. Blood tests: These can help identify certain inherited diseases by measuring enzyme levels or identifying specific proteins in the blood.
3. Imaging studies: X-rays, CT scans, and MRI scans can help identify structural changes in the body that may be indicative of an inherited disease.
4. Physical examination: A healthcare provider may perform a physical examination to look for signs of an inherited disease, such as unusual physical features or abnormalities.
Inherited diseases can be treated in various ways, depending on the specific condition and its causes. Some treatments include:
1. Medications: These can help manage symptoms and slow the progression of the disease.
2. Surgery: In some cases, surgery may be necessary to correct physical abnormalities or repair damaged tissues.
3. Gene therapy: This involves using genes to treat or prevent inherited diseases.
4. Rehabilitation: Physical therapy, occupational therapy, and other forms of rehabilitation can help individuals with inherited diseases manage their symptoms and improve their quality of life.
Inherited diseases are a significant public health concern, as they affect millions of people worldwide. However, advances in genetic research and medical technology have led to the development of new treatments and management strategies for these conditions. By working with healthcare providers and advocacy groups, individuals with inherited diseases can access the resources and support they need to manage their conditions and improve their quality of life.
Physical Features:
* Delayed growth and short stature
* Broad forehead
* Long, narrow face with a wide mouth and full lips
* Wide-set eyes that are often blue or green
* Low-set ears
* Curly or wavy hair
Developmental Features:
* Intellectual disability or cognitive impairment
* Delayed speech and language development
* Difficulty with fine motor skills and hand-eye coordination
* Poor musical ability
Personality Profile:
* Friendly and outgoing personality
* High level of empathy and compassion for others
* Excellent social skills
* Love of music and dance
* Curiosity and playfulness
Causes and Inheritance:
Williams syndrome is caused by a deletion of genetic material from chromosome 7, specifically the q11.23 region. This deletion occurs spontaneously, without a known family history or environmental trigger. The disorder is not inherited in a Mendelian pattern, meaning that it does not follow traditional patterns of inheritance.
Diagnosis:
Williams syndrome can be diagnosed through a combination of physical and developmental assessments, as well as genetic testing. Physical features such as broad foreheads and wide mouths are often present at birth, while developmental delays and cognitive impairments may not become apparent until later in childhood. Genetic testing can confirm the diagnosis by identifying the deletion of genetic material on chromosome 7.
Treatment and Management:
There is no cure for Williams syndrome, but early intervention and specialized management can help individuals with the disorder reach their full potential. Treatment may include:
* Physical therapy to improve fine motor skills and coordination
* Speech and language therapy to improve communication skills
* Occupational therapy to develop daily living skills
* Special education programs tailored to individual needs
* Medications to manage cardiovascular problems, hypertension, and sleep disorders
Prognosis:
The prognosis for individuals with Williams syndrome varies depending on the severity of the symptoms. Some individuals may experience significant developmental delays and cognitive impairments, while others may have fewer or no symptoms. With early intervention and specialized management, many individuals with Williams syndrome can lead fulfilling lives and achieve their full potential.
Inheritance Pattern:
Williams syndrome is not inherited in a Mendelian pattern, meaning that it does not follow traditional patterns of inheritance. The disorder is caused by a spontaneous deletion of genetic material on chromosome 7, and there is no known family history or environmental trigger. Each child of an individual with Williams syndrome has a 50% chance of inheriting the deletion and developing the disorder.
Prenatal Testing:
Prenatal testing for Williams syndrome is available but not routine. The test is typically offered to pregnant women who have a family history of the disorder or who have had a previous child with Williams syndrome. Prenatal testing involves analyzing cells from the developing fetus, usually through chorionic villus sampling (CVS) or amniocentesis.
Genetic Counseling:
Genetic counseling is essential for individuals and families affected by Williams syndrome. A genetic counselor can provide information on the inheritance pattern of the disorder, discuss prenatal testing options, and offer guidance on managing the condition. Genetic counseling can also help families understand the risks and benefits of genetic testing and make informed decisions about their reproductive options.
In conclusion, Williams syndrome is a rare genetic disorder that affects approximately 1 in 10,000 individuals worldwide. It is caused by a spontaneous deletion of genetic material on chromosome 7 and is characterized by developmental delays, cognitive impairments, and cardiovascular problems. Early intervention and specialized management can significantly improve the prognosis for individuals with Williams syndrome. Prenatal testing and genetic counseling are available for families who have a risk of inheriting the disorder. With proper care and support, individuals with Williams syndrome can lead fulfilling lives and achieve their full potential.
List of MeSH codes (D08)
NtrC
Leucyl-tRNA synthetase
Photosynthetic reaction centre protein family
Trypanothione synthase
Aminoacyl tRNA synthetase
Acetyl-CoA synthetase
Citric acid cycle
Hydrogen sulfide
Glutamine synthetase
Long-chain-fatty-acid-CoA ligase
Succinic acid
Orotate phosphoribosyltransferase
Adenosine triphosphate
Acetyl-CoA
Adenylylation
Mitochondrial matrix
Mahlon Hoagland
Marcin Hoffmann
Long-chain-fatty-acid-luciferin-component ligase
ATP citrate synthase
Nonribosomal code
Polynucleotide adenylyltransferase
Ribonucleotide
ATP synthase
CAD protein
Cofactor F430
ACOT4
ACOT1
ACOT11
Metabolism
Find-me signals
Aminoacyl-tRNA
Glutathione synthetase
Protocell
List of OMIM disorder codes
Aliivibrio fischeri
Phosphoribosylaminoimidazolesuccinocarboxamide synthase
Chromatiaceae
DNA unwinding element
Sulfur assimilation
Thymidine kinase in clinical chemistry
CTP synthetase
Botany
Phosphoribosylglycinamide formyltransferase
Purine metabolism
Ap4A
Fatty acid synthesis
SUCLG2
List of enzymes
Dino Moras
Nucleotide
Transferase
Methylglyoxal synthase
Gcn2
Glutaminolysis
Rates and mechanisms of resistance development in Mycobacterium tuberculosis to a novel diarylquinoline ATP synthase inhibitor ...
Bedaquiline: a novel antitubercular agent for the treatment of multidrug-resistant tuberculosis - PubMed
Publication Detail
MeSH Browser
Publication : USDA ARS
SCOP 1.55: Domain d1e22a1: 1e22 A:11-153
Biomarkers Search
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DeCS
NDF-RT Code NDF-RT Name
Pesquisa | Prevenção e Controle de Câncer
NR 20.0 31819.3
NEW (2002) MESH HEADINGS WITH SCOPE NOTES (UNIT RECORD FORMAT; 8/27/2001
Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase. | NECAT
phosphatase complex - Ontology Browser - Rat Genome Database
FlyMine: Gene blw D. melanogaster
RCSB PDB - 3MWD: Truncated Human ATP-Citrate Lyase with Citrate Bound
Pharos : Target Details - LARS
ybeX protein (Escherichia coli K12 MG1655) - STRING interaction network
Citric acid cycle. Medical search
Severe Pantothenic Acid Deficiency Induces Alterations in the Intestinal Mucosal Proteome of Starter Pekin Ducks | Research...
Glossary | Arthur Kornberg - Profiles in Science
"sequence id","alias","species","description",...
Glossary | Arthur Kornberg - Profiles in Science
Frontiers | Phylogenomics and Comparative Genomic Studies Robustly Support Division of the Genus Mycobacterium into an Emended...
1 - London drug trading
Nutrients | Free Full-Text | Towards an Integrative Understanding of tRNA Aminoacylation-Diet-Host-Gut Microbiome Interactions...
SMART: Pfam domain S-AdoMet synt C
Posttranscriptional Processing
AMINOACYL TRNA SYNTH1
- This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. (nih.gov)
Enzyme10
- Multisubunit enzyme complexes that synthesize ADENOSINE TRIPHOSPHATE from energy sources such as ions traveling through channels. (nih.gov)
- Glutamine-dependent NAD+ synthetase is an essential enzyme and a validated drug target in Mycobacterium tuberculosis (mtuNadE). (cornell.edu)
- The encoded enzyme catalyzes the ATP-dependent ligation of L-leucine to tRNA(Leu). (nih.gov)
- Note how protein factors bind not only to their recognition sequences but also to each other and to RNA polymerase, itself a very large and complex enzyme. (happylibus.com)
- is that synthase is (enzyme) any enzyme that catalyzes the synthesis of a biological compound but, unlike synthetases, does not make use of atp as a source of energy while synthetase is (enzyme) any ligase that synthesizes biological compounds using atp as a source of energy. (moviecultists.com)
- The ATP synthase is a mitochondrial enzyme localized in the inner membrane, where it catalyzes the synthesis of ATP from ADP and phosphate, driven by a flux of protons across a gradient generated by electron transfer from the proton chemically positive to the negative side. (moviecultists.com)
- ATP synthase is a ubiquitous, highly conserved enzyme that catalyses the formation of ATP from ADP and P i using a unique rotary motor mechanism. (moviecultists.com)
- In glutamine metabolism, by contrast, the activity of its key enzyme, glutamine synthetase, is regulated by the two systems of interconvertible enzyme cycles, which are tightly linked. (nih.gov)
- Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. (pbit.co.in)
- The synthesis begins with carbon dioxide and ammonia combining to form carbamoyl phosphate catalysed by the cytosolic enzyme carbamoyl phosphate synthetase-II. (pbit.co.in)
Hydrolysis7
- It catalyses the ATP-dependent formation of NAD+ from NaAD+ (nicotinic acid-adenine dinucleotide) at the synthetase active site and glutamine hydrolysis at the glutaminase active site. (cornell.edu)
- ATP-citrate lyase (ACLY) catalyzes the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, coupled with the hydrolysis of ATP. (rcsb.org)
- A synthase is also acknowledged as a lyase that catalyzes the cleavage of various chemical bonds through means excluding hydrolysis and oxidation without demand for any energy, whereas a synthetase is a ligase joining two chemicals or compounds with requirement for energy . (moviecultists.com)
- Kinases are enzymes that couple the hydrolysis of ATP to the addition of a phosphate group to its substrate. (moviecultists.com)
- Reactions in which it participates are often driven in the direction leading to hydrolysis (reaction with water) of ATP. (nih.gov)
- Transcription factor Rho is a ring-shaped, homohexameric protein that causes transcript termination through actions on nascent RNAs that are coupled to ATP hydrolysis. (embl-heidelberg.de)
- Escherichia coli transcription termination factor Rho is a ring-shaped hexameric protein that uses the energy derived from ATP hydrolysis to dissociate RNA transcripts from the ternary elongation complex. (embl-heidelberg.de)
Succinyl-CoA synthe1
- Residues 2-425 form three domains homologous to the beta-subunit of succinyl-CoA synthetase (SCS), while residues 487-820 form two domains homologous to the alpha-subunit of SCS. (rcsb.org)
Mitochondrial2
- The aryl hydrocarbon receptor interacts with ATP5α1, a subunit of the ATP synthase complex, and modulates mitochondrial function. (nih.gov)
- The protons return to the mitochondrial matrix through the process of chemiosmosis through the protein ATP synthase . (bionity.com)
Coli2
- Identification of an RNA-binding Site in the ATP binding domain of Escherichia coli Rho by H2O2/Fe-EDTA cleavage protection studies. (embl-heidelberg.de)
- RNA passes through the hole of the protein hexamer in the complex with the Escherichia coli Rho factor. (embl-heidelberg.de)
Ribosome-nascent chain1
- Syroegin, E. A. , Aleksandrova, E. V. , and Polikanov, Y. S. (2022) Insights into the ribosome function from the structures of non-arrested ribosome-nascent chain complexes . (cornell.edu)
Citrate1
- Because this is the first structure of any member of the acyl-CoA synthetase (NDP-forming) superfamily in complex with its organic acid substrate, locating the citrate-binding site is significant for understanding the catalytic mechanism of each member, including the prototype SCS. (rcsb.org)
Bacteria1
- In bacteria there is a single isoform of AdoMet synthetase (gene metK), there are two in budding yeast (genes SAM1 and SAM2) and in mammals while in plants there is generally a multigene family. (embl.de)
Induces2
- In our models, the dietary tryptophan metabolite tryptamine produced by human gut microbiome induces tryptophanyl-tRNA synthetase (TrpRS) deficiency with consequent neurodegeneration in cells and mice. (mdpi.com)
- Mechanistically, arginine starvation induces asparagine synthetase (ASNS), depleting these cancer cells of aspartate, and disrupting their malate-aspartate shuttle. (nature.com)
Synthase complex1
- TAP of the AHR, followed by mass spectrometry (MS) identified ATP5α1, a subunit of the ATP synthase complex, as a strong AHR interactor in the absence of ligand. (nih.gov)
Substrates1
- In the present paper, we report the structures of the inactive glutaminase C176A variant in an apo form and in three synthetase-ligand complexes with substrates (NaAD+/ATP), substrate analogue {NaAD+/AMP-CPP (adenosine 5'-[α,β-methylene]triphosphate)} and intermediate analogues (NaAD+/AMP/PPi), as well as the structure of wild-type mtuNadE in a product complex (NAD+/AMP/PPi/glutamate). (cornell.edu)
Glutamine2
- Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase. (cornell.edu)
- 26 Pyrimidine nucleosides and bases can be either synthesized de novo from glutamine, aspartic acid, ATP, and bicarbonate, or they can be salvaged from the environment (Fig. Another important site of regulation is the inosinate branch point. (pbit.co.in)
Nucleoside2
- ATP, or Adenosine triphosphate -- Nucleoside triphosphate composed of adenine, ribose, and three phosphate groups that is the primary carrier of chemical energy in cells. (nih.gov)
- Under the original definition, synthases do not use energy from nucleoside triphosphates (such as ATP, GTP, CTP, TTP, and UTP), whereas synthetases do use nucleoside triphosphates. (moviecultists.com)
Proteins5
- The protein coding genes include 14 genes in the respiratory complexes, four ATP synthetase genes, 16 ribosomal proteins genes, a tatC translocase gene, six conserved ORFs and a unique orf402. (usda.gov)
- Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. (string-db.org)
- The past few years have witnessed remarkable progress in knowledge of the structure and function of RNA-binding proteins and their RNA complexes. (embl-heidelberg.de)
- X-ray crystallography and NMR spectroscopy have provided structures for all major classes of RNA-binding proteins, both alone and complexed with RNA. (embl-heidelberg.de)
- A variety of regulatory proteins including DNA methyltransferases, methyl-CpG binding proteins, histone- modifying enzymes, chromatin remodeling factors, and their multimolecular complexes are involved in the overall epigenetic process. (nih.gov)
Adenosine diphosphate1
- An important carrier of energy in cells, ATP is formed from adenosine diphosphate (ADP) by an oxidation reaction in mitochondria, or by a photo reaction in plants. (nih.gov)
Catalyzes2
- Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. (nih.gov)
- A complex protein which catalyzes a specific biochemical reaction without changing itself. (nih.gov)
Subunit1
- The enzymatic activity of this multi-subunit complex resides in its catalytic core composed of RPA194, RPA135, and RPA12, a subunit with functions in RNA cleavage, transcription initiation and elongation. (bvsalud.org)
Interacts2
- It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginine tRNA synthetase through its C-terminal domain. (nih.gov)
- Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. (string-db.org)
Ligase1
- ligase , also called Synthetase, any one of a class of about 50 enzymes that catalyze reactions involving the conservation of chemical energy and provide a couple between energy-demanding synthetic processes and energy-yielding breakdown reactions. (moviecultists.com)
Dinucleotide2
20181
- In eukaryotes, especially in animals, this machinery is complex and sophisticated, involving large, multi-component protein factors that assist in the operation of eukaryotic ribosomes ( Hashem and Frank, 2018 ). (elifesciences.org)
Bound1
- upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. (string-db.org)
Pyruvate2
- In order to enter the Kreb's Cycle pyruvate must first be converted into Acetyl-CoA by pyruvate dehydrogenase complex found in the mitochondria. (libretexts.org)
- In order for pyruvate from glycolysis to enter the Kreb's Cycle it must first be converted into acetyl-CoA by the pyruvate dehydrogenase complex which is an oxidative process wherein NADH and CO 2 are formed. (libretexts.org)
Molecule1
- The generic name for numerous enzymes that are specific for the transfer of an adenylyl group (adenosine[mono]phosphor group) from a donor molecule (usually adenosine triphosphate, ATP) to an acceptor, such as a nucleotide, a protein, and a sugar. (nih.gov)
Species2
Enzymes2
- Made up of a complex of amino-acids, enzymes are part of every chemical reaction in living things. (nih.gov)
- Which enzymes are also called as synthetase? (moviecultists.com)
Cleavage2
- The binding of ATP caused one distinct change in the cleavage pattern, a strong protection at a cleavage point in the P-loop of the ATP binding domain. (embl-heidelberg.de)
- RNA molecules but not DNA molecules also caused a strong, ATP-dependent protection at a cleavage site in the predicted Q-loop of the ATP binding domain. (embl-heidelberg.de)
Structures1
- Variation in the number and radius of the tunnel constrictions is apparent in the crystal structures and is related to ligand binding at the synthetase domain. (cornell.edu)
Form2
- Two phosphates are added to AMP to form ATP. (nih.gov)
- In the proposed quaternary structure of Rho, the Q-loops from the six subunits form the upper entrance to the hole in the ring-shaped hexamer through which the nascent transcript is translocated by actions coupled to ATP hydrolyses. (embl-heidelberg.de)
Transcriptional1
- The growth of GBM cells depends on the core transcriptional apparatus, thus rendering RNA polymerase (RNA pol) complex as a candidate therapeutic target. (bvsalud.org)
Domain3
- The Rho polypeptide has a distinct RNA binding domain of known structure as well as an ATP binding domain for which a structure has been proposed based on homology modeling. (embl-heidelberg.de)
- Besides the site composed of multiples of the RNA binding domain, to which single-stranded DNA as well as RNA can bind, it has a separate, RNA-specific site on the Q-loop in the ATP binding domain. (embl-heidelberg.de)
- and 3) near the proposed secondary RNA-binding site in the ATP-binding domain (Cys-325 Rho). (embl-heidelberg.de)
Electron2
- 15. Modulations of the reduction potentials of flavin-based electron bifurcation complexes and semiquinone stabilities are key to control directional electron flow. (nih.gov)
- ATP synthase is a complex which makes use of the proton potential created by the action of the electron transport chain in mitochondria . (moviecultists.com)
Soluble1
- Isolated fractions were examined for their capacity to bind [125I]C1q as a measure of immune complex levels, and for their ability to bind soluble tumour-specific antigen as well as to react with antigens expressed at the surface of viable hepatoma cells. (nih.gov)
Energy1
- It transports a proton down the gradient and uses the energy to complete the phosphorylation of ADP to ATP. (moviecultists.com)
Found1
- Although complex, translation in eukaryotes conserves four main phases that are also found in its prokaryotic counterparts, namely: initiation, elongation, termination and recycling ( Schmeing and Ramakrishnan, 2009 ). (elifesciences.org)
Active1
- and (iii) at the end near the synthetase active site. (cornell.edu)
Cells1
- ATP also participates in numerous synthetic reactions in cells. (nih.gov)
Structure2
- Comparisons of the nucleotide-binding site of SCSs with the similar structure in ACLY indicates that this is the ATP-binding site of ACLY. (rcsb.org)
- Our model of the CSD(FRG)-RNA complex constitutes the first prediction of the three-dimensional structure of a CSD-RNA complex and is consistent with the hypothesis of a convergent evolution of CSD and RRM towards a related single-stranded RNA-binding surface. (embl-heidelberg.de)
Made1
- How is ATP synthase made? (moviecultists.com)