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
ec00830  Retinol metabolism
ec01100  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(BCO1)
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)
ORO: 101377344(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)
OOR: 101285979(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)
TMU: 101341485
MDO: 100031779(BCO1)
SHR: 100920512(BCO1)
OAA: 103171493(BCO1)
GGA: 395346(BCMO1)
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)
EGZ: 104133740(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)
TRU: 101076274(bco1) 101078539
NCC: 104954746 104958616(bco1)
PRET: 103457901 103482517(bco1)
LCM: 102362963(BCO1)
CMK: 103175958(bco1)
CIN: 778841(bco)
SPU: 591892
CRG: 105341121
OBI: 106882614
EPA: 110233465
PAM: PANA_1898
PAJ: PAJ_1228
PVA: Pvag_1853
MBS: MRBBS_2788(blh)
GNI: GNIT_0397
GPS: C427_1920
LHA: LHA_1128
SALN: SALB1_1269
SMUL: SMUL_1186
SHAL: SHALO_1176
SULJ: SJPD1_1205
MDI: METDI1925
MCH: Mchl_1482
MET: M446_0536
SSAN: NX02_06035
SPHR: BSY17_1104
ABG: Asbog_01119(blh)
GOB: Gobs_1772
RXY: Rxyl_2039
TAQ: TO73_1641
IPA: Isop_3504
SRU: SRU_0742(brp) SRU_2210
SRM: SRM_00919(brp) SRM_02436
SLI: Slin_1644
DOK: MED134_07114(blh)
DDO: I597_1807
NDO: DDD_0295
POM: MED152_12849(blh)
WIN: WPG_3400
HAL: VNG_1465G(brp) VNG_2136G(blh)
HSL: OE_3102R(brp) OE_3980R(blh)
HHB: Hhub_3440(blh)
HMA: rrnAC1901(brp) rrnAC2066(blh)
HHI: HAH_2414(brp) HAH_2561(blh)
NPH: NP_0206A(brp) NP_0650A(blh)
NMO: Nmlp_1292(blh) Nmlp_3577(brp)
HWA: HQ_1019A(blh) HQ_1864A(brp) HQ_2381A
HWC: Hqrw_1021(blh) Hqrw_2002(brp)
HLA: Hlac_2732
NAT: NJ7G_2814
 » 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 241:1929-32 (1966)
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 242:3543-3554 (1967)
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 72:193-202 (2001)
DOI:10.1006/geno.2000.6476
  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 40:2613-2617 (2001)
DOI:10.1002/1521-3773(20010716)40:14<2613::AID-ANIE2613>3.0.CO;2-Z
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 31:403-8 (2009)
DOI:10.1007/s10529-008-9873-4
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 284:15781-93 (2009)
DOI:10.1074/jbc.M109.002618
  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 32:957-61 (2010)
DOI:10.1007/s10529-010-0239-3
  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 289:13661-6 (2014)
DOI:10.1074/jbc.M114.557710
  Sequence
[hsa:53630]
Other DBs
ExplorEnz - The Enzyme Database: 1.13.11.63
IUBMB Enzyme Nomenclature: 1.13.11.63
ExPASy - ENZYME nomenclature database: 1.13.11.63
BRENDA, the Enzyme Database: 1.13.11.63

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