Results 21 to 30 of about 7,672 (250)

Bacterial Isothiocyanate Biosynthesis by Rhodanese‐Catalyzed Sulfur Transfer onto Isonitriles

open access: yesChemBioChem, 2023
Natural products bearing isothiocyanate (ITC) groups are an important group of specialized metabolites that play various roles in health, nutrition, and ecology. Whereas ITC biosynthesis via glucosinolates in plants has been studied in detail, there is a
Mandy D Mlotek   +2 more
semanticscholar   +1 more source

Sulfur Administration in Fe–S Cluster Homeostasis

open access: yesAntioxidants, 2021
Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters.
Leszek Rydz   +2 more
doaj   +1 more source

Isolation and statistical optimization of rhodanese (a thiosulphate sulphur transferase) production potential of Klebsiella oxytoca JCM 1665 using response surface methodology

open access: yesNova Biotechnologica et Chimica, 2022
Microorganisms are increasingly being used in cyanide bioremediation. Several organisms have been reported to thrive in cyanide contaminated wastewater due to their ability to produce cyanide detoxifying enzymes.
B. Itakorode, R. Okonji
semanticscholar   +1 more source

Transfer RNA Bound to MnmH Protein Is Enriched with Geranylated tRNA--A Possible Intermediate in Its Selenation? [PDF]

open access: yesPLoS ONE, 2016
The wobble nucleoside 5-methylaminomethyl-2-thio-uridine (mnm5s2U) is present in bacterial tRNAs specific for Lys and Glu and 5-carboxymethylaminomethyl-2-thio-uridine (cmnm5s2U) in tRNA specific for Gln.
Gunilla Jäger   +2 more
doaj   +1 more source

Rhodanese Rdl2 produces reactive sulfur species to protect mitochondria from reactive oxygen species.

open access: yesFree Radical Biology & Medicine, 2021
Mitochondria damage is related to a broad spectrum of pathologies including Alzheimer's, Parkinson's disease, and carcinogenesis. Recently, it has been found that reactive sulfur species (RSS) has a close connection with mitochondrial health.
Qingda Wang   +6 more
semanticscholar   +1 more source

Evaluation of the activity of cyanide-metabolizing sulfurtransferase enzymes in different tissues of turkey (Meleagris gallopavo) [PDF]

open access: yesThe Iranian Journal of Veterinary Science and Technology, 2015
This study was undertaken to estimate specific activities of rhodanese and 3-mercaptopyruvate sulfurtransferase (MST) in different tissues of turkey.
Kamal JalilianKabiri, Hassan Baghishani
doaj   +1 more source

Characterization of Rhodanese Extracted from Synodontis schall Liver

open access: yesEAS Journal of Nutrition and Food Sciences, 2022
Rhodanese, a cyanide detoxifying enzyme was extracted from the liver of Synodontis schall and its characteristics investigated. Crude enzyme preparation was prepared and the enzyme was assayed by measuring the activity of rhodanese in RU min-1 mg-1.
E. Wodu   +3 more
semanticscholar   +1 more source

Environmental risk assessments of uses cyanide in gold extraction on water quality parameters and its effect on rhodanese activities in selected organs of coptodon zillii in igun reservoir, Southwestern, Nigeria

open access: yesOpen Access Journal of Science, 2022
This study was conducted to investigate the effect of cyanide on the pattern of rhodanese activity distribution in selected organs of Coptodon zillii and water quality of Igun reservoir.
Oluwakemi Victoria Okunola   +5 more
semanticscholar   +1 more source

Urm1: A Non-Canonical UBL

open access: yesBiomolecules, 2021
Urm1 (ubiquitin related modifier 1) is a molecular fossil in the class of ubiquitin-like proteins (UBLs). It encompasses characteristics of classical UBLs, such as ubiquitin or SUMO (small ubiquitin-related modifier), but also of bacterial sulfur-carrier
Martin Termathe, Sebastian A. Leidel
doaj   +1 more source

The titration of rhodanese with substrates [PDF]

open access: yesFEBS Letters, 1974
The transfer of sulfur catalyzed by rhodanese (EC 2.8.1 .l .) is thought to proceed through a double displacement mechanism where the enzyme is first charged with the donor sulfur and then discharged by the acceptor [ 1 ] . Earlier workers have reported that the enzyme accepts from 1 to 1.9 atoms of sulfur per mole of enzyme of mol. wt. of 37 000 (2-4).
Cannella, C.   +4 more
openaire   +2 more sources

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