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Information on EC 5.5.1.19 - lycopene beta-cyclase and Organism(s) Capsicum annuum and UniProt Accession Q43415

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IUBMB Comments
The enzyme is a non-redox flavoprotein, containing FADH2 that is used for stabilization of a transition state. Lycopene has a psi-end group at both ends. When acting on one end, the enzyme forms gamma-carotene. When acting on both ends it forms beta-carotene. It also acts on neurosporene to give beta-zeacarotene.
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Capsicum annuum
UNIPROT: Q43415
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Word Map
The taxonomic range for the selected organisms is: Capsicum annuum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
lycopene cyclase, lycopene beta-cyclase, cyc-b, lcy-b, dclcyb1, lycopene beta cyclase, lcyb1, crtl-b, beta-lcy, lcyb2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
capsanthin-capsorubin synthase
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CrtL
-
-
-
-
CrtL-b
-
-
-
-
CrtY
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
carotenoid beta-end group lyase (decyclizing)
The enzyme is a non-redox flavoprotein, containing FADH2 that is used for stabilization of a transition state. Lycopene has a psi-end group at both ends. When acting on one end, the enzyme forms gamma-carotene. When acting on both ends it forms beta-carotene. It also acts on neurosporene to give beta-zeacarotene.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
lycopene
beta-carotene
show the reaction diagram
-
-
-
?
additional information
?
-
CCS is mainly dedicated to the synthesis of kappa-cyclic carotenoids (capsanthin and capsorubin) but also has lycopene beta-cyclase activity
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
the enzyme contains one noncovalently bound FAD that is essential for enzyme activity only in the presence of NADPH, which functions as the FAD reductant
NADPH
the enzyme contains one noncovalently bound FAD that is essential for enzyme activity only in the presence of NADPH, which functions as the FAD reductant
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(4-chlorophenylthio)-triethylamine
0.4 mM, complete inhibition
2-(4-methyl-phenoxy)-triethylamine
0.1 mM, complete inhibition
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
lycopene cyclase transcript is detected at all stages of leaf and fruit development. There is no significant increase in lycopene cyclase transcript level during fruit ripening. The latter transcript level is approximately five to 10 times higher in young leaves than in senescing leaves and fruits
Manually annotated by BRENDA team
lycopene cyclase transcript is detected at all stages of leaf and fruit development. There is no significant increase in lycopene cyclase transcript level during fruit ripening. The latter transcript level is approximately five to 10 times higher in young leaves than in senescing leaves and fruits
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LCYB_CAPAN
498
0
55626
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
1 * 66000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 66000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D127A
the mutation drastically reduces the lycopene cyclase activity of CCS up to 90%
D259A
the mutation drastically reduces the lycopene cyclase activity of CCS up to 90%
E128A
the mutation drastically reduces the lycopene cyclase activity of CCS up to 90%
E296A
the mutation reduces the lycopene cyclase activity of CCS
E332A
the mutation drastically reduces the lycopene cyclase activity of CCS up to 90%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography, Affigel 501 gel filtration, Mono-P column chromatography, and Sephacryl gel filtration, and Superose 6 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli TOPO10 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hugueney, P.; Badillo, A.; Chen, H.C.; Klein, A.; Hirschberg, J.; Camara, B.; Kuntz, M.
Metabolism of cyclic carotenoids: a model for the alteration of this biosynthetic pathway in Capsicum annuum chromoplasts
Plant J.
8
417-424
1995
Capsicum annuum (Q43415), Capsicum annuum, Capsicum annuum cv. Yolo Wonder (Q43415)
Manually annotated by BRENDA team
Mialoundama, A.S.; Heintz, D.; Jadid, N.; Nkeng, P.; Rahier, A.; Deli, J.; Camara, B.; Bouvier, F.
Characterization of plant carotenoid cyclases as members of the flavoprotein family functioning with no net redox change
Plant Physiol.
153
970-979
2010
Capsicum annuum (Q42435)
Manually annotated by BRENDA team