Any feedback?
No. of entries
Information on EC 1.3.99.41 - 3-(methylsulfanyl)propanoyl-CoA 2-dehydrogenase
for references in articles please use BRENDA:EC1.3.99.41
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.99 With unknown physiological acceptors
1.3.99.41 3-(methylsulfanyl)propanoyl-CoA 2-dehydrogenase
IUBMB Comments
The enzyme, found in marine bacteria, participates in a 3-(methylsulfanyl)propanoate degradation pathway. Based on similar enzymes, the in vivo electron acceptor is likely electron-transfer flavoprotein (ETF).
The expected taxonomic range for this enzyme is: Roseobacteraceae
Reaction Schemes
showSynonyms
mmpa-coa dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dmdC
MMPA-CoA dehydrogeanase
MMPA-CoA dehydrogenase
SPO3804
dmdC
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-(methylsulfanyl)propanoyl-CoA + acceptor = 3-(methylsulfanyl)acryloyl-CoA + reduced acceptor
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
methylthiopropanoate degradation I (cleavage)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
3-(methylsulfanyl)propanoyl-CoA:acceptor 2-oxidoreductase
The enzyme, found in marine bacteria, participates in a 3-(methylsulfanyl)propanoate degradation pathway. Based on similar enzymes, the in vivo electron acceptor is likely electron-transfer flavoprotein (ETF).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-(methylsulfanyl)propanoyl-CoA + acceptor
3-(methylsulfanyl)acryloyl-CoA + reduced acceptor
3-(methylthio)propionyl-CoA + acceptor
(2E)-3-(methylthio)prop-2-enoyl-CoA + reduced acceptor
3-(methylsulfanyl)propanoyl-CoA + acceptor
3-(methylsulfanyl)acryloyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
3-(methylsulfanyl)propanoyl-CoA + acceptor
3-(methylsulfanyl)acryloyl-CoA + reduced acceptor
-
Substrates: best substrate
Products: -
Products: -
?
3-(methylsulfanyl)propanoyl-CoA + FAD
3-(methylsulfanyl)acryloyl-CoA + FADH2
Substrates: -
Products: -
Products: -
?
3-(methylsulfanyl)propanoyl-CoA + FAD
3-(methylsulfanyl)acryloyl-CoA + FADH2
-
Substrates: -
Products: -
Products: -
?
3-(methylsulfanyl)propanoyl-CoA + FAD
3-(methylsulfanyl)acryloyl-CoA + FADH2
-
Substrates: -
Products: -
Products: -
?
3-(methylthio)propionyl-CoA + acceptor
(2E)-3-(methylthio)prop-2-enoyl-CoA + reduced acceptor
Substrates: -
Products: -
Products: -
?
3-(methylthio)propionyl-CoA + acceptor
(2E)-3-(methylthio)prop-2-enoyl-CoA + reduced acceptor
Substrates: 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 DmdC, 3-(methylthio)propionyl-CoA dehydrogenase, catalyzes the first step in the demethylation pathway
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-(methylsulfanyl)propanoyl-CoA + acceptor
3-(methylsulfanyl)acryloyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
3-(methylthio)propionyl-CoA + acceptor
(2E)-3-(methylthio)prop-2-enoyl-CoA + reduced acceptor
Substrates: 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 DmdC, 3-(methylthio)propionyl-CoA dehydrogenase, catalyzes the first step in the demethylation pathway
Products: -
Products: -
?
3-(methylsulfanyl)propanoyl-CoA + FAD
3-(methylsulfanyl)acryloyl-CoA + FADH2
Substrates: -
Products: -
Products: -
?
3-(methylsulfanyl)propanoyl-CoA + FAD
3-(methylsulfanyl)acryloyl-CoA + FADH2
-
Substrates: -
Products: -
Products: -
?
3-(methylsulfanyl)propanoyl-CoA + FAD
3-(methylsulfanyl)acryloyl-CoA + FADH2
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is not affected by physiological concentrations of potential effectors, such as DMSP, MMPA, ATP, and ADP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.036
3-(methylsulfanyl)propanoyl-CoA
-
pH and temperature not specified in the publication
1.4
3-(methylsulfanyl)propanoyl-CoA
wild type enzyme, at pH 9.0 and 40Ā°C
1.6
3-(methylsulfanyl)propanoyl-CoA
mutant enzyme Y434A, at pH 9.0 and 40Ā°C
2
3-(methylsulfanyl)propanoyl-CoA
mutant enzyme H280A, at pH 9.0 and 40Ā°C
2
3-(methylsulfanyl)propanoyl-CoA
mutant enzyme K223A, at pH 9.0 and 40Ā°C
6.3
3-(methylsulfanyl)propanoyl-CoA
mutant enzyme M161A, at pH 9.0 and 40Ā°C
8
3-(methylsulfanyl)propanoyl-CoA
mutant enzyme K281A, at pH 9.0 and 40Ā°C
12.4
3-(methylsulfanyl)propanoyl-CoA
mutant enzyme R284A, at pH 9.0 and 40Ā°C
14.3
3-(methylsulfanyl)propanoyl-CoA
mutant enzyme F287A, at pH 9.0 and 40Ā°C
100
3-(methylsulfanyl)propanoyl-CoA
Km above 100 mM, mutant enzyme R448A, at pH 9.0 and 40Ā°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
a dmdC2 mutant (SPO3804::Tn5) can not grow on 3-(methylthio)propanoate as the sole source of carbon, indicating that this pathway is essential for growth on 3-(methylthio)propanoate. In contrast, the mutant grows similarly to wild-type with 3-(dimethylsulphonio)propanoate, indicating that the cleavage pathway, initiated by DddQ or DddP13, remains capable of supporting growth
metabolism
in extracts of chemostat-grown cells the levels of DmdB, DmdC and DmdD activities exceed the minimum level, 57 nmol/min*mg of protein, necessary to support growth. The amount of transcripts for dmdB, dmdC and dmdD increase during growth on 3-(methylthio)propanoate or 3-(dimethylsulphonio)propanoate, as expected if the pathway is required for 3-(methylthio)propanoate metabolism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A3SI50_ROSNI
Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM)
591
0
64197
TrEMBL
-
DMDC_RUEPO
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
588
0
62854
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.2 M sodium nitrate, 0.1 M Bis-Tris propane (pH 8.5) and 20% (w/v) PEG 3350
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E435A
the mutation completely abolishes the activity of the enzyme
F195A
the mutation almost completely abolishes the activity of the enzyme to 0.4% of wild type activity
F287A
the mutant with 76.3% of wild type activity shows significantly increased Km to 3-(methylsulfanyl)propanoyl-CoA
H280A
the mutation severely reduces the activity of the enzyme to 18.2%, but does not affect its Km value to 3-(methylsulfanyl)propanoyl-CoA
K223A
the mutation severely reduces the activity of the enzyme to 9.4%, but does not affect its Km value to 3-(methylsulfanyl)propanoyl-CoA
K281A
the mutation severely reduces the activity of the enzyme to 54.5%, but does not affect its Km value to 3-(methylsulfanyl)propanoyl-CoA
M161A
the mutation significantly decreases the activity of the enzyme to 37.5% and does not affect its Km value to FAD or 3-(methylsulfanyl)propanoyl-CoA
R284A
the mutant with 97.2% of wild type activity shows significantly increased Km to 3-(methylsulfanyl)propanoyl-CoA
R448A
the mutant with 44.9% of wild type activity shows significantly increased Km for 3-(methylsulfanyl)propanoyl-CoA
S197A
the mutation significantly decreases the activity of the enzyme to 3.6% and increases its Km value to FAD
T170A
the mutation significantly decreases the activity of the enzyme to 37.5% and increases its Km value to FAD
Y434A
the mutation significantly decreases the activity of the enzyme to 51.2% and increases its Km value to FAD but does not affect its Km value to 3-(methylsulfanyl)propanoyl-CoA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the amount of transcripts for dmdB, dmdC and dmdD increases during growth of wild-type enzyme on methylmercaptopropionate or 3-(dimethylsulphonio)propanoate, as expected if the pathway is required for 3-(methylthio)propanoate metabolism. Following growth with 3-(dimethylsulphonio)propanoate, the levels of DmdC and DmdD activity in the deletion mutant dmdC are greatly reduced
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reisch, C.R.; Stoudemayer, M.J.; Varaljay, V.A.; Amster, I.J.; Moran, M.A.; Whitman, W.B.
Novel pathway for assimilation of dimethylsulphoniopropionate widespread in marine bacteria
Nature
473
208-211
2011
Ruegeria pomeroyi (Q5LLW7)
brenda
Wang, T.; Shi, H.; Whitman, W.B.
Substrate specificity of the 3-methylmercaptopropionyl coenzyme A dehydrogenase (DmdC1) from Ruegeria pomeroyi DSS-3
Appl. Environ. Microbiol.
88
e0172921
2022
Ruegeria pomeroyi
brenda
Bullock, H.; Luo, H.; Whitman, W.
Evolution of dimethylsulfoniopropionate metabolism in marine phytoplankton and bacteria
Front. Microbiol.
8
637
2017
Ruegeria pomeroyi
brenda
Shao, X.; Cao, H.; Zhao, F.; Peng, M.; Wang, P.; Li, C.; Shi, W.; Wei, T.; Yuan, Z.; Zhang, X.; Chen, X.; Todd, J.; Zhang, Y.
Mechanistic insight into 3-methylmercaptopropionate metabolism and kinetical regulation of demethylation pathway in marine dimethylsulfoniopropionate-catabolizing bacteria
Mol. Microbiol.
111
1057-1073
2019
Roseovarius nubinhibens (A3SI50)
brenda
Reisch, C.R.;Stoudemayer, M.J.; Varaljay, V.A.; Amster, I.J.; Moran, M.A.; Whitman, W.B.
Novel pathway for assimilation of dimethylsulphoniopropionate widespread in marine bacteria
Nature
473
208-211
2011
Ruegeria pomeroyi, Ruegeria lacuscaerulensis
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.99.41)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
