KEGG   ENZYME: 1.13.11.63Help
Entry
EC 1.13.11.63               Enzyme                                 

Name
beta-carotene 15,15'-dioxygenase;
blh (gene name);
BCO1 (gene name);
BCDO (gene name);
carotene dioxygenase;
carotene 15,15'-dioxygenase;
BCMO1 (misleading);
beta-carotene 15,15'-monooxygenase (incorrect)
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname
beta-carotene:oxygen 15,15'-dioxygenase (bond-cleaving)
Reaction(IUBMB)
beta-carotene + O2 = 2 all-trans-retinal [RN:R00032]
Reaction(KEGG)
Substrate
beta-carotene [CPD:C02094];
O2 [CPD:C00007]
Product
all-trans-retinal [CPD:C00376]
Comment
Requires Fe2+. The enzyme cleaves beta-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products [8]. The enzyme can also process beta-cryptoxanthin, 8'-apo-beta-carotenal, 4'-apo-beta-carotenal, alpha-carotene and gamma-carotene in decreasing order. The presence of at least one unsubstituted beta-ionone ring in a substrate greater than C(30) is mandatory [5]. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].
History
EC 1.13.11.63 created 2012 (EC 1.14.99.36 created 1972 as EC 1.13.11.21, transferred 2001 to EC 1.14.99.36, incorporated 2015), modified 2016
Pathway
Retinol metabolism
Metabolic pathways
Orthology
K00515  
beta-carotene 15,15'-dioxygenase
K21817  
beta-carotene 15,15'-dioxygenase
Genes
HSA: 
53630(BCO1)
PTR: 
468043(BCO1)
PPS: 
100987572(BCO1)
GGO: 
101132534(BCO1)
PON: 
100454129(BCMO1)
NLE: 
100603806(BCO1)
MCC: 
721412(BCO1)
MCF: 
102121880(BCO1)
CSAB: 
103233367(BCO1)
RRO: 
104671629(BCO1)
RBB: 
108539495(BCO1)
CJC: 
100393264(BCO1)
SBQ: 
101032680(BCO1)
MMU: 
63857(Bco1)
RNO: 
114106(Bco1)
CGE: 
100760350(Bco1)
NGI: 
103732128(Bco1)
HGL: 
101724039(Bco1)
CCAN: 
109696646(Bco1)
OCU: 
100358087(BCO1)
TUP: 
102484616(BCO1)
CFA: 
489695(BCO1)
AML: 
100483748(BCO1)
UMR: 
103662084(BCO1)
FCA: 
101101606(BCO1)
PTG: 
102959940(BCO1)
AJU: 
106984030(BCO1)
BTA: 
534696(BCO1)
BOM: 
102266127(BCO1)
BIU: 
109572100(BCO1)
PHD: 
102315733(BCO1)
CHX: 
102179507(BCO1)
OAS: 
100294509(BCMO1) 101121875(BCO1)
SSC: 
100192320(BCO1)
CFR: 
102513983(BCO1)
CDK: 
105089436(BCO1)
BACU: 
103015035(BCO1)
LVE: 
103072015(BCO1)
ECB: 
100069873(BCO1)
EPZ: 
103554670(BCO1)
EAI: 
106833126(BCO1)
MYB: 
102263079(BCO1)
MYD: 
102771959(BCO1)
HAI: 
109378342(BCO1)
RSS: 
109434307(BCO1)
PALE: 
102897588(BCO1)
MDO: 
100031779(BCO1)
SHR: 
100920512(BCO1)
OAA: 
103171493(BCO1)
GGA: 
395346(BCO1)
MGP: 
100549225(BCO1)
CJO: 
107319380(BCO1)
APLA: 
101798614(BCO1)
ACYG: 
106033290(BCO1)
TGU: 
100228904(BCO1)
GFR: 
102040064(BCO1)
FAB: 
101812113(BCO1)
PHI: 
102103988(BCO1)
PMAJ: 
107209839(BCO1)
CCW: 
104691821(BCO1)
FPG: 
101914506(BCO1)
FCH: 
102058462(BCO1)
CLV: 
102086476(BCO1)
AAM: 
106483349(BCO1)
ASN: 
102378066(BCO1)
AMJ: 
102573601(BCO1)
PSS: 
102455966(BCO1)
CMY: 
102929893(BCO1)
CPIC: 
101934984(BCO1)
ACS: 
100563614(bco1)
PVT: 
110085493(BCO1)
GJA: 
107105786(BCO1)
XLA: 
108714030(bco1.L)
XTR: 
100486582(bco1)
NPR: 
108786164(BCO1)
DRE: 
393580(bco1l) 84039(bco1)
SRX: 
SANH: 
SGH: 
IPU: 
AMEX: 
TRU: 
TNG: 
LCO: 
NCC: 
MZE: 
OLA: 
XMA: 
CSEM: 
LCF: 
HCQ: 
BPEC: 
SASA: 
ELS: 
SFM: 
LCM: 
102362963(BCO1)
CMK: 
103175958(bco1)
BFO: 
CIN: 
778841(bco)
SPU: 
FCD: 
ISC: 
NAI: 
LGI: 
LAK: 
PAM: 
PLF: 
PAJ: 
PAQ: 
PVA: 
VHA: 
VCA: 
POR: 
PPSL: 
MBS: 
MPQ: 
GNI: 
GPS: 
HJA: 
LHA: 
TCY: 
SSAL: 
SPIU: 
KUS: 
KMA: 
VAA: 
MBAC: 
MBAT: 
SMUL: 
SHAL: 
SULS: 
MDI: 
MCH: 
MET: 
MAQU: 
MZA: 
OAT: 
OAR: 
SSAN: 
SPHR: 
EGN: 
ANH: 
ABG: 
PUB: 
PEL: 
APC: 
APM: 
APB: 
RPLA: 
GOB: 
PLAN: 
PLAK: 
RXY: 
TTL: 
TOS: 
TAQ: 
IPA: 
PHM: 
SRU: 
SRM: 
HHY: 
ALM: 
SLI: 
RSI: 
FIB: 
HYE: 
HYP: 
HYZ: 
MTT: 
KDI: 
DOK: 
DDO: 
PTQ: 
NDO: 
NOM: 
NSD: 
POM: 
WIN: 
WIJ: 
SYI: 
FOR: 
FOH: 
BBAU: 
HAL: 
HSL: 
OE_3102R(brp) OE_3980R(blh)
HHB: 
HMA: 
HHI: 
HAH_2414(brp) HAH_2561(blh)
HHN: 
HAB: 
NPH: 
NP_0206A(brp) NP_0650A(blh)
NMO: 
HUT: 
HTI: 
HMU: 
HWA: 
HWC: 
HLA: 
HXA: 
NAT: 
NPE: 
NGE: 
HLC: 
NAJ: 
 » show all
Taxonomy
Reference
1  [PMID:5946623]
  Authors
Goodman DS, Huang HS, Shiratori T.
  Title
Mechanism of the biosynthesis of vitamin A from beta-carotene.
  Journal
J. Biol. Chem. 241 (1966) 1929-32.
Reference
2
  Authors
Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T.
  Title
The enzymatic conversion of all-trans beta-carotene into retinal.
  Journal
J. Biol. Chem. 242 (1967) 3543-3554.
Reference
3  [PMID:11401432]
  Authors
Yan W, Jang GF, Haeseleer F, Esumi N, Chang J, Kerrigan M, Campochiaro M, Campochiaro P, Palczewski K, Zack DJ
  Title
Cloning and characterization of a human beta,beta-carotene-15,15'-dioxygenase that is highly expressed in the retinal pigment epithelium.
  Journal
Genomics. 72 (2001) 193-202.
  Sequence
[hsa:53630] [mmu:63857]
Reference
4  [PMID:11458349]
  Authors
Leuenberger MG, Engeloch-Jarret C, Woggon WD.
  Title
The Reaction Mechanism of the Enzyme-Catalyzed Central Cleavage of beta-Carotene  to Retinal This research was supported by F. Hoffmann-La Roche AG and the Swiss National Science Foundation. We are grateful to F. Hoffmann-La Roche AG for a generous gift of carotenoids and Dr. Claus Bornemann for preliminary experiments.
  Journal
Angew. Chem. Int. Ed. Engl. 40 (2001) 2613-2617.
Reference
5  [PMID:18979213]
  Authors
Kim YS, Oh DK
  Title
Substrate specificity of a recombinant chicken beta-carotene 15,15'-monooxygenase that converts beta-carotene into retinal.
  Journal
Biotechnol. Lett. 31 (2009) 403-8.
Reference
6  [PMID:19366683]
  Authors
Kim YS, Kim NH, Yeom SJ, Kim SW, Oh DK
  Title
In vitro characterization of a recombinant Blh protein from an uncultured marine  bacterium as a beta-carotene 15,15'-dioxygenase.
  Journal
J. Biol. Chem. 284 (2009) 15781-93.
  Sequence
Reference
7  [PMID:20229064]
  Authors
Kim YS, Park CS, Oh DK
  Title
Retinal production from beta-carotene by beta-carotene 15,15'-dioxygenase from an unculturable marine bacterium.
  Journal
Biotechnol. Lett. 32 (2010) 957-61.
  Sequence
Reference
8  [PMID:24668807]
  Authors
dela Sena C, Riedl KM, Narayanasamy S, Curley RW Jr, Schwartz SJ, Harrison EH.
  Title
The human enzyme that converts dietary provitamin A carotenoids to vitamin A is a dioxygenase.
  Journal
J. Biol. Chem. 289 (2014) 13661-6.
  Sequence
[hsa:53630]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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