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Information on EC 1.13.11.75 - all-trans-8'-apo-beta-carotenal 15,15'-oxygenase and Organism(s) Synechocystis sp. and UniProt Accession P74334

for references in articles please use BRENDA:EC1.13.11.75
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IUBMB Comments
Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria .
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Synechocystis sp.
UNIPROT: P74334
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The taxonomic range for the selected organisms is: Synechocystis sp.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
carotenoid cleavage oxygenase, apocarotenoid oxygenase, apocarotenoid-15-15'-oxygenase, sll1541, apocarotenoid cleavage oxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
apocarotenoid cleavage oxygenase
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apocarotenoid-15-15'-oxygenase
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additional information
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ACO belongs to an outgroup of the CCO enzyme family
SYSTEMATIC NAME
IUBMB Comments
all-trans-8'-apo-beta-carotenal:oxygen 15,15'-oxidoreductase (bond-cleaving)
Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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the substrate specificity of the enzyme is unique in that it cleaves only all-trans apocarotenoids of different chain lengths, but not C40 beta-carotene to yield all-trans C20 retinal or its derivatives
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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the substrate specificity of the enzyme is unique in that it cleaves only all-trans apocarotenoids of different chain lengths, but not C40 beta-carotene to yield all-trans C20 retinal or its derivatives
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?
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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plant CCD1 enzymes and the NosCCD might have evolved into ACOs without losing their ability to cleave C40 carotenoids
physiological function
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role of CCD1 as an ACO of C27 apocarotenoid intermediates, following their predicted export from plastid to cytosol
additional information
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importance of sequential cleavage reactions of C40 carotenoid precursors, the apocarotenoid cleavage oxygenase, ACO, nature of several carotenoid cleavage oxygenases and the topic of compartmentation. ACO belongs to an outgroup of the CCO enzyme family, but in the mycorrhizal root system suggest CCD1 to preferentially act as an apocarotenoid oxygenase, ACO, in planta cleaving C27 and perhaps other apocarotenoids, enzyme parameters, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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three-dimensional structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional structure analysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walter, M.H.; Floss, D.S.; Strack, D.
Apocarotenoids: hormones, mycorrhizal metabolites and aroma volatiles
Planta
232
1-17
2010
Synechocystis sp.
Manually annotated by BRENDA team