Literature summary for 1.17.4.1 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.

Search for more literature for 1.17.4.1

Cloned(Commentary)

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

Protein Variants

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P69924	-	-

Substrates and Products (Substrate)

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

Subunits

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)