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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
2.8.1.7
760457
Catalytic intermediate crystal structures of cysteine desulfurase from the archaeon Thermococcus onnurineus NA1
Archaea
2017
5395293
2017
Thermococcus onnurineus
28536498
2.8.1.7
761245
Cysteine desulfurase IscS2 plays a role in oxygen resistance in Clostridium difficile
Infect. Immun.
86
e00326
2018
Clostridioides difficile
29866903
2.8.1.7
761245
Cysteine desulfurase IscS2 plays a role in oxygen resistance in Clostridium difficile
Infect. Immun.
86
e00326
2018
Clostridioides difficile 630
29866903
2.8.1.7
761497
Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues
J. Biol. Chem.
294
12444-12458
2019
Escherichia coli
31248989
2.8.1.7
760243
Expression, purification and function of cysteine desulfurase from Sulfobacillus acidophilus TPY isolated from deep-sea hydrothermal vent
3 Biotech
7
360
2017
Sulfobacillus acidophilus
28979833
2.8.1.7
760243
Expression, purification and function of cysteine desulfurase from Sulfobacillus acidophilus TPY isolated from deep-sea hydrothermal vent
3 Biotech
7
360
2017
Sulfobacillus acidophilus TPY
28979833
2.8.1.7
760587
Human mitochondrial ferredoxin 1 (FDX1) and ferredoxin 2 (FDX2) both bind cysteine desulfurase and donate electrons for iron-sulfur cluster biosynthesis
Biochemistry
56
487-499
2017
Homo sapiens
28001042
2.8.1.7
761145
Hydrogen sulfide from cysteine desulfurase, not 3-mercaptopyruvate sulfurtransferase, contributes to sustaining cell growth and bioenergetics in E. coli under anaerobic conditions
Front. Microbiol.
10
2357
2019
Escherichia coli
31681220
2.8.1.7
761583
Localization and characterization of a putative cysteine desulfurase in Chlamydia psittaci
J. Cell. Biochem.
120
4409-4422
2019
Chlamydia psittaci
30260037
2.8.1.7
760523
Molecular basis of function and the unusual antioxidant activity of a cyanobacterial cysteine desulfurase
Biochem. J.
474
2435-2447
2017
Nostoc sp. PCC 7120 = FACHB-418
28592683
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