Rhodanaasi entsyymi on mitokondriaalinen ja katalysoi tiosulfaatin ja syanidin muuttumista tiosyanaatiksi ja sulfiitiksi. Siis aloittaa syanidin detoksikaatiota.
- Official Symbol
- TSTprovided by HGNC
- Official Full Name
- thiosulfate sulfurtransferaseprovided by HGNC
- Also known as
- RDS
- Summary
- This is one of two neighboring genes encoding similar proteins that each contain two rhodanese domains. The encoded protein is localized to the mitochondria and catalyzes the conversion of thiosulfate and cyanide to thiocyanate and sulfite. In addition, the protein interacts with 5S ribosomal RNA and facilitates its import into the mitochondria. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2012]
- Expression
- Broad expression in colon (RPKM 83.2), liver (RPKM 73.2) and 22 other tissues See more
- Orthologs mouse all
- Polymorphic Variants of Human Rhodanese Exhibit Differences in Thermal Stability and Sulfur Transfer Kinetics. Libiad M, et al. J Biol Chem, 2015 Sep 25. PMID 26269602, Free PMC Article
- Decreased mucosal sulfide detoxification capacity in patients with Crohn's disease. Arijs I, et al. Inflamm Bowel Dis, 2013 Apr. PMID 23399736
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Assessment of cassava toxicity in patients with tropical chronic pancreatitis.
Girish BN, et al. Trop Gastroenterol, 2011 Apr-Jun. PMID 21922874There have been conflicting reports on the role of cassava ingestion in tropical pancreatitis (TCP). In this study we aimed to estimate cyanogens detoxifying enzyme rhodanese, thiocyanate and sulfur containing amino acids in cassava consumer as well as cassava non-consumer TCP patients and healthy controls and compare the same.
Eighty-six TCP patients and 90 healthy controls were recruited. Serum rhodanese, thiocyanate, plasma amino acids, urinary inorganic sulfate/creatinine were measured.
There was significant reduction in serum rhodanese activity in both cassava consumer- and non-consumer TCP patients as compared to controls but no significant difference between cassava consumer- and non-consumer TCP patients was observed. Serum thiocyanate was significantly lower in cassava consumer TCP patients as compared to cassava consumer controls but not significantly different from cassava non-consumer TCP patients. Plasma methionine, cysteine and urinary inorganic sulfate / creatinine ratio was significantly lower in both cassava consumer and non-consumer TCP patients as compared to controls but were comparable among cassava consumers and non-consumers.
Significant reduction in rhodanese activity with concomitant decrease in sulfur containing amino acids and antioxidants such as glutathione suggests that TCP patients are at higher risk of defective detoxification of cyanogens. However there was no difference between cassava consumers and non-consumers. Low levels of sulfur amino acids may contribute to the development of pancreatitis. - Thiol levels, protein carbonylation and anaerobic sulfur metabolism in erythrocytes of peritoneal dialysis and predialysis patients. Włodek P, et al. Nephrology (Carlton), 2010 Dec. PMID 21175961
- Evidence for a functional genetic polymorphism of the human thiosulfate sulfurtransferase (Rhodanese), a cyanide and H2S detoxification enzyme. Rhodanese or thiosulfate sulfurtransferase (TST) is a mitochondrial matrix enzyme that plays roles in cyanide detoxification, the formation of iron-sulfur proteins and the modification of sulfur-containing enzymes. Transsulfuration reaction catalyzed by TST is also involved in H(2)S detoxification. To date, no polymorphism of the human TST gene had been reported. We developed a screening strategy based on a PCR-SSCP method to search for mutations in the 3 exons of TST and their proximal flanking regions. This strategy has been applied to DNA samples from 50 unrelated French individuals of Caucasian origin. Eleven polymorphisms consisting in seven nucleotide substitutions in non-coding regions, two silent mutations and two missense mutations were characterized. The functional consequences of the identified mutations were assessed in vivo by measurement of erythrocyte TST activity and/or in vitro using heterologous expression in Saccharomyces cerevisiae or transient transfection assay in HT29 and Caco-2 cell lines. The P(285)A variant appears to encode a protein with a 50% decrease of in vitro intrinsic clearance compared to the wild-type enzyme. Additionally, the six polymorphisms located upstream the ATG initiation codon are responsible for a significant decrease (ranging from 40% to 73%) in promoter activity of a reporter gene compared to the corresponding wild-type sequence. This work constitutes the first report of the existence of a functional genetic polymorphism affecting TST activity and should be of great help to investigate certain disorders for which impairment of CN(-) or H(2)S detoxification have been suggested to be involved.
Ubiquitin-specific
protease 8 (USP8) (DUB) hydrolyzes mono and polyubiquitylated targets such as
epidermal growth factor receptors (EGFR) and is involved in clathrin-mediated
internalization. In 1182 residues, USP8 contains multiple domains,
including coiled-coil, rhodanese, and catalytic domains. We report the
first high-resolution crystal structures of these domains and discuss
their implications for USP8 function. The amino-terminal domain is a
homodimer with a novel fold. It is composed of two five-helix bundles,
where the first helices are swapped, and carboxyl-terminal helices are
extended in an antiparallel fashion. The structure of the rhodanese
domain, determined in complex with the E3 ligase NRDP1, reveals the
canonical rhodanese fold but with a distorted primordial active site.
The USP8 (DUB) recognition domain of NRDP1 (RNF41) has a novel protein fold that
interacts with a conserved peptide loop of the rhodanese domain. A
consensus sequence of this loop is found in other NRDP1 targets,
suggesting a common mode of interaction. The structure of the
carboxyl-terminal catalytic domain of USP8 exhibits the conserved
tripartite architecture but shows unique traits. Notably, the active
site, including the ubiquitin binding pocket, is in a closed
conformation, incompatible with substrate binding. The presence of a
zinc ribbon subdomain near the ubiquitin binding site further suggests a
polyubiquitin-specific binding site and a mechanism for substrate
induced conformational changes.
- E3 ubikitiiniligaasi RNF41 https://www.ncbi.nlm.nih.gov/gene/10193
- Data (including data from studies using knockout and transgenic mice/cells) suggest that CLEC16A, NRDP1, and USP8 form tripartite complex; CLEC16A-NRDP1-USP8 complex appears to rely on ubiquitin signals to promote mitophagy and maintain mitochondrial function necessary for beta-cell function. (CLEC16A = C-type lectin domain family 16 member A; NRDP1 = ubiquitin-protein ligase NRDP1; USP8 = ubiquitin specific peptidase 8)
- USP8
- Also known as
- UBPY; PITA4; SPG59; HumORF8
- Summary This gene encodes a protein that belongs to the ubiquitin-specific processing protease family of proteins. The encoded protein is thought to regulate the morphology of the endosome by ubiquitination of proteins on this organelle and is involved in cargo sorting and membrane trafficking at the early endosome stage. This protein is required for the cell to enter the S phase of the cell cycle and also functions as a positive regulator in the Hedgehog signaling pathway in development. Pseudogenes of this gene are present on chromosomes 2 and 6. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]
- Expression Ubiquitous expression in testis (RPKM 16.5), thyroid (RPKM 12.8) and 25 other tissues See more
- NP_001122082.1 ubiquitin carboxyl-terminal hydrolase 8 isoform a
- Conserved Domains (5) summary
-
- smart00450
Location:199 → 310 - RHOD; Rhodanese Homology Domain An alpha beta fold found duplicated in the Rhodanese protein. The Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
- TIGR02794
Location:375 → 547 - tolA_full; TolA protein
- pfam00443
Location:777 → 1106 - UCH; Ubiquitin carboxyl-terminal hydrolase
- pfam08969
Location:8 → 115 - USP8_dimer; USP8 dimerisation domain
- pfam10243
Location:474 → 646 - MIP-T3; Microtubule-binding protein MIP-T3
- smart00450
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