硫氰酸酶
硫氰酸酶结构式
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常用名 | 硫氰酸酶 | 英文名 | Rhodanese from bovine liver |
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| CAS号 | 9026-04-4 | 分子量 | N/A | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | N/A | 熔点 | N/A | |
| MSDS | 美版 | 闪点 | N/A |
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Probing the functional mechanism of Escherichia coli GroEL using circular permutation.
PLoS ONE 6(10) , e26462, (2011) The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism. Here, we have used circular permutation to study the structural and functiona... |
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Effects of nitric oxide synthase deficiency on a disintegrin and metalloproteinase domain-containing protein 12 expression in mouse brain samples.
Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 154(3) , 180-6, (2011) A disintegrin and metalloproteinase domain-containing protein 12 (ADAM12) belongs to the ADAM family of transmembrane proteins. Via proteolysis, cell adhesion, cell-cell fusion, cell-matrix interaction and membrane protein shedding, ADAM proteins are involved... |
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Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
Protein Sci. 20(8) , 1380-6, (2011) Nuclear magnetic resonance (NMR) observation of the uniformly (2) H,(15) N-labeled stringent 33-kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1, was ach... |
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A novel rhodanese is required to maintain chloroplast translation in Chlamydomonas.
Plant Mol. Biol. 79(4-5) , 495-508, (2012) Rhodanese-domain proteins (RDPs) are widespread in plants and other organisms, but their biological roles are mostly unknown. Here we report on a novel RDP from Chlamydomonas that has a single rhodanese domain, and a predicted chloroplast transit peptide. The... |
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Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme.
FEBS Lett. 586(6) , 717-21, (2012) 5-Methylaminomethyl-2-selenouridine (mnm(5)Se(2)U) is found in the first position of the anticodon in certain tRNAs from bacteria, archaea and eukaryotes. This selenonucleoside is formed in Escherichia coli from the corresponding thionucleoside mnm(5)S(2)U by... |
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The effect of the uremic toxin cyanate (CNO⁻) on anaerobic cysteine metabolism and oxidative processes in the rat liver: a protective effect of lipoate.
Toxicol. Mech. Methods 21(6) , 473-8, (2011) Chronic renal failure (CRF) patients have an increased plasma level of urea, which can be a source of cyanate. This compound can cause protein carbamoylation thereby changing biological activity of proteins. Therefore, in renal failure patients, cyanate can d... |
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Rhodanese activity in different tissues of the ostrich.
Br. Poult. Sci. 53(2) , 270-3, (2012) 1. The purpose of this investigation was to determine the activity, and compare the pattern of distribution, of rhodanese (thiosulphate: cyanide sulphurtransferase, EC. 2.8.1.1) in different tissues of male and female ostriches. 2. Tissue samples from male an... |
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Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures.
Biosci. Rep. 32(3) , 299-303, (2012) The chaperonin GroEL binds to non-native substrate proteins via hydrophobic interactions, preventing their aggregation, which is minimized at low temperatures. In the present study, we investigated the refolding of urea-denatured rhodanese at low temperatures... |
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Crystal structure of the Tum1 protein from the yeast Saccharomyces cerevisiae.
Protein Pept. Lett. 19(11) , 1139-43, (2012) Yeast tRNA-thiouridine modification protein 1 (Tum1) plays essential role in the sulfur transfer process of Urm1 system, which in turn is involved in many important cellular processes. In the rhodanese-like domain (RLD), conserved cysteine residue is proved t... |
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Structural insight into the mode of interactions of SoxL from Allochromatium vinosum in the global sulfur oxidation cycle.
Mol. Biol. Rep. 39(12) , 10243-8, (2012) Microbial redox reactions of inorganic sulfur compounds are one of the important reactions for the recycling of sulfur to maintain the environmental sulfur balance. These reactions are carried out by phylogenetically diverse microorganisms. The sulfur oxidizi... |