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Ligand reduced carbamoyl methyl viologen

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (14 results)

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Show Substrate (14 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.30

phenylpyruvate + reduced carbamoylmethyl viologen = (2R)-phenyllactate + oxidized carbamoylmethyl viologen

654958, 655314

-

1.2.99.6

3-Chlorobenzoate + reduced carbamoyl methyl viologen = 3-Chlorobenzaldehyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

3-Fluorobenzoate + reduced carbamoyl methyl viologen = 3-Fluorobenzaldehyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

3-Hydroxybenzoate + reduced carbamoyl methyl viologen = 3-Hydroxybenzaldehyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

3-Methoxybenzoate + reduced carbamoyl methyl viologen = 3-Methoxybenzaldhyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

3-Methylbenzoate + reduced carbamoyl methyl viologen = 3-Methylbenzaldehyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

4-(Hydroxymethyl)benzoate + reduced carbamoyl methyl viologen = 4-(Hydroxymethyl)benzaldehyde + carbamoyl methyl viologen

11939

-

1.2.99.6

4-Chlorobenzoate + reduced carbamoyl methyl viologen = 4-Chlorobenzaldehyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

4-Fluorobenzoate + reduced carbamoyl methyl viologen = 4-Fluorobenzaldehyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

4-Hydroxybenzoate + reduced carbamoyl methyl viologen = 4-Hydroxybenzaldehyde + carbamoyl methyl viologen

11943

-

1.2.99.6

4-Methoxybenzoate + reduced carbamoyl methyl viologen = 4-Methoxybenzaldehyde + carbamoyl methyl viologen

11943

-

1.2.99.6

4-Methylbenzoate + reduced carbamoyl methyl viologen = 4-Methylbenzaldehyde + carbamoyl methyl viologen

11939, 11943

-

1.2.99.6

5-Phenyl-2,4-pentadienate + reduced carbamoyl methyl viologen = ? + carbamoyl methyl viologen

11939

-

1.2.99.6

Pyridine 4-carboxylate + reduced carbamoyl methyl viologen = Pyridine 4-carboxaldehyde + carbamoyl methyl viologen

11939

-

1.2.99.6

13 entries

Product in Enzyme-catalyzed Reactions (13 results)

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Show Product (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.7.12

formylmethanofuran + oxidized carbamoylmethylviologen + H2O = methanofuran + reduced carbamoylmethylviologen + CO2

11920

-

1.2.99.6

3,4-Dimethoxy-5-hydroxy-benzaldehyde + carbamoyl methyl viologen = 3,4-Dimethoxy-5-hydroxy-benzoate + reduced carbamoyl methyl viologen

0

-

1.2.99.6

3,5-Dimethoxy-4-hydroxy-benzaldehyde + carbamoyl methyl viologen = 3,5-Dimethoxy-4-hydroxy-benzoate + reduced carbamoyl methyl viologen

0

-

1.2.99.6

4-Hydroxy-3-methoxy-benzaldehyde + carbamoyl methyl viologen = 4-Hydroxy-3-methoxy-benzoate + reduced carbamoyl methyl viologen

0

-

1.2.99.6

4-Hydroxybenzaldehyde + carbamoyl methyl viologen = 4-Hydroxybenzoate + reduced carbamoyl methyl viologen

11939

-

1.2.99.6

4-Methoxybenzaldehyde + benzyl viologen = 4-Methoxybenzoate + reduced carbamoyl methyl viologen

11939, 0

-

1.2.99.6

Acetaldehyde + carbamoyl methyl viologen = acetate + reduced carbamoyl methyl viologen

11939

-

1.2.99.6

Benzaldehyde + carbamoyl methyl viologen = Benzoate + reduced carbamoyl methyl viologen

0, 11939

-

1.2.99.6

Cinnamaldehyde + carbamoyl methyl viologen = Cinnamate + reduced carbamoyl methyl viologen

11939

-

1.2.99.6

Methanal + methyl viologen = Formate + reduced carbamoyl methyl viologen

0

-

1.2.99.6

Propanal + NH2CO-methyl viologen = Propanoate + reduced carbamoyl methyl viologen

0, 11943

-

1.2.99.6

terephthalaldehyde + carbamoyl methyl viologen = terephthalate + reduced carbamoyl methyl viologen

11939

-

1.2.99.6

Butanal + NH2CO-methyl viologen = Butanoate + reduced NH2CO-methyl viologen

0

-

1.2.99.6

12 entries

Enzyme Kinetic Parameters

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.99.6

0.03

-

with propanoate as cosubstrate

11939

1.2.99.6

0.16

-

with benzoate as cosubstrate

11939

1.2.99.6

2 entries

References & Links

Literature References (5)

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Show Reference (5 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

11920

7813470

Thermodynamics of the formylmethanofuran dehydrogenase reaction in Methanobacterium thermoautotrophicum

1994

Bertram, P.A.; Thauer, R.K.

Eur. J. Biochem.

226

811-818

11939

-

Pterin cofactor, substrate specificity, and observations on the kinetics of the reversible tungsten-containing aldehyde oxidoreductase from Clostridium thermoaceticum

1995

Huber, C.; Skopan, H.; Feicht, R.; White, H.; Simon, H.

Arch. Microbiol.

164

110-118

11943

1793519

Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum

1991

White, H.; Feicht, R.; Huber, C.; Lottspeich, F.; Simon, H.

Biol. Chem. Hoppe-Seyler

372

999-1005

654958

8000871

Proteus mirabilis dehydrogenates aldonates and aldarates with an (R)-configured alpha-carbon atom to the corresponding 2-oxocarboxylates

1994

Schinschel, C.; Simon, H.

Bioorg. Med. Chem.

2

483-491

655314

-

Additional experiences with Proteus vulgaris and its hydroxycarboxylate-oxidoreductase for the preparation of (2R)- or (2S)-hydroxycarboxylates

1988

Krauss, F.; Guenther, H.; Skopan, H.; Simon, H.

DECHEMA Biotechnol. Conf.

1

313-318

Links to other databases for reduced carbamoyl methyl viologen

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Show Links (1 entry)

ChEBI

PubChem

-