Document Type: Article All Authors / Contributors: Ha S.C.; Hwang E.Y.; Kim E.-A.; Cho S.-W.; Son H.J.; Ahn J.-Y.; Choi S.Y. ISSN:1976-6696 Language Note: English Unique Identifier: 825798451 Awards:
| Title | : | Roles of cysteine residues in the inhibition of human glutamate dehydrogenase by palmitoyl-CoA |
| Author | : | Ha S.C.; Hwang E.Y.; Kim E.-A.; Cho S.-W.; Son H.J.; All authors |
| Language | : | en |
| Rating | : | 4.90 out of 5 stars |
| Type | : | PDF, ePub, Kindle |
| Uploaded | : | Apr 12, 2021 |
Full Download Roles of cysteine residues in the inhibition of human glutamate dehydrogenase by palmitoyl-CoA - Ha S.C.; Hwang E.Y.; Kim E.-A.; Cho S.-W.; Son H.J.; All authors | PDF
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1489 949 1283 4149 680 4353 3996 2532 4913 3294 1428 3155 1603 1804 4152 2124 4767 1988
The disulphide bonds of cystine are crucial to defining the structures of many proteins. Disulfide bonds play an important role in the folding and stability of some.
The role of cysteine residues in the transport of mercuric ions by the tn501 mert and merp mercury-resistance proteins.
Cysteine residues are critical to activity and structure of sr protein resolving as dimeric in gel-filtration chromatography could potentially include covalent and/or noncovalent dimers. Human sr has eight cysteine residues, creating ample opportunity for a variety of redox-based modifications including disulfide bonds.
The haemagglutinin (h) protein is the dominant en- velope glycoprotein of measles virus. The protein contains 13 cysteine residues among its 617 amino acids.
The biochemical literature is replete with studies claiming an essential role for sulfhydryl groups in the activity of particular enzymes. These conclusions are usually based on studies utilizing agents, such as p-chloromercuribenzoate or iodoacetate, that alkylate the sulfhydryl moiety on cysteine residues.
Ncr amps are cationic and have conserved cysteine residues, which form disulfide (s–s) bridges. However, the natural configuration of ncr amp s–s bridges and the role of these in the activity of the peptide are unknown.
Role of extracellular cysteine residues in the adenosine a2a receptor purinergic signal.
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In order to get a detailed view on the role of extracellular disulfide bonds of the a 2a ar, we generated mutant a 2a receptors in which cysteine residues were exchanged with serine (c146s, c159s, c166s, and a double mutant c146s-c159s) focusing on ligand binding and receptor function with various ligands (fig.
Cysteinum) — это алифатическая серосодержащая кислота. Цистеин считается условно незаменимой аминокислотой, которая активно.
While free cysteine residues do occur in proteins, most are covalently bonded to other cysteine residues to form disulfide bonds. Disulfide bonds play an important role in the folding and stability.
In this study, we investigated the role of cysteine residues that could potentially contribute to regulation of mtb pck specificity by the change of reducing conditions. We identified critical cysteine residues in positions 391 and 397 that significantly contribute to protein stability and consequently to mtb pck activity.
Together, the results suggested that free thiol groups, but not disulphide bonding, of seven cysteine residues within the intracisternal region of human ugt1a1 are important for its catalytic activity, while cysteine residues in the cytosolic domain may be involved in its physiological activation by udp-glcnac.
In conclusion, cysteine residues 287, 300, 381, 394, 494, 579 and 583 appear to play a particularly critical role in the antigenic structure and processing of the h molecules and they probably participate in the inter- or intramolecular disulphide bonding.
Non-catalytic cysteine residues can work synergistically to protect proteins againstoxidativedamage. Italsoshows that once expressed either in the sur-face or buried, non-catalytic cysteine residues play a critical role and can thereforebevalidatedasdrug-oriented targets. At last, i would like to express my sincere gratitude for and acknowledge.
Cysteine residues fragment was then subcloned into bluescript vector (stratagene, la jolla, ca) and the entire mutant fragment was verified by dna also can form intermolecular disulphide bonds with sequencing (37). Other proteins, leading to the assembly of multiprotein yeast two-hybrid analyses.
Apr 5, 2010 serine proteases provide a nice example of rational design of inhibitors based on the catalytic mechanism of an enzyme.
Cysteine residues are shown to play important roles in the folding of proteins (branden and tooze 1999). C155 in mtb ftsz might be involved in proper folding of protein and the modification or the mutation of the cysteine residue may induce a conformational change in mtb ftsz (discussed below).
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It also shows that once expressed either in the surface or buried, non-catalytic cysteine residues play a critical role and can therefore be validated as drug-oriented targets. Figure 1 schematics of the proposed water-bridged cysteine-cysteine redox regulation mechanism in protein tyrosine phosphatases.
Over 1500 cysteine residues from ∼450 mitochondrial proteins were identified, thereby enabling interrogation of an unprecedented number of mitochondrial cysteines. Specifically, these mitochondrial cysteines were ranked by reactivity to identify hyper-reactive cysteines with potential catalytic and regulatory functional roles.
If tehb is pre-exposed to incubation in sds buffer then tellurite binding prohibits nem protein reactivity, which suggests that nem and tellurite may be reacting with the same cysteine residue. It is clear from these results that soft-ion thiol chemistry plays a role in the biochemical mechanism of the teh te r determinant.
Although the role of arginine and lysine residues in the enhancement of chaperone function has been investigated, the role of cysteine residues is yet to be determined. In this study, we have investigated the effect of mgo modification on the structure and chaperone function of αa-crystallin mutant proteins in which c131 and c142 were replaced.
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Nov 11, 2014 chapter 3 the roles of cysteine residues in lysylation and ap4a synthesis by human lysyl-trna synthetase.
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He and his multidisciplinary research lab study the roles of cys residues in eukaryotic protein kinases.
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However, the role of the individual cysteine residues in human ugt1a1 has not been delineated systematically. It is also unknown whether function of the cysteine residues is exerted via disulphide bonding or by cysteine residues with free thiol groups.
We examined the role of cysteines in their the v(v)-reductase activity of vanabin2. • when all eighteen cysteine residues were substituted, the activity was lost. • substitutions of three sets of cysteines resulted in a moderate decrease. • more than a single cysteine pair is responsible for the v(v)-reductase activity.
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Schiedel ac, hinz s, thimm d, sherbiny f, borrmann t, maass a et al (2011) the four cysteine residues in the second extracellular loop of the human adenosine a 2b receptor: role in ligand binding and receptor function.
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Oct 1, 2019 analysis of germline gene segments reveals noncanonical cysteines in the hc v regions and significant cysteine content in the hc d regions.
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These results suggested that cysteine residues in the protein could have a role in stabilization or in catalysis. Ecop15i dna mtase, a 645-amino acid protein, contains six cysteine residues at positions 30, 213, 344, 434, 553, and 577 as deduced from the dna sequence of the mod gene (fig.
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In this study we determined the role of cysteine residues in the oxidation of ferritin. Loading iron into recombinant human ferritin by its own ferroxidase activity decreased its conjugation by a cysteine specific spin label, indicating that cysteine residues were altered during iron loading.
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Furthermore, in double and triple mutants where two or three cysteine residues were replaced by serine, all such mutants in which the cysteine at position 344 was changed, were inactive. Taken together, these results convincingly demonstrate that the cys-344 is necessary for enzyme activity and indicate an essential role for it in dna binding.
A beta turn is a turn in the primary structure, stabilized by hydrogen bonding. Because proline has an odd, cyclic structure, when it forms peptide bonds, it induces.
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