Cinnamoyl-CoA

Cinnamoyl-Coenzyme A
Names
	IUPAC name 3′-O-Phosphonoadenosine 5′-[(3R)-3-hydroxy-2,2-dimethyl-4-({3-[(2-{[(2E)-3-phenylprop-2-enoyl]sulfanyl}ethyl)amino]-3-oxopropyl}amino)-4-oxobutyl dihydroxen diphosphate]
	Systematic IUPAC name [(2R,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-({3-[(2-{[(2E)-3-phenylprop-2-enoyl]sulfanyl}ethyl)amino]-3-oxopropyl}amino)-4-oxobutyl dihydrogen diphosphate
	Other names Cinnamoyl-coa; (E)-cinnamoyl-CoA; Coenzyme A, S-(3-phenyl-2-propenoate); (E)-benzylideneacetyl-CoA; 3-phenylacryloyl-CoA
Identifiers
CAS Number	76109-04-1; 30801-99-1 (non-specific) ;
3D model (JSmol)	Interactive image;
ChemSpider	4947984;
PubChem CID	6444037;
UNII	6YVQ9P5RAT ;
CompTox Dashboard (EPA)	DTXSID501030398 ;
	InChI InChI=1S/C30H42N7O17P3S/c1-30(2,25(41)28(42)33-11-10-20(38)32-12-13-58-21(39)9-8-18-6-4-3-5-7-18)15-51-57(48,49)54-56(46,47)50-14-19-24(53-55(43,44)45)23(40)29(52-19)37-17-36-22-26(31)34-16-35-27(22)37/h3-9,16-17,19,23-25,29,40-41H,10-15H2,1-2H3,(H,32,38)(H,33,42)(H,46,47)(H,48,49)(H2,31,34,35)(H2,43,44,45)/b9-8+/t19-,23-,24-,25+,29-/m1/s1 Key: JVNVHNHITFVWIX-KZKUDURGSA-N; InChI=1/C30H42N7O17P3S/c1-30(2,25(41)28(42)33-11-10-20(38)32-12-13-58-21(39)9-8-18-6-4-3-5-7-18)15-51-57(48,49)54-56(46,47)50-14-19-24(53-55(43,44)45)23(40)29(52-19)37-17-36-22-26(31)34-16-35-27(22)37/h3-9,16-17,19,23-25,29,40-41H,10-15H2,1-2H3,(H,32,38)(H,33,42)(H,46,47)(H,48,49)(H2,31,34,35)(H2,43,44,45)/b9-8+/t19-,23-,24-,25+,29-/m1/s1 Key: JVNVHNHITFVWIX-KZKUDURGBU;
	SMILES CC(C)(COP(=O)(O)OP(=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)N2C=NC3=C(N=CN=C32)N)O)OP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCSC(=O)/C=C/C4=CC=CC=C4)O;
Properties
Chemical formula	C30H42N7O17P3S
Molar mass	897.68 g·mol−1
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Infobox references

Cinnamoyl-coenzyme A is an intermediate in the phenylpropanoid metabolic pathway. It is the thioester formed between cinnamic acid and coenzyme A.

Biosynthesis

Cinnamoyl-CoA is produced in two enzymatically-catalysed steps of the phenylpropanoid metabolic pathway. In the first, phenylalanine ammonia-lyase (PAL), converts the amino acid phenylalanine to cinnamic acid:^[1]

phenylalanine

PAL

NH₃

Rightward reaction arrow with minor product(s) to top right

cinnamic acid

Subsequently, 4-coumarate-CoA ligase produces the thioester with coenzyme A. The reaction is driven to completion by the energy produced by the hydrolysis of adenosine triphosphate (ATP) to its monophosphate AMP, releasing diphosphate.^[2]

cinnamic acid + coenzyme A

Enzymes using cinnamoyl-coenzyme A

Cinnamoyl-CoA reductase catalyzes the chemical reaction which produces cinnamaldehyde from cinnamoyl-CoA:^[3]

cinnamoyl-CoA

+ NADPH

H⁺

Rightward reaction arrow with minor substrate(s) from top left

cinnamaldehyde

+ coenzyme A + NADP⁺

The reaction is important in the production of monolignols, which are the building blocks for plant lignin.^[4]

Pinosylvin synthase combines one unit of cinnamoyl-CoA with three of malonyl-CoA to form the stilbene, pinosylvin, with coenzyme A and carbon dioxide as byproducts. The product is produced in response to fungal attack on the pine tree Pinus sylvestris.^[5]^[6]

cinnamoyl-CoA + 3

malonyl-CoA

4 CO₂

pinosylvin

+ 4 coenzyme A

Cinnamoyl-CoA:phenyllactate CoA-transferase catalyzes a chemical reaction which transfers the coenzyme A thioester from cinnamoyl-CoA to (R)-phenyllactic acid, giving (R)-phenyllactyl-CoA and cinnamic acid.^[7]

References

↑ Appert C, Logemann E, Hahlbrock K, Schmid J, Amrhein N (October 1994). "Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.)". European Journal of Biochemistry. 225 (1): 491–9. doi:10.1111/j.1432-1033.1994.00491.x. PMID 7925471.
↑ Gross GG, Zenk MH (1974). "Isolation and properties of hydroxycinnamate: CoA ligase from lignifying tissue of Forsythia". Eur. J. Biochem. 42 (2): 453–9. doi:10.1111/j.1432-1033.1974.tb03359.x. PMID 4364250.
↑ Pan H, Zhou R, Louie GV, Mühlemann JK, Bomati EK, Bowman ME, Dudareva N, Dixon RA, Noel JP, Wang X (September 2014). "Structural studies of cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase, key enzymes of monolignol biosynthesis". The Plant Cell. 26 (9): 3709–27. Bibcode:2014PlanC..26.3709P. doi:10.1105/tpc.114.127399. PMC 4213152. PMID 25217505.
↑ Lauvergeat V, Lacomme C, Lacombe E, Lasserre E, Roby D, Grima-Pettenati J (August 2001). "Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria". Phytochemistry. 57 (7): 1187–95. Bibcode:2001PChem..57.1187L. doi:10.1016/s0031-9422(01)00053-x. PMID 11430991.
↑ Gehlert R (1990). "Stilbene Synthase from Seedlings of Pinus sylvestris : Purification and Induction in Response to Fungal Infection". Molecular Plant-Microbe Interactions. 3 (6): 444. Bibcode:1990MPMI....3..444G. doi:10.1094/MPMI-3-444.
↑ Valletta A, Iozia LM, Leonelli F (January 2021). "Impact of Environmental Factors on Stilbene Biosynthesis". Plants. 10 (1): 90. Bibcode:2021Plnts..10...90V. doi:10.3390/plants10010090. PMC 7823792. PMID 33406721.
↑ Dickert S, Pierik AJ, Linder D, Buckel W (2000). "The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes". Eur. J. Biochem. 267 (12): 3874–84. doi:10.1046/j.1432-1327.2000.01427.x. PMID 10849007.

[1] Appert C, Logemann E, Hahlbrock K, Schmid J, Amrhein N (October 1994). "Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.)". European Journal of Biochemistry. 225 (1): 491–9. doi:10.1111/j.1432-1033.1994.00491.x. PMID 7925471.

[2] Gross GG, Zenk MH (1974). "Isolation and properties of hydroxycinnamate: CoA ligase from lignifying tissue of Forsythia". Eur. J. Biochem. 42 (2): 453–9. doi:10.1111/j.1432-1033.1974.tb03359.x. PMID 4364250.

[3] Pan H, Zhou R, Louie GV, Mühlemann JK, Bomati EK, Bowman ME, Dudareva N, Dixon RA, Noel JP, Wang X (September 2014). "Structural studies of cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase, key enzymes of monolignol biosynthesis". The Plant Cell. 26 (9): 3709–27. Bibcode:2014PlanC..26.3709P. doi:10.1105/tpc.114.127399. PMC 4213152. PMID 25217505.

[4] Lauvergeat V, Lacomme C, Lacombe E, Lasserre E, Roby D, Grima-Pettenati J (August 2001). "Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria". Phytochemistry. 57 (7): 1187–95. Bibcode:2001PChem..57.1187L. doi:10.1016/s0031-9422(01)00053-x. PMID 11430991.

[5] Gehlert R (1990). "Stilbene Synthase from Seedlings of Pinus sylvestris : Purification and Induction in Response to Fungal Infection". Molecular Plant-Microbe Interactions. 3 (6): 444. Bibcode:1990MPMI....3..444G. doi:10.1094/MPMI-3-444.

[:0-6] Valletta A, Iozia LM, Leonelli F (January 2021). "Impact of Environmental Factors on Stilbene Biosynthesis". Plants. 10 (1): 90. Bibcode:2021Plnts..10...90V. doi:10.3390/plants10010090. PMC 7823792. PMID 33406721.

[7] Dickert S, Pierik AJ, Linder D, Buckel W (2000). "The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes". Eur. J. Biochem. 267 (12): 3874–84. doi:10.1046/j.1432-1327.2000.01427.x. PMID 10849007.

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