Reference to 1.1.98.6; Id = 741351 - BRENDA Enzyme Database

iron-sulfur center

in its active form, the enzyme contains an iron-sulfur center and an oxygen-sensitive glycyl radical (Gly681)

Escherichia coli

P28903

-

ribonucleoside 5'-triphosphate + formate

-

741351

Escherichia coli

2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O

in its active form, the enzyme contains an iron-sulfur center and an oxygen-sensitive glycyl radical (Gly681). The radical is generated in the inactive protein from S-adenosylmethionine by an auxiliary enzyme system. During catalysis, formate is stoichiometrically oxidized to CO2, and isotope from [3H]formate appears in water

-

?

iron-sulfur center

in its active form, the enzyme contains an iron-sulfur center and an oxygen-sensitive glycyl radical (Gly681)

Escherichia coli

ribonucleoside 5'-triphosphate + formate

-

741351

Escherichia coli

2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O

in its active form, the enzyme contains an iron-sulfur center and an oxygen-sensitive glycyl radical (Gly681). The radical is generated in the inactive protein from S-adenosylmethionine by an auxiliary enzyme system. During catalysis, formate is stoichiometrically oxidized to CO2, and isotope from [3H]formate appears in water

-

?

740573

Wei

A chemically competent thiosul ...

Escherichia coli

J. Am. Chem. Soc.

136

9001-9013

2014

-

1

-

1

-

2

-

1

-

2

-

740969

Kirdis

Ribonucleotide reductase class ...

Staphylococcus aureus, Staphylococcus aureus Newman

Microb. Pathog.

43

179-188

2007

-

1

-

2

-

1

-

1

-

660352

Logan

A metal-binding site in the ca ...

Escherichia virus T4, Escherichia coli

Proc. Natl. Acad. Sci. USA

100

3826-3831

2003

-

1

4

-

2

-

4

-

1

4

-

2

-

740670

Torrents

The anaerobic ribonucleotide r ...

Lactococcus lactis subsp. cremoris

J. Biol. Chem.

276

33488-33494

2001

4

-

1

-

1

-

5

-

4

1

2

-

4

-

1

-

1

-

4

1

-

2

-

740895

Cho

-

The substrate reaction mechani ...

Escherichia coli

J. Phys. Chem. B

105

6445-6452

2001

-

1

-

1

-

1

-

740665

Andersson

Allosteric regulation of the c ...

Escherichia virus T4

J. Biol. Chem.

275

19443-19448

2000

5

-

6

-

6

-

10

-

5

-

5

-

6

-

10

-

5

-

740666

Andersson

Cysteines involved in radical ...

Escherichia virus T4

J. Biol. Chem.

275

19449-19455

2000

-

1

-

10

-

5

-

1

-

10

-

740769

Mulliez

Iron-sulfur interconversions i ...

Escherichia coli

J. Biol. Inorg. Chem.

4

614-620

1999

-

4

-

1

-

1

-

1

-

740662

Olcott

Localization and characterizat ...

Escherichia virus T4

J. Biol. Chem.

273

24853-24860

1998

-

1

-

1

-

5

-

1

-

1

-

1

-

1

-

1

-

740660

Ollagnier

Activation of the anaerobic ri ...

Escherichia coli

J. Biol. Chem.

272

24216-24223

1997

-

4

-

2

-

2

-

740659

Ollagnier

The anaerobic Escherichia coli ...

Escherichia coli

J. Biol. Chem.

271

9410-9416

1996

-

1

-

2

-

1

-

2

-

1

-

1

-

2

-

2

-

739975

Eliasson

The mechanism of the anaerobic ...

Escherichia coli

Biochem. Biophys. Res. Commun.

214

28-35

1995

-

3

-

1

-

1

-

1

-

1

-

741351

Mulliez

Formate is the hydrogen donor ...

Escherichia coli

Proc. Natl. Acad. Sci. USA

92

8759-8762

1995

-

1

-

3

-

1

-

1

-

1

-

740656

Eliasson

Allosteric control of the subs ...

Escherichia coli

J. Biol. Chem.

269

26052-26057

1994

-

2

6

-

3

-

5

-

2

-

2

6

-

5

-

740653

Mulliez

An iron-sulfur center and a fr ...

Escherichia coli

J. Biol. Chem.

268

2296-2299

1993

-

3

-

1

-

2

-

2

-

1

-

740651

Eliasson

Characterization of components ...

Escherichia coli

J. Biol. Chem.

267

25541-25547

1992

1

-

5

-

2

-

3

-

1

-

1

-

1

2

-

1

-

5

-

2

-

1

-

1

-

1

2

-

1

-

741348

Eliasson

The anaerobic ribonucleoside t ...

Escherichia coli

Proc. Natl. Acad. Sci. USA

87

3314-3318

1990

-

1

-

1

-

1

-

1

-

1

-

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli

Data extracted from this reference: