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| IUBMB_EC_number = 1/3/99/31
| IUBMB_EC_number = 1/3/99/31
| GO_code =
| GO_code =
| image =
| image = Pantoea-ananatis-crti 4dgk.png
| width =
| width =
| caption =[[Protein crystallography|Crystallographic]] structure of a bacterial phytoene desaturase monomer from ''Pantoea ananatis''.<ref name="pmid22745782 ">{{PDB|4dgk}}; {{cite journal | author1 = Schaub P |author2 =Yu Q|author3= Gemmecker S|author4= Poussin-Courmontagne P|author5= Mailliot J|author6= McEwen AG|author7= Ghisla S|author8= Al-Babili S|author9 = Cavarelli J |author10= Beyer P | title = On the Structure and Function of the Phytoene Desaturase CRTI from Pantoea ananatis, a Membrane-Peripheral and FAD-Dependent Oxidase/Isomerase | journal = PLoS One| volume = 7 | issue = 6 | pages = e39550 | date = 2012 | pmid = 22745782 |pmc= PMC3382138 | doi = 10.1371/journal.pone.0039550 }}</ref>
| caption =
}}
}}
'''Phytoene desaturase (lycopene-forming)''' ({{EC number|1.3.99.31}}, ''4-step phytoene desaturase'', ''four-step phytoene desaturase'', ''phytoene desaturase (ambiguous)'', ''CrtI (ambiguous)'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''15-cis-phytoene:acceptor oxidoreductase (lycopene-forming)''.<ref>{{cite journal | title = Expression in ''Escherichia coli'', purification, and reactivation of the recombinant ''Erwinia uredovora'' phytoene desaturase |author1 = Fraser, P.D. |author2 =Misawa, N. |author3 =Linden, H. |author4 =Yamano, S. |author5 =Kobayashi, K. |author6 =Sandmann, G. | journal = J. Biol. Chem. |year = 1992 |volume = 267 |pages = 19891–19895 |pmid = 1400305}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
'''Phytoene desaturase (lycopene-forming)''' ('''CrtI''', ''four-step phytoene desaturase'') ({{EC number|1.3.99.31}}, ''15-cis-phytoene:acceptor oxidoreductase (lycopene-forming)'') are [[enzyme]]s found in [[archaea]], [[bacteria]] and [[fungi]] that are involved in [[carotenoid]] biosynthesis. <ref>{{cite journal | title = Expression in ''Escherichia coli'', purification, and reactivation of the recombinant ''Erwinia uredovora'' phytoene desaturase |author1 = Fraser, P.D. |author2 =Misawa, N. |author3 =Linden, H. |author4 =Yamano, S. |author5 =Kobayashi, K. |author6 =Sandmann, G. | journal = J. Biol. Chem. |year = 1992 |volume = 267 |pages = 19891–19895 |pmid = 1400305}}</ref> They catalyze the conversion of colorless [[phytoene|15-''cis''-phytoene]] into a bright red [[lycopene]]. The same process in plants and [[cyanobacteria]] utilizes four separate enzymes.

==Biochemistry==
Bacterial phytoene desaturases were shown to require FAD as a cofactor for their function.<ref name="pmid9593705 ">{{cite journal | author1 = Dailey TA|author2= Dailey HA| title = Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of ''Myxococcus xanthus''.
Dailey TA1, Dailey HA. | journal = Journal of Biological Chemistry| volume = 273 | issue = 22 | pages = 13658-13662| date = May 1998 | pmid = 9593705 | doi = 10.1074/jbc.273.22.13658}}</ref> During the [[chemical reaction]] in total four additional [[double bonds]] are introduced into phytoene:


: 15-''cis''-[[phytoene]] + 4 acceptor <math>\rightleftharpoons</math> [[lycopene|all-''trans''-lycopene]] + 4 reduced acceptor (overall reaction)
: 15-''cis''-[[phytoene]] + 4 acceptor <math>\rightleftharpoons</math> [[lycopene|all-''trans''-lycopene]] + 4 reduced acceptor (overall reaction)
Line 16: Line 20:
: (1c) all-''trans''-''zeta''-carotene + acceptor <math>\rightleftharpoons</math> [[neurosporene |all-''trans''-neurosporene]] + reduced acceptor:
: (1c) all-''trans''-''zeta''-carotene + acceptor <math>\rightleftharpoons</math> [[neurosporene |all-''trans''-neurosporene]] + reduced acceptor:
: (1d) all-''trans''-neurosporene + acceptor <math>\rightleftharpoons</math> all-''trans''-lycopene + reduced acceptor
: (1d) all-''trans''-neurosporene + acceptor <math>\rightleftharpoons</math> all-''trans''-lycopene + reduced acceptor
==Applications==
In 2000 it was discovered that the [[gene]] insertion of a bacterial phytoene desaturase into [[Genetically_modified_tomato|transgenic tomatos]] increased the lycopene content without the need to alter several of the plants enzymes.<ref name=Romer>{{cite journal|last=Romer|first=S. |author2=Fraser, P.D. |author3=Kiano, J.W. |author4=Shipton, C.A. |author5=Misawa, N |author6=Schuch, W. |author7=Bramley, P.M.|title=Elevation of provitamin A content of transgenic tomato plants.|journal=Nature Biotechnology|year=2000|volume=18|pages=666–669|doi=10.1038/76523|url=http://www.nature.com/nbt/journal/v18/n6/full/nbt0600_666.html|pmid=10835607|issue=6}}</ref> This approach was later used in [[rice]] to increase its [[β-carotene]] content resulting in the [[Golden Rice]] project.


== See also ==
This enzyme is involved in [[carotenoid]] biosynthesis.
* [[15-Cis-phytoene desaturase]]

* [[Phytoene desaturase (neurosporene-forming)]]
* [[Phytoene desaturase (zeta-carotene-forming)]]
* [[Phytoene desaturase (3,4-didehydrolycopene-forming)]]
== References ==
== References ==
{{reflist}}
{{reflist}}

Revision as of 17:25, 16 November 2018

Phytoene desaturase (lycopene-forming)
Crystallographic structure of a bacterial phytoene desaturase monomer from Pantoea ananatis.[1]
Identifiers
EC no.1.3.99.31
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

Phytoene desaturase (lycopene-forming) (CrtI, four-step phytoene desaturase) (EC 1.3.99.31, 15-cis-phytoene:acceptor oxidoreductase (lycopene-forming)) are enzymes found in archaea, bacteria and fungi that are involved in carotenoid biosynthesis. [2] They catalyze the conversion of colorless 15-cis-phytoene into a bright red lycopene. The same process in plants and cyanobacteria utilizes four separate enzymes.

Biochemistry

Bacterial phytoene desaturases were shown to require FAD as a cofactor for their function.[3] During the chemical reaction in total four additional double bonds are introduced into phytoene:

15-cis-phytoene + 4 acceptor all-trans-lycopene + 4 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor all-trans-zeta-carotene + reduced acceptor
(1c) all-trans-zeta-carotene + acceptor all-trans-neurosporene + reduced acceptor:
(1d) all-trans-neurosporene + acceptor all-trans-lycopene + reduced acceptor

Applications

In 2000 it was discovered that the gene insertion of a bacterial phytoene desaturase into transgenic tomatos increased the lycopene content without the need to alter several of the plants enzymes.[4] This approach was later used in rice to increase its β-carotene content resulting in the Golden Rice project.

See also

References

  1. ^ PDB: 4dgk​; Schaub P; Yu Q; Gemmecker S; Poussin-Courmontagne P; Mailliot J; McEwen AG; Ghisla S; Al-Babili S; Cavarelli J; Beyer P (2012). "On the Structure and Function of the Phytoene Desaturase CRTI from Pantoea ananatis, a Membrane-Peripheral and FAD-Dependent Oxidase/Isomerase". PLoS One. 7 (6): e39550. doi:10.1371/journal.pone.0039550. PMC 3382138. PMID 22745782.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  2. ^ Fraser, P.D.; Misawa, N.; Linden, H.; Yamano, S.; Kobayashi, K.; Sandmann, G. (1992). "Expression in Escherichia coli, purification, and reactivation of the recombinant Erwinia uredovora phytoene desaturase". J. Biol. Chem. 267: 19891–19895. PMID 1400305.
  3. ^ Dailey TA; Dailey HA (May 1998). "Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus. Dailey TA1, Dailey HA". Journal of Biological Chemistry. 273 (22): 13658–13662. doi:10.1074/jbc.273.22.13658. PMID 9593705. {{cite journal}}: line feed character in |title= at position 204 (help)CS1 maint: unflagged free DOI (link)
  4. ^ Romer, S.; Fraser, P.D.; Kiano, J.W.; Shipton, C.A.; Misawa, N; Schuch, W.; Bramley, P.M. (2000). "Elevation of provitamin A content of transgenic tomato plants". Nature Biotechnology. 18 (6): 666–669. doi:10.1038/76523. PMID 10835607.

External links

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