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) Galleria mellonella and UniProt Accession A8Y9I2

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:
Galleria mellonella
UNIPROT: A8Y9I2
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: Galleria mellonella
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sir-1, carotenoid isomerooxygenase, sala_1698, 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
alpha-carotene + O2
?
show the reaction diagram
-
-
-
?
beta,beta-carotene + O2
all-trans-retinal + 11-cis-retinal
show the reaction diagram
-
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
-
?
cryptoxanthin + O2
11-cis-3-hydroxyretinal + 11-cis-retinal
show the reaction diagram
-
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
-
?
lutein + O2
?
show the reaction diagram
-
-
-
?
zeaxanthin + O2
(3R)-all-trans-3-hydroxyretinal + (3R)-11-cis-3-hydroxyretinal
show the reaction diagram
-
-
-
?
additional information
?
-
enzyme combines isomerase and isomerooxygenase activity in a single polypeptide
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0221
alpha-carotene
pH 6.8, 20°C
0.0104
beta,beta-carotene
pH 6.8, 20°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0082
alpha-carotene
pH 6.8, 20°C
0.0087
beta,beta-carotene
pH 6.8, 20°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NINAB_GALME
513
0
57839
Swiss-Prot
other Location (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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