Literature summary extracted from

Tong, W.; Burdi, D.; Riggs-Gelasco, P.; Chen, S.; Edmondson, D.; Huynh, V.; Stubbe, J.; Han, S.; Arvai, A.; Tainer, J.
Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography (1998), Biochemistry, 37, 5840-5848.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.17.4.1	expression of Y122F, Y356F and Y122F/Y356F mutant enzymes in Escherichia coli	Escherichia coli

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.17.4.1	Y122F	mutant enzyme cannot generate a Y122 tyrosyl radical necessary for catalysis, 0.5% of wild-type activity	Escherichia coli
1.17.4.1	Y122F/Y356F	0.5% of wild-type activity	Escherichia coli
1.17.4.1	Y356F	similar properties as wild-type	Escherichia coli

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.17.4.1	Iron	proposed in vitro mechanism for the assembly of the diferric tyrosyl radical cofactor of subunit R2	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.17.4.1	Escherichia coli	P69924	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.17.4.1	ribonucleoside diphosphate + reduced thioredoxin	-	Escherichia coli	2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O	-	ir

Subunits

EC Number	Subunits	Comment	Organism
1.17.4.1	More	proposed in vitro mechanism for the assembly of the diferric tyrosyl radical cofactor of subunit R2	Escherichia coli

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Release 2023.1 (January 2023)