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Ligand N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2 = coenzyme B + coenzyme M + coenzyme F420

654386, 657172

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine = coenzyme B + coenzyme M + methanophenazine

639394

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2 = coenzyme B + coenzyme M

655400, 655398, 655396, 655825

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced cytochrome b = coenzyme B + coenzyme M + oxidized cytochrome b

655823

-

1.8.98.1

4 entries

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.98.1

coenzyme B + coenzyme M + methanophenazine = N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine

-

-

Substrate in Enzyme-catalyzed Reactions (16 results)

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Show Substrate (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2 = coenzyme B + coenzyme M + coenzyme F420

654386, 655532, 657172

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydro-2-hydroxyphenazine = coenzyme B + coenzyme M

655825

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine = coenzyme B + coenzyme M + methanophenazine

639394

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2 = coenzyme B + coenzyme M

655396, 655400, 655398, 655471, 655531, 655825, 654385, 639391

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced 2-bromophenazine = coenzyme B + coenzyme M + 2-bromophenazine

440299

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced 2-hydroxyphenazine = coenzyme B + coenzyme M + 2-hydroxyphenazine

440299

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzyl viologen = coenzyme B + coenzyme M + benzyl viologen

655396, 655416

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzylviologen = coenzyme B + coenzyme M + benzylviologen

639391

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced benzylviologen = coenzyme B + coenzyme M + oxidized benzyl viologen

655416

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced cytochrome b = coenzyme B + coenzyme M + oxidized cytochrome b

655823

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methyl viologen = coenzyme B + coenzyme M + methyl viologen

639394

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue = coenzyme B + coenzyme M + methylene blue

639391

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen = coenzyme B + coenzyme M + methyl viologen

655400, 440299

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen = coenzyme B + coenzyme M + methylviologen

639393, 654386

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylviologen = coenzyme B + coenzyme M + oxidized methylviologen

655823

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced phenazine-1-carboxylic acid = coenzyme B + coenzyme M + phenazine-1-carboxylic acid

440299

-

1.8.98.1

16 entries

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.98.1

coenzyme B + coenzyme M + methanophenazine = N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + dihydromethanophenazine

-

-

1.8.98.1

coenzyme B + coenzyme M + methylene blue = N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + reduced methylene blue

-

-

1.8.98.1

2 entries

Enzyme Kinetic Parameters

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.8.98.1

0.1

-

pH 7.6, 54°C

639391

1.8.98.1

0.13

-

pH 7.6, 65°C

639391

1.8.98.1

0.144

-

25°C

639394

1.8.98.1

0.2

-

pH 7, 65°C, H2: heterodisulfide oxidoreductase complex

655398

1.8.98.1

0.4

-

pH 7.0, 37°C, reaction with reduced benzyl viologen

655400

1.8.98.1

5 entries

References & Links

Literature References (16)

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Show Reference (16 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

440299

9555882

Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Go1

1998

Abken, H.J.; Tietze, M.; Brodersen, J.; Baumer, S.; Beifuss, U.; Deppenmeier, U.

J. Bacteriol.

180

2027-2032

639391

2121478

Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)

1990

Hedderich, R.; Berkessel, A.; Thauer, R.K.

Eur. J. Biochem.

193

255-261

639393

9665708

Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila

1998

Simianu, M.; Murakami, E.; Brewer, J.M.; Ragsdale, S.W.

Biochemistry

37

10027-10039

639394

11034998

Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophilo

2001

Murakami, E.; Deppenmeier, U.; Ragsdale, S.W.

J. Biol. Chem.

276

2432-2439

654385

-

H2:heterodisulfide oxidoreductase, a second energy-conserving system in the methanogenic strain Goe1

1991

Deppenmeier, U.; Blaut, M.; Gottschalk, G.

Arch. Microbiol.

155

272-277

654386

9914308

Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus voltae

1999

Brodersen, J.; Gottschalk, G.; Deppenmeier, U.

Arch. Microbiol.

171

115-121

655396

8477725

Purification of a cytochrome b containing H2:heterodisulfide oxidoreductase complex from membranes of Methanosarcina barkeri

1993

Heiden, S.; Hedderich, R.; Setzke, E.; Thauer, R.K.

Eur. J. Biochem.

213

529-535

655398

8119281

H2:heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties

1994

Setzke, E.; Hedderich, R.; Heiden, S.; Thauer, R.K.

Eur. J. Biochem.

220

139-148

655400

8174566

Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri

1994

Heiden, S.; Hedderich, R.; Setzke, E.; Thauer, R.K.

Eur. J. Biochem.

221

855-861

655416

11322875

A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea

2001

Madadi-Kahkesh, S.; Duin, E.C.; Heim, S.; Albracht, S.P.; Johnson, M.K.; Hedderich, R.

Eur. J. Biochem.

268

2566-2577

655471

12492476

Bioenergetics of the formyl-methanofuran dehydrogenase and heterodisulfide reductase reactions in Methanothermobacter thermautotrophicus

2003

de Poorter, L.M.; Geerts, W.G.; Theuvenet, A.P.; Keltjens, J.T.

Eur. J. Biochem.

270

66-75

655531

-

Methanobacterium thermoautotrophicum contains a soluble enzyme system that specifically catalyzes the reduction of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate with H2

1988

Hedderich, R.; Thauer, R.K.

FEBS Lett.

234

223-227

655532

-

Membrane-bound F420H2-dependent heterodisulfide reductase in methanogenic bacterium strain Go1 and Methanolobus tindarius

1990

Deppenmeier, U.; Blaut, M.; Mahlmann, A.; Gottschalk, G.

FEBS Lett.

261

199-203

655823

7961460

Characterization of a CO:heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila

1994

Peer, C.W.; Painter, M.H.; Rasche, M.E.; Ferry, J.G.

J. Bacteriol.

176

6974-6979

655825

10383977

Energy conservation by the H2:heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: identification of two proton-translocating segments

1999

Ide, T.; Baumer, S.; Deppenmeier, U.

J. Bacteriol.

181

4076-4080

657172

11607121

Reduced coenzyme F420: heterodisulfide oxidoreductase, a proton-translocating redox system in methanogenic bacteria

1990

Deppenmeier, U.; Blaut, M.; Mahlmann, A.; Gottschalk, G.

Proc. Natl. Acad. Sci. USA

87

9449-9453

Links to other databases for N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine

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Show Links (1 entry)

ChEBI

PubChem

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