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Information on EC 1.13.11.65 - carotenoid isomerooxygenase
for references in articles please use BRENDA:EC1.13.11.65
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EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.11 With incorporation of two atoms of oxygen
1.13.11.65 carotenoid isomerooxygenase
IUBMB Comments
The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including β-carotene, α-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.13.11.65
- pacifica
-
carotenoids
-
apocarotenoids
-
lymphoma
- oxygenases
-
ifn-resistant
Reaction Schemes
showSynonyms
sir-1, carotenoid isomerooxygenase, sala_1698, rv0654, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carotenoid cleavage oxygenase
CCO
CSO2
NinaB
Rv0654
NinaB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
11-cis-3-hydroxyretinal biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
zeaxanthin:oxygen 15,15'-oxidoreductase (bond-cleaving, cis-isomerizing)
The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including beta-carotene, alpha-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxy-beta-apo-10'-carotenal + O2
3-hydroxy-beta-apo-13-carotenone + 3-hydroxy-beta-apo-15-carotenal
Substrates: -
Products: plus a minor product presumably representing 3-hydroxy-beta-apo-11-carotenal
Products: plus a minor product presumably representing 3-hydroxy-beta-apo-11-carotenal
?
3-hydroxy-beta-apo-8'-carotenal + O2
?
Substrates: -
Products: -
Products: -
?
astaxanthin + O2
?
-
Substrates: -
Products: single cleavage site at the 13'/14' double bond
Products: single cleavage site at the 13'/14' double bond
?
beta-apo-10'-carotenal + O2
beta-apo-13-carotenone
Substrates: -
Products: plus minor amounts of beta-apo-15-carotenal
Products: plus minor amounts of beta-apo-15-carotenal
?
beta-apo-8'-carotenal + O2
beta-apo-13-carotenone + retinal
Substrates: -
Products: -
Products: -
?
beta-carotene + O2
retinal + beta-apo-14'-carotenal + beta-apo-13-carotenone
Substrates: -
Products: -
Products: -
?
canthaxanthin + O2
?
-
Substrates: -
Products: two cleavage sites at the 11'/12' or 13'/14' double bond
Products: two cleavage sites at the 11'/12' or 13'/14' double bond
?
cryptoxanthin + O2
11-cis-3-hydroxyretinal + 11-cis-retinal
Substrates: -
Products: 11-cis-3-hydroxyretinal and 11-cis-retinal exist in a molar ratio of 8:1, indicating that the enzyme preferentially isomerizes the half site of cryptoxanthin with the hydroxylated beta-ionone ring
Products: 11-cis-3-hydroxyretinal and 11-cis-retinal exist in a molar ratio of 8:1, indicating that the enzyme preferentially isomerizes the half site of cryptoxanthin with the hydroxylated beta-ionone ring
?
nostoxanthin + O2
?
-
Substrates: -
Products: two cleavage sites at the 11'/12' or 13'/14' double bond
Products: two cleavage sites at the 11'/12' or 13'/14' double bond
?
zeaxanthin + O2
(3R)-all-trans-3-hydroxyretinal + (3R)-11-cis-3-hydroxyretinal
Substrates: -
Products: -
Products: -
?
4-vinylguaiacol + O2
vanillin
Substrates: -
Products: -
Products: -
?
apo-8'-carotenal + O2
?
-
Substrates: -
Products: cleavage at the 9'/10'- and 11'/12'-double bond
Products: cleavage at the 9'/10'- and 11'/12'-double bond
?
apo-8'-carotenal + O2
?
Substrates: -
Products: cleavage at the 9'/10'- and 11'/12'-double bond
Products: cleavage at the 9'/10'- and 11'/12'-double bond
?
beta,beta-carotene + O2
all-trans-retinal + 11-cis-retinal
Substrates: -
Products: -
Products: -
?
beta,beta-carotene + O2
all-trans-retinal + 11-cis-retinal
Substrates: -
Products: enzyme catalyzes the production of 11-cis-retinal and all-trans-retinal, i.e. cleavage at the 15,15' double bond. The 11-cis-retinal product maybe thermally converted either into the all-trans or the 13-cis stereoisomer in the aqueous test solution
Products: enzyme catalyzes the production of 11-cis-retinal and all-trans-retinal, i.e. cleavage at the 15,15' double bond. The 11-cis-retinal product maybe thermally converted either into the all-trans or the 13-cis stereoisomer in the aqueous test solution
?
dihydroxylycopene + O2
?
-
Substrates: i.e. 1,2,1',2'-tetrahydro-psi,psi-carotene-1,1'-diol
Products: -
Products: -
?
dihydroxylycopene + O2
?
Substrates: i.e. 1,2,1',2'-tetrahydro-psi,psi-carotene-1,1'-diol
Products: -
Products: -
?
hydroxylycopene + O2
?
-
Substrates: i.e. 1,2-dihydro-psi,psi-carotene-1-ol
Products: -
Products: -
?
hydroxylycopene + O2
?
Substrates: i.e. 1,2-dihydro-psi,psi-carotene-1-ol
Products: -
Products: -
?
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
Substrates: -
Products: beta-carotene is first converted to zeaxanthin and then cleaved by the enzmye to directly yield 3-hydroxy-retinal
Products: beta-carotene is first converted to zeaxanthin and then cleaved by the enzmye to directly yield 3-hydroxy-retinal
?
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
Substrates: -
Products: -
Products: -
?
zeaxanthin + O2
?
-
Substrates: -
Products: two cleavage sites at the 11'/12' or 13'/14' double bond
Products: two cleavage sites at the 11'/12' or 13'/14' double bond
?
additional information
?
-
Substrates: enzyme combines isomerase and isomerooxygenase activity in a single polypeptide
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme combines isomerase and isomerooxygenase activity in a single polypeptide
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme cleaves the central C15-C15' and an excentric double bond at the C13-C14 position, leading to retinal (C20), beta-apo-14'-carotenal (C22) and beta-apo-13-carotenone (C18) from beta-carotene, as well as the corresponding hydroxylated products from zeaxanthin and lutein. Enzyme also cleaves 3,3'-dihydroxy-isorenieratene representing aromatic carotenoids synthesized by other mycobacteria. The preference for each of the cleavage positions is determined by the hydroxylation and the nature of the ionone ring. Incubation of apocarotenoids shorter than beta-apo-10'-carotenal reveals only weak activity, substrates with a shorter chain length are not converted
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme cleaves the central C15-C15' and an excentric double bond at the C13-C14 position, leading to retinal (C20), beta-apo-14'-carotenal (C22) and beta-apo-13-carotenone (C18) from beta-carotene, as well as the corresponding hydroxylated products from zeaxanthin and lutein. Enzyme also cleaves 3,3'-dihydroxy-isorenieratene representing aromatic carotenoids synthesized by other mycobacteria. The preference for each of the cleavage positions is determined by the hydroxylation and the nature of the ionone ring. Incubation of apocarotenoids shorter than beta-apo-10'-carotenal reveals only weak activity, substrates with a shorter chain length are not converted
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: resveratrol, cholecalciferol, phylloquinone and alpha-tocopherol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: resveratrol, cholecalciferol, phylloquinone and alpha-tocopherol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme carotenoid cleavage requires the presence of either hydroxy or keto groups
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme cleaves acyclic and monocyclic substrates
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
Substrates: -
Products: -
Products: -
?
4-vinylguaiacol + O2
vanillin
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
0.1% (v/v) Triton X-100 significantly inhibits vanillin production (to less than 40%)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycerol
10% (v/v) glycerol slightly (1.2fold) stimulates vanillin production
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
The Mycobacterium tuberculosis ORF Rv0654 encodes a carotenoid oxygenase mediating central and excentric cleavage of conventional and aromatic carotenoids.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
more than 80% activity between pH 6.0 and 10.0. Less than 10% of the maximum activity is retained when the pH is lower than 6.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 30
more than 80% activity between 5 and 30°C. Less than 10% of the maximum activity is retained when the temperature is higher than 30°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
gene expression is eye-dependent and is activated as adownstream target of the eyeless/pax6 and sine oculis master control genes for eye development
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
mutants show no photophobic behavior indicating that NinaB is essential for larval light perception. Enzyme expression and chromophore production is governed by eyeless and so, major control genes for eye development
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NINAB_DROME
620
0
69932
Swiss-Prot
other Location (Reliability: 2)
NINAB_GALME
513
0
57839
Swiss-Prot
other Location (Reliability: 1)
D5VGA0_CAUST
Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / TK0059)
491
0
55021
TrEMBL
-
CCO_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
501
0
54944
Swiss-Prot
-
Q1GSG1_SPHAL
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
480
0
53352
TrEMBL
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A49P
the catalytic efficiency of the mutant is 1.6fold that of the wild type enzyme. The mutant exhibits better thermostability than that of wild type. Under temperatures lower than 30°C, mutant A49P retains almost all the activities within the shorter incubation time (less than 5 h). The mutant also shows better performance even at 35°C
I234A
the mutant shows strongly decreased catalytic efficiency compared to the wild type enzyme
Q390A
the catalytic efficiency of the mutant is 1.64fold that of the wild type enzyme. The mutant exhibits better thermostability than that of wild type
A49P
-
the catalytic efficiency of the mutant is 1.6fold that of the wild type enzyme. The mutant exhibits better thermostability than that of wild type. Under temperatures lower than 30°C, mutant A49P retains almost all the activities within the shorter incubation time (less than 5 h). The mutant also shows better performance even at 35°C
-
I234A
-
the mutant shows strongly decreased catalytic efficiency compared to the wild type enzyme
-
Q390A
-
the catalytic efficiency of the mutant is 1.64fold that of the wild type enzyme. The mutant exhibits better thermostability than that of wild type
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 35
the enzyme retains about 70-90% activity after approximately 3 h at 15-23°C. At 30°C, the enzyme maintains about 50% activity after 3 h incubation. The enzyme is inactivated after about 3 h at 35°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression is eye-dependent and is activated as a downstream target of the eyeless/pax6 and sine oculis master control genes for eye development
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oberhauser, V.; Voolstra, O.; Bangert, A.; von Lintig, J.; Vogt, K.
NinaB combines carotenoid oxygenase and retinoid isomerase activity in a single polypeptide
Proc. Natl. Acad. Sci. USA
105
19000-19005
2008
Drosophila melanogaster (Q9VFS2), Galleria mellonella (A8Y9I2)
brenda
Scherzinger, D.; Scheffer, E.; Bar, C.; Ernst, H.; Al-Babili, S.
The Mycobacterium tuberculosis ORF Rv0654 encodes a carotenoid oxygenase mediating central and excentric cleavage of conventional and aromatic carotenoids
FEBS J.
277
4662-4673
2010
Mycobacterium tuberculosis (P9WPR5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPR5)
brenda
Voolstra, O.; Oberhauser, V.; Sumser, E.; Meyer, N.E.; Maguire, M.E.; Huber, A.; von Lintig, J.
NinaB is essential for Drosophila vision but induces retinal degeneration in opsin-deficient photoreceptors
J. Biol. Chem.
285
2130-2139
2010
Drosophila melanogaster (Q9VFS2)
brenda
Hoffmann, J.; Bona-Lovasz, J.; Beuttler, H.; Altenbuchner, J.
In vivo and in vitro studies on the carotenoid cleavage oxygenases from Sphingopyxis alaskensis RB2256 and Plesiocystis pacifica SIR-1 revealed their substrate specificities and non-retinal-forming cleavage activities
FEBS J.
279
3911-3924
2012
Plesiocystis pacifica SIR-1, Sphingopyxis alaskensis (Q1GSG1)
brenda
Yao, X.; Lv, Y.; Yu, H.; Cao, H.; Wang, L.; Wen, B.; Gu, T.; Wang, F.; Sun, L.; Xin, F.
Site-directed mutagenesis of coenzyme-independent carotenoid oxygenase CSO2 to enhance the enzymatic synthesis of vanillin
Appl. Microbiol. Biotechnol.
104
3897-3907
2020
Caulobacter segnis (D5VGA0), Caulobacter segnis ATCC 21756 (D5VGA0)
brenda
Poliakov, E.; Uppal, S.; Rogozin, I.B.; Gentleman, S.; Redmond, T.M.
Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases
Biochim. Biophys. Acta Mol. Cell Biol. Lipids
1865
158665
2020
Sphingopyxis alaskensis (Q1GSG1)
brenda
EXTERNAL LINKS (specific for EC-Number 1.13.11.65)
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Release 2023.1 (January 2023)
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