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Ligand acryloyl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

alanine metabolism, CO2 fixation in Crenarchaeota

KEGG

beta-Alanine metabolism, Carbon fixation pathways in prokaryotes, Carbon metabolism, Microbial metabolism in diverse environments, Propanoate metabolism, Styrene degradation more

MetaCyc

3-hydroxypropanoate cycle, 3-hydroxypropanoate/4-hydroxybutanate cycle, acrylate degradation I, acrylate degradation II, beta-alanine biosynthesis II, crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered), glyoxylate assimilation, propanoyl-CoA degradation II, pyruvate fermentation to propanoate II (acrylate pathway) more

Show all BRENDA pathways known for acryloyl-CoA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.84

acrylyl-CoA + NADPH + H+ = propanoyl-CoA + NADP+

745213, 745800, 745491, 745689

-

1.3.1.84

acrylyl-CoA + NADPH + H+ = propionyl-CoA + NADP+

740623

-

1.3.1.84

2 entries

1.3.8.1

2-propenoyl-CoA + reduced electron transfer flavoprotein = propanoyl-CoA + electron transfer protein

391284

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.2.1.116

3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O

0

-

4.2.1.54

(R)-lactoyl-CoA = acryloyl-CoA + H2O

0

-

Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Substrate (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.84

acryloyl-CoA + NADPH + H+ = propanoyl-CoA + NADP+

698624

-

1.3.1.84

acrylyl-CoA + NADH + H+ = propanoyl-CoA + NAD+

745213

-

1.3.1.84

acrylyl-CoA + NADPH + H+ = propanoyl-CoA + NADP+

698624, 745213, 745800, 745491, 745689

-

1.3.1.84

acrylyl-CoA + NADPH + H+ = propionyl-CoA + NADP+

740623

-

1.3.1.84

4 entries

1.3.1.85

acryloyl-CoA + CO2 + NADPH + H+ = methylmalonyl-CoA + NADP+

713409

-

1.3.1.95

acryloyl-CoA + methyl viologen = ?

696519

-

1.3.1.95

acryloyl-CoA + NADH + H+ = propanoyl-CoA + NAD+

697707, 718680

-

1.3.1.95

acryloyl-CoA + NADPH + H+ = propanoyl-CoA + NADP+

698624

-

1.3.8.1

2-propenoyl-CoA + reduced electron transfer flavoprotein = propanoyl-CoA + electron transfer protein

391274, 391279, 391284

-

1.3.8.1

acryloyl-CoA + benzyl viologen = propanoyl-CoA + reduced benzyl viologen

697969

-

1.3.8.1

acryloyl-CoA + reduced methylviologen = propanoyl-CoA + oxidized methylviologen

696519

-

1.3.1.95

3 entries

1.3.8.1

3 entries

2.8.3.1

acrylate + acrylyl-CoA = acetate + propionyl-CoA

724088

-

4.2.1.54

acrylyl-CoA + H2O = lactoyl-CoA

33926, 33927, 33931, 33929

-

4.3.1.6

acryloyl-CoA + NH3 = beta-alanyl-CoA

664903

-

4.3.1.6

acrylyl-CoA + NH3 = beta-alanyl-CoA

34369

-

4.3.1.6

2 entries

Product in Enzyme-catalyzed Reactions (16 results)

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Show Product (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.8.1

3-fluoropropionyl-CoA + phenazine methosulfate + dichlorophenolindophenol = 2-propenoyl-CoA + HF

391279

-

1.3.8.1

propionyl-CoA + 2,6-dichlorophenolindophenol = 2-propenoyl-CoA + reduced acceptor

0, 391300, 391308

-

1.3.8.1

propionyl-CoA + electron transfer flavoprotein = 2-propenoyl-CoA + reduced acceptor

391201

-

1.3.8.1

propionyl-CoA + phenazine methosulfate = 2-propenoyl-CoA + reduced acceptor

391201

-

1.3.8.1

4 entries

2.1.3.1

3-fluoropropionyl-CoA + oxaloacetate = acrylyl-CoA + pyruvate + F- + CO2

485821

-

2.8.3.1

acetyl-CoA + acrylate = acetate + acryloyl-CoA

0

-

2.8.3.12

acetyl-CoA + acrylate = acrylyl-CoA + acetate

0

-

2.8.3.9

acrylate + acetoacetyl-CoA = acrylyl-CoA + acetoacetate

0

-

4.2.1.116

3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O

0

-

4.2.1.54

(R)-lactoyl-CoA = acryloyl-CoA + H2O

0

-

4.2.1.54

lactoyl-CoA = acrylyl-CoA

33929, 33931

-

4.2.1.54

2 entries

6.2.1.1

ATP + acrylate + CoA = AMP + diphosphate + acryloyl-CoA

0

-

6.2.1.17

ATP + acrylate + CoA = AMP + diphosphate + acryloyl-CoA

0

-

6.2.1.17

ATP + acrylate + CoA = AMP + diphosphate + acrylyl-CoA

0

-

6.2.1.17

2 entries

6.2.1.36

acrylate + ATP + coenzyme A = acryloyl-CoA + AMP + diphosphate

0

-

6.2.1.44

ATP + acrylate + CoA = AMP + diphosphate + acryloyl-CoA

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (9 results)

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Show Turnover Number (9 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.84

45

-

at pH 7.0 and 30°C

740623

1.3.1.84

45

-

pH 7.0, 30°C, recombinant His-tagged enzyme

745213

1.3.1.84

60

-

at pH 7.0 and 30°C

740623

1.3.1.84

60

-

pH 7.0, 30°C, recombinant His-tagged enzyme

745213

1.3.1.84

80

-

at pH 7.0 and 30°C

740623

1.3.1.84

80

-

pH 7.0, 30°C, recombinant His-tagged enzyme

745213

1.3.1.95

4.5

-

in 50 mM Tris/HCl, pH 7.0, at 25°C

697707

1.3.1.95

13

-

apparent value, recombinant enzyme, at pH 7.5 and 22°C

698624

1.3.1.84

6 entries

1.3.1.95

2 entries

4.3.1.6

195

-

pH 7.5

664903

K_M Value (14 results)

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Show KM Value (14 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.84

0.0011

-

at pH 7.0 and 30°C

740623

1.3.1.84

0.0011

-

pH 7.0, 30°C, recombinant His-tagged enzyme

745213

1.3.1.84

0.0015

-

at pH 7.0 and 30°C

740623

1.3.1.84

0.0015

-

pH 7.0, 30°C, recombinant His-tagged enzyme

745213

1.3.1.84

0.0028

-

at pH 7.0 and 30°C

740623

1.3.1.84

0.0028

-

pH 7.0, 30°C, recombinant His-tagged enzyme

745213

1.3.1.84

0.003

-

pH 6.0, 65°C

698624

1.3.1.84

7 entries

1.3.1.85

0.5

-

pH and temperature not specified in the publication

713409

1.3.1.95

0.00083

-

in 0.1 M phosphate buffer pH 6.4, at 22°C

696519

1.3.1.95

0.002

-

apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C

697707

1.3.1.95

0.01

-

apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C

698624

1.3.1.95

0.036

-

apparent value, recombinant enzyme, at pH 7.5 and 22°C

698624

1.3.1.95

4 entries

1.3.8.1

0.00083

-

22°C, pH 6.4

696519

4.3.1.6

0.023

-

pH 7.5

664903

References & Links

Literature References (25)

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Show Reference (25 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

33926

-

Lactyl-CoA dehydrase

1966

Baldwin, R.L.; Wood, W.A.

Methods Enzymol.

9

683-685

33927

14292829

Lactate metabolism by Peptostreptococcus elsdenii: evidence for lactyl coenzyme A dehydrase

1965

Baldwin, R.L.; Wood, W.A.; Emery, R.S.

Biochim. Biophys. Acta

97

202-213

33929

3026450

Fe-S centers in lactyl-CoA dehydratase

1986

Kuchta, R.D.; Hanson, G.R.; Holmquist, B.; Abeles, R.H.

Biochemistry

25

7301-7307

33931

-

The stereochemistry of hydration of acrylyl-CoA catalyzed by lactyl-CoA dehydratase

1993

Brunelle, S.L.; Abeles, R.H.

Bioorg. Chem.

21

118-126

34369

-

The enzymatic synthesis of beta-alanyl coenzyme A

1955

Stadtman, E.R.

J. Am. Chem. Soc.

77

5765-5766

391201

3597357

Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver

1987

Finocchiaro, G.; Ito, M.; Tanaka, K.

J. Biol. Chem.

262

7982-7989

391274

6712628

Butyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction

1984

Williamson, G.; Engel, P.C.

Biochem. J.

218

521-529

391279

7159554

Mechanism of action of butyryl-CoA dehydrogenase: reactions with acetylenic, olefinic, and fluorinated substrate analogues

1982

Fendrich, G.; Abeles, R.H.

Biochemistry

21

6685-6695

391284

-

Butyryl-CoA dehydrogenase from Megasphaera elsdenii

1981

Engel, P.C.

Methods Enzymol.

71

359-366

391300

13130521

Studies on the fatty acid oxidization system of animal tissues. III. Butyryl coenzyme A dehydrogenase

1954

Green, D.E.; Mahler, H.R.

J. Biol. Chem.

206

1-12

391308

9009069

NAD-independent lactate and butyryl-CoA dehydrogenases of Clostridium acetobutylicum P262

1997

Diez-Gonzalez, F.; Russell, J.B.; Hunter, J.B.

Curr. Microbiol.

34

162-166

485821

7350155

Are carboxylations involving biotin concerted or nonconcerted?

1980

Stubbe, J.; Fish, S.; Abeles, R.H.

J. Biol. Chem.

255

236-242

664903

15670161

Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum

2005

Herrmann, G.; Selmer, T.; Jessen, H.J.; Gokarn, R.R.; Selifonova, O.; Gort, S.J.; Buckel, W.

FEBS J.

272

813-821

696519

4063066

Purification and some properties of an acryloyl-CoA reductase of Clostridium kluyveri

1985

Sedlmeier, H.; Simon, H.

Biol. Chem. Hoppe-Seyler

366

953-961

697707

12603323

Acryloyl-CoA reductase from Clostridium propionicum: An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein

2003

Hetzel, M.; Brock, M.; Selmer, T.; Pierik, A.; Golding, B.; Buckel, W.

Eur. J. Biochem.

270

902-910

697969

12052552

Energetics and kinetics of lactate fermentation to acetate and propionate via methylmalonyl-CoA or acrylyl-CoA

2002

Seeliger, S.; Janssen, P.; Schink, B.

FEMS Microbiol. Lett.

211

65-70

698624

19429610

3-Hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales

2009

Teufel, R.; Kung, J.; Kockelkorn, D.; Alber, B.; Fuchs, G.

J. Bacteriol.

191

4572-4581

713409

19458256

Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase

2009

Erb, T.J.; Brecht, V.; Fuchs, G.; Muller, M.; Alber, B.E.

Proc. Natl. Acad. Sci. USA

106

8871-8876

718680

22810300

Engineering Escherichia coli with acrylate pathway genes for propionic acid synthesis and its impact on mixed-acid fermentation

2013

Kandasamy, V.; Vaidyanathan, H.; Djurdjevic, I.; Jayamani, E.; Ramachandran, K.; Buckel, W.; Jayaraman, G.; Ramalingam, S.

Appl. Microbiol. Biotechnol.

97

1191-1200

724088

23250223

A propionate CoA-transferase of Ralstonia eutropha H16 with broad substrate specificity catalyzing the CoA thioester formation of various carboxylic acids

2012

Lindenkamp, N.; Schuermann, M.; Steinbuechel, A.

Appl. Microbiol. Biotechnol.

97

7699-7709

740623

23955006

Acrylyl-coenzyme A reductase, an enzyme involved in the assimilation of 3-hydroxypropionate by Rhodobacter sphaeroides

2013

Asao, M.; Alber, B.E.

J. Bacteriol.

195

4716-4725

745213

23955006

Acrylyl-coenzyme A reductase, an enzyme involved in the assimilation of 3-hydroxypropionate by Rhodobacter sphaeroides

2013

Asao, M.; Alber, B.E.

J. Bacteriol.

195

4716-4725

745491

27722922

Production of acrylic acid and propionic acid by constructing a portion of the 3-hydroxypropionate/4-hydroxybutyrate cycle from Metallosphaera sedula in Escherichia coli

2016

Liu, Z.; Liu, T.

J. Ind. Microbiol. Biotechnol.

43

1659-1670

745689

27771364

Reaction kinetic analysis of the 3-hydroxypropionate/4-hydroxybutyrate CO2 fixation cycle in extremely thermoacidophilic archaea

2016

Loder, A.J.; Han, Y.; Hawkins, A.B.; Lian, H.; Lipscomb, G.L.; Schut, G.J.; Keller, M.W.; Adams, M.W.; Kelly, R.M.

Metab. Eng.

38

446-463

745800

23815737

Metabolism of dimethylsulphoniopropionate by Ruegeria pomeroyi DSS-3

2013

Reisch, C.; Crabb, W.; Gifford, S.; Teng, Q.; Stoudemayer, M.; Moran, M.; Whitman, W.

Mol. Microbiol.

89

774-791

Links to other databases for acryloyl-CoA

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Show Links (1 entry)

ChEBI

PubChem