Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.13.11.65 - carotenoid isomerooxygenase and Organism(s) Drosophila melanogaster and UniProt Accession Q9VFS2

for references in articles please use BRENDA:EC1.13.11.65
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Drosophila melanogaster
UNIPROT: Q9VFS2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sir-1, sala_1698, carotenoid isomerooxygenase, rv0654, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NinaB
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta,beta-carotene + O2
all-trans-retinal + 11-cis-retinal
show the reaction diagram
-
-
-
?
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
show the reaction diagram
-
beta-carotene is first converted to zeaxanthin and then cleaved by the enzmye to directly yield 3-hydroxy-retinal
-
?
additional information
?
-
enzyme combines isomerase and isomerooxygenase activity in a single polypeptide
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NINAB_DROME
620
0
69932
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team