Literature summary for 2.8.1.7 extracted from

Cai, K.; Tonelli, M.; Frederick, R.O.; Markley, J.L.
Human mitochondrial ferredoxin 1 (FDX1) and ferredoxin 2 (FDX2) both bind cysteine desulfurase and donate electrons for iron-sulfur cluster biosynthesis (2017), Biochemistry, 56, 487-499 .

Search for more literature for 2.8.1.7

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y697	-	-

Synonyms

Synonyms	Comment	Organism
Nfs1	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	ferredoxins FDX1 and FDX2 in both their reduced and oxidized states interact with the protein complex responsible for mitochondrial iron-sulfur cluster assembly, which contains cysteine desulfurase (NFS1), ISD11 (LYRM4), and acyl carrier protein (Acp). Reduced FDX1 and FDX2 each donate electrons to the cysteine desulfurase complex in vitro and facilitate iron-sulfur cluster assembly. Ferredoxin Both FDX1 and FDX2 stimulate cysteine desulfurase activity. FDX2 binds more tightly to the cysteine desulfurase complex than FDX1 does. The reduced form of each ferredoxin becomes oxidized in the presence of the cysteine desulfurase complex when L-cysteine is added, leading to its conversion to L-alanine and the generation of sulfide	Homo sapiens

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Release 2023.1 (January 2023)