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Information on EC 4.2.1.175 - phenyllactyl-CoA dehydratase and Organism(s) Clostridium sporogenes and UniProt Accession Q93AL8
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4.2.1.175 phenyllactyl-CoA dehydrataseIUBMB Comments
The enzyme, found in some amino acid-fermenting anaerobic bacteria, participates in the fermentation pathways of L-phenylalanine, L-tyrosine, and L-tryptophan. It is a heterodimeric protein consisting of the FldB and FldC polypeptides, both of which contain an [4Fe-4S] cluster, and forms a complex with EC 2.8.3.17, 3-(aryl)acryloyl-CoA:(R)-3-(aryl)lactate CoA-transferase (FldA). In order to catalyse the reaction, the enzyme requires one high-energy electron that transiently reduces the electrophilic thiol ester carbonyl of the substrate to a nucleophilic ketyl radical anion, facilitating the elimination of the hydroxyl group. This electron, which is provided by by EC 5.6.1.9, (R)-2-hydroxyacyl-CoA dehydratase activating ATPase, needs to be supplied only once, before the first reaction takes place, as it is regenerated at the end of each reaction cycle. The enzyme acts on (R)-3-(aryl)lactoyl-CoAs produced by FldA, and regenerates the CoA donors used by that enzyme.
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The taxonomic range for the selected organisms is: Clostridium sporogenes
The expected taxonomic range for this enzyme is: Archaea, Bacteria
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
Synonyms
phenyllactyl-coa dehydratase, fldbc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-phenyllactoyl-CoA dehydratase
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-
-
-
aryllactyl-CoA dehydratase
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-
-
-
phenyllactyl-CoA dehydratase
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-
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-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
(R)-3-phenyllactyl-CoA hydro-lyase
The enzyme, found in some amino acid-fermenting anaerobic bacteria, participates in the fermentation pathways of L-phenylalanine, L-tyrosine, and L-tryptophan. It is a heterodimeric protein consisting of the FldB and FldC polypeptides, both of which contain an [4Fe-4S] cluster, and forms a complex with EC 2.8.3.17, 3-(aryl)acryloyl-CoA:(R)-3-(aryl)lactate CoA-transferase (FldA). In order to catalyse the reaction, the enzyme requires one high-energy electron that transiently reduces the electrophilic thiol ester carbonyl of the substrate to a nucleophilic ketyl radical anion, facilitating the elimination of the hydroxyl group. This electron, which is provided by by EC 5.6.1.9, (R)-2-hydroxyacyl-CoA dehydratase activating ATPase, needs to be supplied only once, before the first reaction takes place, as it is regenerated at the end of each reaction cycle. The enzyme acts on (R)-3-(aryl)lactoyl-CoAs produced by FldA, and regenerates the CoA donors used by that enzyme.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-(4-hydroxyphenyl)lactoyl-CoA
(E)-4-coumaroyl-CoA + H2O
-
-
-
?
(R)-3-(indol-3-yl)lactoyl-CoA
3-(indol-3-yl)acryloyl-CoA + H2O
-
-
-
?
(R)-3-(phenyl)lactoyl-CoA
(E)-cinnamoyl-CoA + H2O
-
-
-
?
(R)-3-phenyllactoyl-CoA
(2E)-3-phenylprop-2-enoyl-CoA + H2O
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i.e. (E)-cinnamoyl-CoA, (E)-3-phenylacryloyl-CoA
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?
(R)-3-phenyllactoyl-CoA
(2E)-3-phenylprop-2-enoyl-CoA + H2O
the enzyme is involved in fermentation of phenylalanine
i.e. (E)-cinnamoyl-CoA, (E)-3-phenylacryloyl-CoA
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-phenyllactoyl-CoA
(2E)-3-phenylprop-2-enoyl-CoA + H2O
the enzyme is involved in fermentation of phenylalanine
i.e. (E)-cinnamoyl-CoA, (E)-3-phenylacryloyl-CoA
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q93AL9 i.e. alpha-subunit FldB, Q93AL8 i.e. beta-subunit FldC
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme is involved in fermentation of phenylalanine
metabolism
reaction may employ a ketyl radical intermediate
physiological function
comparison of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans, Clostridium symbiosum and Fusobacterium nucleatum, 2-phenyllactate dehydratase from Clostridium sporogenes, 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile, and lactyl-CoA dehydratase from Clostridium propionicum. The 2-hydroxyacyl-CoA dehydratases are two-component systems composed of an extremely oxygen-sensitive component A, an activator, and component D, the actual dehydratase. Component A, a homodimer with one [4Fe-4S]cluster, transfers an electron to component D, a heterodimer with 1-2 [4Fe-4S] clusters and FMN, concomitant with hydrolysis of two ATP. From component D the electron is further transferred to the substrate, where it facilitates elimination of the hydroxyl group. In the resulting enoxyradical the beta-hydrogen is activated. After elimination the electron is handed-over to the next incoming substrate without further hydrolysis of ATP. The helix-cluster-helix architecture of component A forms an angle of 105°, which probably opens to 180° upon binding of ATP resembling an archer shooting arrows
physiological function
FldC is essential for the reductive metabolism of aromatic amino acids phenylalanine, tyrosine and tryptophan
physiological function
heterotrimeric phenyllactate dehydratase, FldABC, catalyses the reversible dehydration of (R)-phenyllactate to (E)-cinnamate in two steps: first CoA-transfer from the cofactor cinnamoyl-CoA to phenyllactate to yield phenyllactyl-CoA and the product cinnamate mediated by FldA, a (R)-phenyllactate CoA-transferase, second dehydration of phenyllactyl-CoA to cinnamoyl-CoA mediated by heterodimeric FldBC, a phenyllactyl-CoA dehydratase. Phenyllactate dehydratase requires initiation by ATP, MgCl2 and a reducing agent such as dithionite mediated by an extremely oxygen-sensitive initiator protein (FldI) present in the cell-free extract
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
1 * 46000 (FldA), 1 * 43000 (FldB), 1 * 40000 (FldC), the 46000 Da FldA subunit mediates CoA-transfer to phenyllactate, subunits FldBC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA, SDS-PAGE
43000
1 * 46000 (FldA), 1 * 43000 (FldB), 1 * 40000 (FldC), the 46000 Da FldA subunit mediates CoA-transfer to phenyllactate, subunits FldBC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA, SDS-PAGE
46000
1 * 46000 (FldA), 1 * 43000 (FldB), 1 * 40000 (FldC), the 46000 Da FldA subunit mediates CoA-transfer to phenyllactate, subunits FldBC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 46239, subunit FldB, and x * 43150, subunit FldC, calculated from sequence. X * 45490, subunit FldB, and x * 37420, subunit FldC, MALDI-TOF
heterotrimer
1 * 46000 (FldA), 1 * 43000 (FldB), 1 * 40000 (FldC), the 46000 Da FldA subunit mediates CoA-transfer to phenyllactate, subunits FldBC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitive with a half-life of approximately 12 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
in mice colonized by a wild-type Clostridium sporogenes strain, the mean indolepropionic acid concentration is around 80 microM, but in mice colonized with theFfldC mutant, indolepropionic acid is undetectable. Animals colonized by the FldC mutant exhibit significantly elevated frequencies of circulating myeloid cells, including neutrophils and classical (Ly6C+) monocytes, as well as increased antigen-experienced effector/memory T cells. Mice colonized by the FldC mutant strain show a significant increase in circulating Clostridium sporogenes-specific IgG
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dickert, S.; Pierik, A.J.; Linder, D.; Buckel, W.
The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes
Eur. J. Biochem.
267
3874-3884
2000
Clostridium sporogenes (Q93AL9 and Q93AL8), Clostridium sporogenes ATCC 3584 (Q93AL9 and Q93AL8)
Kim, J.; Hetzel, M.; Boiangiu, C.; Buckel, W.
Dehydration of (R)-2-hydroxyacyl-CoA to enoyl-CoA in the fermentation of alpha-amino acids by anaerobic bacteria
FEMS Microbiol. Rev.
28
455-468
2004
Clostridium sporogenes (Q93AL9 and Q93AL8)
Dickert, S.; Pierik, A.J.; Buckel, W.
Molecular characterization of phenyllactate dehydratase and its initiator from Clostridium sporogenes
Mol. Microbiol.
44
49-60
2002
Clostridium sporogenes (Q93AL9 and Q93AL8), Clostridium sporogenes
Kim, J.; Darley, D.; Buckel, W.; Pierik, A.
An allylic ketyl radical intermediate in clostridial amino-acid fermentation
Nature
452
239-242
2008
Clostridium sporogenes (Q93AL9 and Q93AL8)
Dodd, D.; Spitzer, M.; Van Treuren, W.; Merrill, B.; Hryckowian, A.; Higginbottom, S.; Le, A.; Cowan, T.; Nolan, G.; Fischbach, M.; Sonnenburg, J.
A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites
Nature
551
648-652
2017
Clostridium sporogenes (Q93AL9 and Q93AL8)
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