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IUBMB CommentsA bacterial enzyme that is involved in propanoate fermentation (also known as the acrylate pathway).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
lactyl-coa dehydratase, lactoyl-coa dehydratase, (r)-lactyl-coa dehydratase,
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(R)-lactyl-CoA dehydratase
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acrylyl coenzyme A hydratase
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dehydratase, lactoyl-coenzyme A
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lactoyl coenzyme A dehydratase
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lactoyl-CoA dehydratase subunit alpha
lactyl CoA dehydratase
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lactyl-CoA dehydrase
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lactyl-CoA dehydratase
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lactyl-coenzyme A dehydrase
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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lactoyl-CoA dehydratase subunit alpha
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LCD
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lcdA
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(R)-lactoyl-CoA = acryloyl-CoA + H2O
(R)-lactoyl-CoA = acryloyl-CoA + H2O
3Si hydrogen is removed, no radical mechanism
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(R)-lactoyl-CoA = acryloyl-CoA + H2O
addition in the reverse direction is syn
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(R)-lactoyl-CoA = acryloyl-CoA + H2O
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(R)-lactoyl-CoA hydro-lyase (acryloyl-CoA-forming)
A bacterial enzyme that is involved in propanoate fermentation (also known as the acrylate pathway).
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(2R)-2-hydroxybutyryl-CoA
crotonyl-CoA + H2O
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stereospecific elimination of the 3Si hydrogen
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
acrylyl-CoA + H2O
lactoyl-CoA
crotonoyl-CoA + H2O
2-hydroxybutyryl-CoA
(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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acrylyl-CoA + H2O
lactoyl-CoA
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acrylyl-CoA + H2O
lactoyl-CoA
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r
acrylyl-CoA + H2O
lactoyl-CoA
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acrylyl-CoA + H2O
lactoyl-CoA
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crotonoyl-CoA + H2O
2-hydroxybutyryl-CoA
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r
crotonoyl-CoA + H2O
2-hydroxybutyryl-CoA
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lactoyl-CoA
acrylyl-CoA
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r
lactoyl-CoA
acrylyl-CoA
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r
lactoyl-CoA + H2O
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lactoyl-CoA + H2O
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enzyme in the pathway of propionate formation
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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(R)-lactoyl-CoA
acryloyl-CoA + H2O
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lactoyl-CoA + H2O
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lactoyl-CoA + H2O
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enzyme in the pathway of propionate formation
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ATP
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required, no stoichiometric hydrolysis of ATP
flavin
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component EII contains flavin
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Fe-S
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component EII contains two Fe-S clusters one 4Fe-4S type, one 3Fe-3/4S type, the loss of Fe does not affect catalytic activity
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Dehydration
(R)-lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA.
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0.031
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recombinant enzyme, pH and temperature not specified in the publication
additional information
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strict anaerobic conditions
additional information
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strict anaerobic conditions
additional information
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strict anaerobic conditions
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subunit alpha
UniProt
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subunit alpha
UniProt
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LCDA_ANAPI
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47390
Swiss-Prot
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LCDB_ANAPI
374
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41810
Swiss-Prot
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A0A068ZY05_CLODI
410
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46593
TrEMBL
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W8EJ66_9FIRM
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26358
TrEMBL
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A0A2P9GYA3_9DELT
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12186
TrEMBL
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1000000
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enzyme consists of two proteins, EI and EII, neither of the two can catalyze the reaction alone, EI: 27000 Da, EII: 10000000 Da, gel filtration
41000
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enzyme consists of two proteins, EI and EII, neither of the two can catalyze the reaction alone, EI: 27000, EII: x * 41000 + x * 48000, SDS-PAGE
48000
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enzyme consists of two proteins, EI and EII, neither of the two can catalyze the reaction alone, EI: 27000, EII: x * 41000 + x * 48000, SDS-PAGE
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polymer
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enzyme consists of two proteins, EI and EII, neither of the two can catalyze the reaction alone, EI: 27000, EII: x * 41000 + x * 48000, SDS-PAGE
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very unstable during purification
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exposure to O2 for 24 h causes complete inactivation
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33929
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-15°C, crude extract relatively stable
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4°C, anaerobic storage, 4 mM (NH4)2SO4, stable for at least 4 months
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expressed in Escherichia coli Rosetta-gami 2(DE3)pLysS cells
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Baldwin, R.L.; Wood, W.A.
Lactyl-CoA dehydrase
Methods Enzymol.
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683-685
1966
Megasphaera elsdenii
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Baldwin, R.L.; Wood, W.A.; Emery, R.S.
Lactate metabolism by Peptostreptococcus elsdenii: evidence for lactyl coenzyme A dehydrase
Biochim. Biophys. Acta
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202-213
1965
Megasphaera elsdenii
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Schweiger, G.; Buckel, W.
On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum
FEBS Lett.
171
79-84
1984
Anaerotignum propionicum
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Kuchta, R.D.; Hanson, G.R.; Holmquist, B.; Abeles, R.H.
Fe-S centers in lactyl-CoA dehydratase
Biochemistry
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7301-7307
1986
Anaerotignum propionicum
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Hofmeister, A.E.M.; Buckel.W.
(R)-lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA
Eur. J. Biochem.
206
547-552
1992
Anaerotignum propionicum
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Brunelle, S.L.; Abeles, R.H.
The stereochemistry of hydration of acrylyl-CoA catalyzed by lactyl-CoA dehydratase
Bioorg. Chem.
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118-126
1993
Anaerotignum propionicum
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Kandasamy, V.; Vaidyanathan, H.; Djurdjevic, I.; Jayamani, E.; Ramachandran, K.; Buckel, W.; Jayaraman, G.; Ramalingam, S.
Engineering Escherichia coli with acrylate pathway genes for propionic acid synthesis and its impact on mixed-acid fermentation
Appl. Microbiol. Biotechnol.
97
1191-1200
2013
Anaerotignum propionicum, Anaerotignum propionicum DSM 1682
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Reichardt, N.; Duncan, S.H.; Young, P.; Belenguer, A.; McWilliam Leitch, C.; Scott, K.P.; Flint, H.J.; Louis, P.
Phylogenetic distribution of three pathways for propionate production within the human gut microbiota
ISME J.
8
1323-1335
2014
[Clostridium] symbiosum, Clostridium botulinum, Clostridioides difficile, Clostridium novyi, Clostridium sp., Megasphaera elsdenii, Coprococcus catus, butyrate-producing bacterium SS3/4, Enterocloster asparagiformis, Anaerotignum propionicum (G3KIM4), Clostridium novyi NT, Coprococcus catus GD/7, [Clostridium] symbiosum WAL-14163, Clostridioides difficile 630, Enterocloster asparagiformis DSM 15981, Anaerotignum propionicum DSM 1682 (G3KIM4), Clostridium sp. M62/1, Clostridium sp. MSTE9 (cluster XIVb), Megasphaera elsdenii LC1 DSM 20460T, Clostridium botulinum C Eklund, Clostridium botulinum A2
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4.2.1.54 lactoyl-CoA dehydratase
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The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 
