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]

Natural Substrates Products

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Natural Substrates Products on EC 6.2.1.44 - 3-(methylthio)propionyl-CoA ligase

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

ATP + 3-(methylthio)propanoate + CoA

AMP + diphosphate + 3-(methylthio)propionyl-CoA

3 entries

ATP + 3-(methylthio)propanoate + CoA

AMP + diphosphate + 3-methylmercaptopropionyl-CoA

Ruegeria pomeroyi

Q5LRT0, Q5LVM3

once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway to form the volatile gas dimethylsulfide or the demethylation pathway, yielding methanethiol, which is readily assimilated or oxidized. The enzyme DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2

727780

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-

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ATP + 3-(methylthio)propanoate + CoA

AMP + diphosphate + 3-(methylthio)propionyl-CoA

Candidatus Pelagibacter ubique

Q4FP19

once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway to form the volatile gas dimethylsulfide or the demethylation pathway, yielding methanethiol, which is readily assimilated or oxidized. The enzyme DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2

727780

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-

?

ATP + 3-(methylthio)propanoate + CoA

AMP + diphosphate + 3-(methylthio)propionyl-CoA

Ruegeria pomeroyi

Q5LRT0

degradation 3-(methylthio)propanoate, the first product in 3-(dimethylsulfonio)propanoate degradation. 3-(Dimethylsulfonio)propanoate is an osmolyte of many marine algae and certain plants. The global importance of dimethylsulfoniopropionate lies in its availability as a carbon and sulfur source for marine microorganisms and as a precursor of the gas dimethylsulfide, the oceanic emission of which leads to the formation of cloud condensation nuclei and promotion of solar radiation backscatter. Two competing pathways exist for the bacterial catabolism of 3-(dimethylsulfonio)propanoate, one releasing dimethylsulphide and the other releasing methanethiol

728373

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ATP + 3-(methylthio)propanoate + CoA

AMP + diphosphate + 3-(methylthio)propionyl-CoA

Ruegeria pomeroyi

Q5LRT0, Q5LVM3

once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway to form the volatile gas dimethylsulfide or the demethylation pathway, yielding methanethiol, which is readily assimilated or oxidized. The enzyme DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2

727780

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-

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