BCDO2_MUSPF
ID BCDO2_MUSPF Reviewed; 541 AA.
AC Q6QT07;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Carotenoid-cleaving dioxygenase, mitochondrial {ECO:0000305|PubMed:16672231};
DE EC=1.13.11.- {ECO:0000269|PubMed:16672231, ECO:0000269|PubMed:21081106};
DE EC=1.13.11.71 {ECO:0000269|PubMed:16672231};
DE AltName: Full=Beta,beta-carotene 9',10'-oxygenase {ECO:0000250|UniProtKB:Q9BYV7};
GN Name=BCO2 {ECO:0000250|UniProtKB:Q9BYV7};
GN Synonyms=CMO {ECO:0000312|EMBL:AAS20392.1},
GN CMO2 {ECO:0000303|PubMed:16672231};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY LYCOPENE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16672231; DOI=10.1074/jbc.m512095200;
RA Hu K.Q., Liu C., Ernst H., Krinsky N.I., Russell R.M., Wang X.D.;
RT "The biochemical characterization of ferret carotene-9',10'-monooxygenase
RT catalyzing cleavage of carotenoids in vitro and in vivo.";
RL J. Biol. Chem. 281:19327-19338(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21081106; DOI=10.1016/j.abb.2010.11.005;
RA Mein J.R., Dolnikowski G.G., Ernst H., Russell R.M., Wang X.D.;
RT "Enzymatic formation of apo-carotenoids from the xanthophyll carotenoids
RT lutein, zeaxanthin and beta-cryptoxanthin by ferret carotene-9',10'-
RT monooxygenase.";
RL Arch. Biochem. Biophys. 506:109-121(2011).
CC -!- FUNCTION: Broad specificity mitochondrial dioxygenase that mediates the
CC asymmetric oxidative cleavage of carotenoids (PubMed:16672231,
CC PubMed:21081106). Cleaves carotenes (pure hydrocarbon carotenoids) such
CC as all-trans-beta-carotene and lycopene as well as xanthophylls
CC (oxygenated carotenoids) such as zeaxanthin, lutein and beta-
CC cryptoxanthin at both the 9,10 and the 9',10' carbon-carbon double bond
CC (PubMed:16672231, PubMed:21081106). Through its function in carotenoids
CC metabolism regulates oxidative stress and the production of important
CC signaling molecules (By similarity). {ECO:0000250|UniProtKB:Q99NF1,
CC ECO:0000269|PubMed:16672231, ECO:0000269|PubMed:21081106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-beta-carotene + O2 = all-trans-10'-apo-beta-
CC carotenal + beta-ionone; Xref=Rhea:RHEA:26389, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17579, ChEBI:CHEBI:32325, ChEBI:CHEBI:53153;
CC EC=1.13.11.71; Evidence={ECO:0000269|PubMed:16672231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26390;
CC Evidence={ECO:0000305|PubMed:16672231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-trien-
CC 2-one + 5-cis-10'-apo-lycopenal; Xref=Rhea:RHEA:68444,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:67207, ChEBI:CHEBI:177905,
CC ChEBI:CHEBI:177906; Evidence={ECO:0000269|PubMed:16672231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68445;
CC Evidence={ECO:0000305|PubMed:16672231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-
CC trien-2-one + 13-cis-10'-apo-lycopenal; Xref=Rhea:RHEA:68448,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:67207, ChEBI:CHEBI:177907,
CC ChEBI:CHEBI:177908; Evidence={ECO:0000269|PubMed:16672231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68449;
CC Evidence={ECO:0000305|PubMed:16672231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein + O2 = (3R)-3-hydroxy-10'-apo-beta-carotenal + (3R,6R)-
CC hydroxy-alpha-ionone; Xref=Rhea:RHEA:68428, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:177902, ChEBI:CHEBI:177904;
CC Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68429;
CC Evidence={ECO:0000269|PubMed:21081106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein + O2 = (3R)-hydroxy-beta-ionone + (3R,6R)-3-hydroxy-
CC 10'-apo-alpha-carotenal; Xref=Rhea:RHEA:68432, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:53173, ChEBI:CHEBI:177903;
CC Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68433;
CC Evidence={ECO:0000269|PubMed:21081106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone +
CC 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial; Xref=Rhea:RHEA:26393,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:53173; Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26394;
CC Evidence={ECO:0000305|PubMed:21081106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + O2 = (3R)-3-hydroxy-10'-apo-beta-
CC carotenal + (3R)-hydroxy-beta-ionone; Xref=Rhea:RHEA:68104,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53173,
CC ChEBI:CHEBI:177902; Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68105;
CC Evidence={ECO:0000305|PubMed:21081106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-cryptoxanthin + O2 = (3R)-hydroxy-beta-ionone + all-
CC trans-10'-apo-beta-carotenal; Xref=Rhea:RHEA:68440,
CC ChEBI:CHEBI:10362, ChEBI:CHEBI:15379, ChEBI:CHEBI:53153,
CC ChEBI:CHEBI:53173; Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68441;
CC Evidence={ECO:0000269|PubMed:21081106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-10'-apo-beta-carotenal + O2 = 4,9-dimethyldodeca-
CC 2,4,6,8,10-pentaenedial + beta-ionone; Xref=Rhea:RHEA:68452,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32325, ChEBI:CHEBI:53153,
CC ChEBI:CHEBI:53171; Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68453;
CC Evidence={ECO:0000269|PubMed:21081106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxy-10'-apo-beta-carotenal + O2 = (3R)-hydroxy-
CC beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial;
CC Xref=Rhea:RHEA:68424, ChEBI:CHEBI:15379, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:53173, ChEBI:CHEBI:177902;
CC Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68425;
CC Evidence={ECO:0000305|PubMed:21081106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,6R)-3-hydroxy-10'-apo-alpha-carotenal + O2 = (3R,6R)-
CC hydroxy-alpha-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial;
CC Xref=Rhea:RHEA:68436, ChEBI:CHEBI:15379, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:177903, ChEBI:CHEBI:177904;
CC Evidence={ECO:0000269|PubMed:21081106};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68437;
CC Evidence={ECO:0000269|PubMed:21081106};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:16672231};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:16672231};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 uM for all-trans-beta-carotene {ECO:0000269|PubMed:16672231};
CC KM=51.7 uM for all-trans-zeaxanthin {ECO:0000269|PubMed:21081106};
CC KM=49.6 uM for lutein {ECO:0000269|PubMed:21081106};
CC KM=80.8 uM for beta-cryptoxanthin {ECO:0000269|PubMed:21081106};
CC Vmax=32.3 pmol/h/mg enzyme for the formation of all-trans-10'-apo-
CC beta-carotenal {ECO:0000269|PubMed:16672231};
CC Vmax=48.4 pmol/min/mg enzyme for the cleavage of all-trans-zeaxanthin
CC {ECO:0000269|PubMed:21081106};
CC Vmax=69.9 pmol/min/mg enzyme for the cleavage of lutein
CC {ECO:0000269|PubMed:21081106};
CC Vmax=34.3 pmol/min/mg enzyme for the cleavage of beta-cryptoxanthin
CC {ECO:0000269|PubMed:21081106};
CC pH dependence:
CC Optimum pH is 8.0-8.5 with all-trans-beta-carotene as substrate.
CC {ECO:0000269|PubMed:16672231};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99NF1}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in heart, spleen, lung,
CC intestine, colon, stomach, kidney, bladder, and prostate. Highly
CC expressed in liver and testis (at protein level).
CC {ECO:0000269|PubMed:16672231}.
CC -!- INDUCTION: Up-regulated by lycopene. {ECO:0000269|PubMed:16672231}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AY527150; AAS20392.1; -; mRNA.
DR RefSeq; NP_001297121.1; NM_001310192.1.
DR GeneID; 101670802; -.
DR CTD; 83875; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0010437; F:9,10 (9', 10')-carotenoid-cleaving dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0102076; F:beta,beta-carotene-9',10'-cleaving oxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; IDA:UniProtKB.
DR GO; GO:0062172; P:lutein catabolic process; IDA:UniProtKB.
DR GO; GO:1901176; P:lycopene catabolic process; IDA:UniProtKB.
DR GO; GO:0016124; P:xanthophyll catabolic process; IDA:UniProtKB.
DR GO; GO:1901826; P:zeaxanthin catabolic process; IDA:UniProtKB.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Lipid metabolism; Metal-binding; Mitochondrion;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..541
FT /note="Carotenoid-cleaving dioxygenase, mitochondrial"
FT /id="PRO_0000454467"
FT BINDING 188
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 248
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 319
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 535
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
SQ SEQUENCE 541 AA; 61162 MW; 42AA5DEC6A514649 CRC64;
MEGTDQKKAA VGTREGLPCI APLLTTVEET PQVVSAQVRG HFPKWLSGSL LRIGPGKFEF
GKDKYNHWFD GMALLHQFKM EKGMVTYRSK FLQSDTYKTN SVHDRIVISE FGTLALPDPC
KNVFERFMSK FELPAITDNT SVNYVRYKGD YYVSTETNFM NKVDIETLEK TEKVDWSKFI
AVNGATAHPH YDPDGTAYNM GNSYGLHGSC YNVIRVPPEK VDLGETLHGA QVICSIASTE
RMKPSYYHSF GMTRNYIIFI EQPLKMNLWK MITSRIRGMA FSDGISWEPQ YNTRFHVVDK
NTGQLLPGMY YSKPFVTFHQ INAFEDQGCV VLDLCCQDDG RSLEAYRLQN LRKAGAGLDQ
VYNSVGRSFP RRFVLPLHVS LNDPEGENLS PLSYSSASAV KQANGKIWCS YENLHPEDLE
EEGGVEFPQI NYGQFSGKKY RFFYGCGFRH LVGDSLIKLD VVNKTLMIWR EDGFYPSEPV
FVPAPGASEE DGGVILSVVI TPDQNENNFL LVLDAKNFEE LGRAEVPVRM PYGFHGTFVT
V
