Dimethylsulfide: acceptor oxidoreductase from Rhodobacter sulfidophilus - The purified enzyme contains b-type haem and a pterin molybdenum cofactor

Hanlon, S.; Toh, T.; Solomon, P.; Holt, R.; McEwan, A.; Eur. J. Biochem. 239, 391-396 (1996)

Data extracted from this reference:

Metals/Ions

Commentary

Organism

Structure

Fe

the enzyme contains 3.5 mol Fe per mol enzyme

Rhodovulum sulfidophilum

Molybdenum

the enzyme contains 0.5 mol molybdenum per mol enzyme

Rhodovulum sulfidophilum

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

Substrate Product ID

dimethyl sulfoxide + reduced 2,6-dichloroindophenol

-

714886

Rhodovulum sulfidophilum

dimethyl sulfide + oxidized 2,6-dichloroindophenol + H2O

-

-

-

?

dimethyl sulfoxide + reduced methyl viologen + H2O

2% activity compared to trimethylamine N-oxide

714886

Rhodovulum sulfidophilum

dimethyl sulfide + oxidized methyl viologen

-

-

-

?

lauryldimethylamine N-oxide + reduced methyl viologen + H2O

69% activity compared to trimethylamine N-oxide

714886

Rhodovulum sulfidophilum

?

-

-

-

?

additional information

no activity with chlorate and bromate

714886

Rhodovulum sulfidophilum

?

-

-

-

-

trimethylamine N-oxide + reduced methyl viologen + H2O

100% activity

714886

Rhodovulum sulfidophilum

?

-

-

-

?

Cofactor

Commentary

Organism

Structure

heme

the cytochrome contains a b-type heme and a content of 0.65 mol protoheme per mol enzyme is determined

Rhodovulum sulfidophilum

iron-sulfur centre

-

Rhodovulum sulfidophilum

molybdopterin

-

Rhodovulum sulfidophilum

Cofactor

Commentary

Organism

Structure

heme

the cytochrome contains a b-type heme and a content of 0.65 mol protoheme per mol enzyme is determined

Rhodovulum sulfidophilum

iron-sulfur centre

-

Rhodovulum sulfidophilum

molybdopterin

-

Rhodovulum sulfidophilum

Metals/Ions

Commentary

Organism

Structure

Fe

the enzyme contains 3.5 mol Fe per mol enzyme

Rhodovulum sulfidophilum

Molybdenum

the enzyme contains 0.5 mol molybdenum per mol enzyme

Rhodovulum sulfidophilum

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

ID

dimethyl sulfoxide + reduced 2,6-dichloroindophenol

-

714886

Rhodovulum sulfidophilum

dimethyl sulfide + oxidized 2,6-dichloroindophenol + H2O

-

-

-

?

dimethyl sulfoxide + reduced methyl viologen + H2O

2% activity compared to trimethylamine N-oxide

714886

Rhodovulum sulfidophilum

dimethyl sulfide + oxidized methyl viologen

-

-

-

?

lauryldimethylamine N-oxide + reduced methyl viologen + H2O

69% activity compared to trimethylamine N-oxide

714886

Rhodovulum sulfidophilum

?

-

-

-

?

additional information

no activity with chlorate and bromate

714886

Rhodovulum sulfidophilum

?

-

-

-

-

trimethylamine N-oxide + reduced methyl viologen + H2O

100% activity

714886

Rhodovulum sulfidophilum

?

-

-

-

?

No.

1st author

Pub Med

title

organims

journal

volume

pages

year

Activating Compound

Application

Cloned(Commentary)

Crystallization (Commentary)

Engineering

General Stability

Inhibitors

KM Value [mM]

Localization

Metals/Ions

Molecular Weight [Da]

Natural Substrates/ Products (Substrates)

Organic Solvent Stability

Organism

Oxidation Stability

Posttranslational Modification

Purification (Commentary)

Reaction

Renatured (Commentary)

Source Tissue

Specific Activity [micromol/min/mg]

Storage Stability

Substrates and Products (Substrate)

Subunits

Synonyms

Temperature Optimum [°C]

Temperature Range [°C]

Temperature Stability [°C]

Turnover Number [1/s]

pH Optimum

pH Range

pH Stability

Cofactor

Ki Value [mM]

pI Value

IC50 Value

Activating Compound (protein specific)

Application (protein specific)

Cloned(Commentary) (protein specific)

Cofactor (protein specific)

Crystallization (Commentary) (protein specific)

Engineering (protein specific)

General Stability (protein specific)

IC50 Value (protein specific)

Inhibitors (protein specific)

Ki Value [mM] (protein specific)

KM Value [mM] (protein specific)

Localization (protein specific)

Metals/Ions (protein specific)

Molecular Weight [Da] (protein specific)

Natural Substrates/ Products (Substrates) (protein specific)

Organic Solvent Stability (protein specific)

Oxidation Stability (protein specific)

Posttranslational Modification (protein specific)

Purification (Commentary) (protein specific)

Renatured (Commentary) (protein specific)

Source Tissue (protein specific)

Specific Activity [micromol/min/mg] (protein specific)

Storage Stability (protein specific)

Substrates and Products (Substrate) (protein specific)

Subunits (protein specific)

Temperature Optimum [°C] (protein specific)

Temperature Range [°C] (protein specific)

Temperature Stability [°C] (protein specific)

Turnover Number [1/s] (protein specific)

pH Optimum (protein specific)

pH Range (protein specific)

pH Stability (protein specific)

pI Value (protein specific)

Expression

General Information

General Information (protein specific)

Expression (protein specific)

KCat/KM [mM/s]

KCat/KM [mM/s] (protein specific)

715664

Creevey

A mechanistic and electrochemi ...

Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1

J. Biol. Inorg. Chem.

13

1231-1238

2008

-

-

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-

-

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-

2

-

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-

2

-

5

-

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1

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4

1

3

-

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3

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2

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1

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4

1

-

-

-

-

1

-

-

-

-

-

-

-

-

-

716248

McDevitt

Molecular analysis of dimethyl ...

Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1

Mol. Microbiol.

44

1575-1587

2002

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1

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6

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9

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1

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12

1

12

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4

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3

6

9

6

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3

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12

3

-

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-

-

-

-

-

2

4

-

-

-

714886

Hanlon

Dimethylsulfide: acceptor oxid ...

Rhodovulum sulfidophilum

Eur. J. Biochem.

239

391-396

1996

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1

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1

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