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IUBMB 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 forms a complex with EC 4.2.1.175 , (R )-3-(aryl)lactoyl-CoA dehydratase.
Synonyms
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cinnamoyl-CoA:phenyllactate CoA-transferase
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coenzyme A-transferase, cinnamoyl-coenzyme A:(R)-phenyllactate
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(E)-4-coumaroyl-CoA + (R)-3-(4-hydroxyphenyl)lactate = 4-coumarate + (R)-3-(4-hydroxyphenyl)lactoyl-CoA
(2)
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(E)-cinnamoyl-CoA + (R)-(phenyl)lactate = (E)-cinnamate + (R)-(phenyl)lactoyl-CoA
3-(indol-3-yl)acryloyl-CoA + (R)-3-(indol-3-yl)lactate = 3-(indol-3-yl)acrylate + (R)-3-(indol-3-yl)lactoyl-CoA
(3)
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(E)-cinnamoyl-CoA + (R)-(phenyl)lactate = (E)-cinnamate + (R)-(phenyl)lactoyl-CoA
mechanism
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(E)-cinnamoyl-CoA + (R)-(phenyl)lactate = (E)-cinnamate + (R)-(phenyl)lactoyl-CoA
(1)
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coenzyme A transfer
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MetaCyc
4-hydroxybenzoate biosynthesis I (eukaryotes), L-phenylalanine degradation VI (reductive Stickland reaction), L-tryptophan degradation XIII (reductive Stickland reaction), L-tyrosine degradation V (reductive Stickland reaction)
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3-(aryl)acryloyl-CoA:(R)-3-(aryl)lactate CoA-transferase
The enzyme, found in some amino acid-fermenting anaerobic bacteria, participates in the fermentation pathways of L-phenylalanine, L-tyrosine, and L-tryptophan. It forms a complex with EC 4.2.1.175, (R)-3-(aryl)lactoyl-CoA dehydratase.
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(E)-cinnamoyl-CoA + (R)-phenyllactate
(E)-cinnamate + (R)-phenyllactoyl-CoA
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Substrates: -
?, r
(E)-cinnamoyl-CoA + 3-(4-hydroxyphenyl)-propionate
(E)-cinnamate + 3-(4-hydroxyphenyl)-propionyl-CoA
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Substrates: -
r
(E)-cinnamoyl-CoA + 3-phenylpropionate
(E)-cinnamate + 3-phenylpropionyl-CoA
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Substrates: in vitro 3-phenylpropionate is a better acceptor than (R)-phenyllactate
r
(E)-cinnamoyl-CoA + 4-phenylbutyrate
(E)-cinnamate + 4-phenylbutyryl-CoA
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Substrates: -
r
cinnamoyl-CoA + phenylpropionate
trans-cinnamate + phenylpropionyl-CoA
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Substrates: -
?
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(E)-cinnamoyl-CoA + (R)-phenyllactate
(E)-cinnamate + (R)-phenyllactoyl-CoA
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Substrates: -
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0.003 - 0.019
cinnamoyl-CoA
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cosubstrate phenylpropionate
0.009 - 0.012
phenylpropionate
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cosubstrate cinnamoyl-CoA
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7 - 8
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50 mM potassium phosphate, best buffer
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brenda
Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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40000
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alpha, beta, gamma, 1 * 46000, 1 * 43000, 1 * 40000, the 46000 kDa subunit A mediates CoA-transfer to phenyllactate, subunits BC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA
43000
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alpha, beta, gamma, 1 * 46000, 1 * 43000, 1 * 40000, the 46000 kDa subunit A mediates CoA-transfer to phenyllactate, subunits BC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA
46000
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alpha, beta, gamma, 1 * 46000, 1 * 43000, 1 * 40000, the 46000 kDa subunit A mediates CoA-transfer to phenyllactate, subunits BC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA
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heterotrimer
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alpha, beta, gamma, 1 * 46000, 1 * 43000, 1 * 40000, the 46000 kDa subunit A mediates CoA-transfer to phenyllactate, subunits BC mediate dehydration of phenyllactyl-CoA to cinnamoyl-CoA
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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
brenda
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
brenda
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