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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.13.122 - chlorophyllide-a oxygenase and Organism(s) Dunaliella salina and UniProt Accession Q9XJ38

for references in articles please use BRENDA:EC1.14.13.122
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Chlorophyll b is required for the assembly of stable light-harvesting complexes (LHCs) in the chloroplast of green algae, cyanobacteria and plants [2,3]. Contains a mononuclear iron centre . The enzyme catalyses two successive hydroxylations at the 7-methyl group of chlorophyllide a. The second step yields the aldehyde hydrate, which loses H2O spontaneously to form chlorophyllide b . Chlorophyll a and protochlorophyllide a are not substrates .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Dunaliella salina
UNIPROT: Q9XJ38
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: Dunaliella salina
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
chlorophyllide a oxygenase, chlorophyll a oxygenase, oscao1, zmcao1, atptc52, pchlide a oxygenase, chlorophyllide a oxygenase 1, chlorophyll a oxygenase/chlorophyll b synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chlorophyll a oxygenase
-
chlorophyllide a oxygenase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
chlorophyllide-a:oxygen 7-oxidoreductase
Chlorophyll b is required for the assembly of stable light-harvesting complexes (LHCs) in the chloroplast of green algae, cyanobacteria and plants [2,3]. Contains a mononuclear iron centre [3]. The enzyme catalyses two successive hydroxylations at the 7-methyl group of chlorophyllide a. The second step yields the aldehyde hydrate, which loses H2O spontaneously to form chlorophyllide b [2]. Chlorophyll a and protochlorophyllide a are not substrates [2].
CAS REGISTRY NUMBER
COMMENTARY hide
216503-73-0
-
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
?
-
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
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fragment containing the CAO gene
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAO_DUNSA
463
0
51532
Swiss-Prot
other Location (Reliability: 4)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression analysis with isolated nuclei
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Masuda, T.; Tanaka, A.; Melis, A.
Chlorophyll antenna size adjustments by irradiance in Dunaliella salina involve coordinate regulation of chlorophyll a oxygenase (CAO) and Lhcb gene expression
Plant Mol. Biol.
51
757-771
2003
Dunaliella salina (Q9XJ38), Dunaliella salina
Manually annotated by BRENDA team