6.2.1.44: 3-(methylthio)propionyl-CoA ligase

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For detailed information about 3-(methylthio)propionyl-CoA ligase, go to the full flat file.

Reaction

Synonyms

3-methylmercaptopropionyl-CoA ligase, BTH_DmdB2, BTH_I2141, DmdB, methylmercaptopropionate-coenzyme A ligase, MMPA-CoA ligase, PA4198, PA_DmdB1, PU_DmdB1, RL_DmdB1, RL_DmdB2, RPO_DmdB1, RPO_DmdB2, SAR11_0248, SL1157_1815, SL1157_2728, SPO0677, SPO2045

ECTree

     6 Ligases

         6.2 Forming carbon-sulfur bonds

             6.2.1 Acid-thiol ligases

                6.2.1.44 3-(methylthio)propionyl-CoA ligase

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Results	in table
198	AA Sequence
6	Cloned(Commentary)
2	Expression
3	General Information
41	Inhibitors
12	kcat/KM [mM/s]
12	KM Value [mM]
14	Metals/Ions
14	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
13	Organism
5	Pathway
3	pH Optimum
6	Purification (Commentary)
1	Reaction
10	Reference
4	Specific Activity [micromol/min/mg]
2	Storage Stability
109	Substrates and Products (Substrate)
17	Subunits
64	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
2	Temperature Range [°C]
12	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 6.2.1.44 - 3-(methylthio)propionyl-CoA ligase

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SYSTEMATIC NAME

IUBMB Comments

3-(methylthio)propanoate:CoA ligase (AMP-forming)

The enzyme is part of a dimethylsulfoniopropanoate demethylation pathway in the marine bacteria Ruegeria pomeroyi and Pelagibacter ubique. It also occurs in some nonmarine bacteria capable of metabolizing dimethylsulfoniopropionate (e.g. Burkholderia thailandensis, Pseudomonas aeruginosa, and Silicibacter lacuscaerulensis). It requires Mg2+ [2].