Information on EC 1.14.99.36 - beta-carotene 15,15'-monooxygenase

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY
1.14.99.36
-
RECOMMENDED NAME
GeneOntology No.
beta-carotene 15,15'-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
15,15'-dihydroxy-beta-carotene + A = 2 all-trans-retinal + AH2
show the reaction diagram
(1c)
-
-
-
beta-carotene + O2 + AH2 = beta-carotene 15,15'-epoxide + H2O + A
show the reaction diagram
(1a)
-
-
-
beta-carotene + O2 = 2 all-trans retinal
show the reaction diagram
overall reaction
-
-
-
beta-carotene + O2 = 2 all-trans retinal
show the reaction diagram
mechanism
-
beta-carotene 15,15'-epoxide + H2O = 15,15'-dihydroxy-beta-carotene
show the reaction diagram
(1b)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
oxidation
Q9VFS2
-
oxidation
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
-
reduction
Q9VFS2
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
retinol biosynthesis
-
Retinol metabolism
-
SYSTEMATIC NAME
IUBMB Comments
beta-carotene:oxygen 15,15'-oxidoreductase (bond-cleaving)
Requires bile salts and Fe(II). This animal enzyme catalyses the reaction in three stages, epoxidation of the 15,15'-double bond, hydration of the epoxide leading to ring opening, and oxidative cleavage of the diol formed. Thus only one atom of the dioxygen is incorporated into each retinal molecule. The nature of the acceptor listed in reactions (1a) and (1c) is assumed to be iron within the active site. Formerly classified in EC 1.13.11 as it had been thought to be a dioxygenase. cf. EC 1.13.11.63, beta-carotene 15,15'-dioxygenase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15,15'-carotenoid monooxygenase
-
-
15,15'-mono-oxygenase
-
-
BCM
-
gene name
BCM
Rattus norvegicus Zucker
-
gene name
-
BCMO
Q9HAY6
-
Bcmo1
Q9HAY6
-
Bcmo1
Q9JJS6
-
Bcmo1
C7C6F6
gene name
BCO1
-
-
BCO2
C1L3B1
gene name
Bcox
Q90WH4
-
beta,beta-carotene 15,15'-monooxygenase
Q9HAY6
-
beta,beta-carotene oxygenase 1
-
-
beta,beta-carotene-15,15'-oxygenase
-
-
beta,beta-carotene-15,15'-oxygenase
Q90WH4
-
beta-carotene 15,15' monooxygenase
-
-
beta-carotene 15,15' monooxygenase
Rattus norvegicus Zucker
-
-
-
beta-carotene 15,15'-dioxygenase
-
-
-
-
beta-carotene 15,15'-monooxygenase
Q9I993
-
beta-carotene 15,15'-monooxygenase
-
-
beta-carotene 15,15'-monooxygenase
Q9HAY6
-
beta-carotene 15,15'-monooxygenase
Q9JJS6
-
beta-carotene 15,15'-monooxygenase
-
-
beta-carotene 15,15'-monooxygenase 1
C7C6F6
-
beta-carotene 15,15'-monoxygenase
Q9HAY6
-
beta-carotene 15,15-monooxygenase
Q9HAY6
-
beta-carotene oxygenase 2
C1L3B1
-
beta-carotene-15,15'-monooxygenase
-
-
beta-carotene-15,15'-monooxygenase
Q9HAY6
-
beta-carotene-15,15'-monooxygenase
-
-
beta-CD
-
-
betaCDIOX
-
-
betaCO
-
-
carotene 15,15'-dioxygenase
-
-
-
-
carotene dioxygenase
-
-
-
-
carotenoid oxygenase
Q9VFS2
-
carotenoid oxygenase
-
-
CDO
-
-
-
-
CMO I
-
-
CMO1
-
-
EC 1.13.11.21
-
-
formerly
-
oxygenase, beta-carotene 15,15'-di-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37256-60-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cattle
-
-
Manually annotated by BRENDA team
cattle with pigmented or non-pigmented, i.e. yellow or white, fat
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Domania subtryug
-
-
-
Manually annotated by BRENDA team
gene Bcmo1
-
-
Manually annotated by BRENDA team
recombinant enzyme
SwissProt
Manually annotated by BRENDA team
no activity in Felis catus
intestine
-
-
Manually annotated by BRENDA team
gene bco2; gene BCO2
UniProt
Manually annotated by BRENDA team
gene bmco1; gene Bcmo1
UniProt
Manually annotated by BRENDA team
Goto-Kakizaki rat
-
-
Manually annotated by BRENDA team
male obese Zucker rats, gene BCM
-
-
Manually annotated by BRENDA team
male wistar rat
-
-
Manually annotated by BRENDA team
Rattus norvegicus Zucker
male obese Zucker rats, gene BCM
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
C1L3B1, C7C6F6, -
a nonsense mutation c.196C-T in the beta-carotene oxygenase 2 BCO2 gene is strongly associated with the yellow fat phenotype in sheep that is caused by accumulation of carotenoids in adipose tissue, a recessive trait. But animals homozygous for the mutation do not suffer from any negative health or development traits, pointing towards a minor role of BCO2 in vitamin A formation
metabolism
-
carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
physiological function
-
enzyme deletion mutants show a significant increase in the total carotenoid content
physiological function
-
beta-carotene cleavage oxygenase determines the beta-carotene content of the cell. Deletion of the cco1 gene, does not affect growth, morphology or pathogenicity
physiological function
-
larvae of ninaB mutants show no photophobic behavior indicating that NinaB is essential for larval light perception. ninaB mutant flies exhibit impaired chromophore production and consequently lack visual pigments. Visual pigment production essentially depends on NinaB
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development. Model of the putative mechanism for the regulation of BCMO1 by dietary fat and PPARgamma, overview
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
C1L3B1, C7C6F6, -
quantitatively important role for BCO2 in carotenoid degradation, which might indicate a broad enzyme specificity for carotenoids
physiological function
-
increased intestinal enzyme expression occurs in obesity and dyslipedemia and may affect the plasma retinol status, overview
physiological function
Rattus norvegicus Zucker
-
increased intestinal enzyme expression occurs in obesity and dyslipedemia and may affect the plasma retinol status, overview
-
metabolism
-
Bcmo1 and retinal dehydrogenase 1 are key enzymes in the retinoid metabolism of inguinal white adipose tissue
additional information
-
transcriptional regulation, overview
additional information
-
beta-carotene represses Ppar gamma and CCAAT/enhancer-binding protein alpha expression in mature adipocytes
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
13-cis-beta-carotene + O2
retinal
show the reaction diagram
-
11.4% of the activity with all-trans-beta-carotene
-
-
?
alpha-carotene + ?
11-cis-retinal + all-trans-retinal + all-trans-alpha-retinal
show the reaction diagram
-
-
32.7% 11-cis-retinal + 17.3% all-trans-retinal + 50.0% all-trans-alpha-retinal
-
?
alpha-carotene + O2
retinal
show the reaction diagram
-
8.2% of the activity with all-trans-beta-carotene
-
-
?
alpha-carotene + O2
retinal + ?
show the reaction diagram
-
one molecule retinal is formed
-
-
?
alpha-carotene + O2
retinal + alpha-retinal
show the reaction diagram
-
one molecule retinal is formed
-
-
?
beta-apo-4'-carotenal + O2
retinal + ?
show the reaction diagram
-
one molecule retinal is formed
-
-
?
beta-apo-8'-carotenal + O2
retinal + ?
show the reaction diagram
-
one molecule retinal is formed
-
-
?
beta-carotene + ?
11-cis-retinal + all-trans-retinal
show the reaction diagram
-
-
41.2% 11-cis-retinal + 58.8% all-trans-retinal
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
Q9JJS6
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-, Q90WH4
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
conversion of the plant product beta-carotene into a product necessary for the growth and life of the animal organism
-
?
beta-carotene + O2
retinal
show the reaction diagram
Q9JJS6
crucial enzyme in development and metabolism that governs the de novo entry of vitamin A from plant-derived precursors, enzyme may play a critical role in gastrulation
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-, Q9HAY6
the enzyme catalyzes the first step in the synthesis of vitamin A from dietary carotenoids. May also play a role in peripheral vitamin A synthesis from plasma-borne provitamin A carotenoids
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
the enzyme is responsible for providing vertebrates with vitamin A by catalyzing oxidative cleavage of beta-carotene at its central double bond to two molecules of retinal in intestinal cells
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
Q9JJS6
enzyme may play a critical role in gastrulation
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
Q9I993
key enzyme in the metabolism of beta,beta-carotene to vitamin A
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
enzyme plays an important role in retinoid synthesis. BCDO may also be a candidate gene for retinal degenerative disease
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
key enzyme in metabolism of provitamin A carotenoids to retinal
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
the enzyme catalyzes the first step in conversion of dietary provitamin A carotenoids to vitamin A. The finding that the enzyme is expressed in all epithelia examined leads to the suggestion that BCO1 may be important for local synthesis of vitamin A, constituting a back-up pathway of vitamin A synthesis during times of insufficient dietary intake of vitamin A
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
the enzyme catalyzes the first step of vitamin A biosynthesis from provitamin A carotenoids
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-, Q90WH4
the enzyme is essential for pattern formation and differentation during zebrafish embryogenesis
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
two molecules retinal are formed
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
two molecules retinal are formed
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
Q9JJS6
-
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
BCMO1 is a key enzyme in the pathway of retinoid synthesis from carotenoids, and is responsible for metabolically limiting the amount of intact beta-carotene that can be absorbed by mice from their diet, regulation of BCMO1 activity, overview
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
BCMO1 is a key enzyme in the pathway of retinoid synthesis from carotenoids, regulation of BCMO1 activity, overview
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
beta-carotene is stored in the fat
-
-
?
beta-carotene + O2
11-cis-retinal + 13-cis-retinal + all-trans-retinal
show the reaction diagram
Q9VFS2
-
-
-
?
beta-carotene + O2
13-cis-retinal + all-trans-retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-, substrate binding structure, overview
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
tyrosine Y235 and Y326 in mouse BCMO1 fix the position of the substrate on the two sides of the 15,15'-double bond most likely due to a mechanism implicating cation pi-stabilization
-
-
?
beta-criptoxanthin + O2
retinal + ?
show the reaction diagram
-
one molecule retinal is formed
-
-
?
beta-cryptoxanthin + O2
retinal + (3R)-3-hydroxy-retinal
show the reaction diagram
-
-
-
-
?
beta-cryptoxanthine + O2
?
show the reaction diagram
-
-
-
-
?
cryptoxanthin + O2
11-cis-retinal + all-trans-retinal + 11-cis-3-hydroxy-retinal + all-trans-3-hydroxy-retinal
show the reaction diagram
-
-
4.2% 11-cis-retinal + 45.8% all-trans-retinal + 35.1% 11-cis-3-hydroxy-retinal + 14.9% all-trans-3-hydroxy-retinal
-
?
gamma-carotene + O2
retinal + acycloretinal
show the reaction diagram
-
-
one molecule retinal is formed
-
?
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
show the reaction diagram
-
-
-
-
?
zeaxanthin + O2
(3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
show the reaction diagram
-
-
41.5% 11-cis-3-hydroxy-retinal + 58.5% all-trans-3-hydroxy-retinal
-
?
lutein + O2
11-cis-3-hydroxy-retinal + all-trans-3-hydroxy-retinal + all-trans-3-hydroxy-alpha-retinal
show the reaction diagram
-
-
39.9% 11-cis-3-hydroxy-retinal + 10.1% all-trans-3-hydroxy-retinal + 47.7% all-trans-3-hydroxy-alpha-retinal
-
?
additional information
?
-
-
catalyses the first step in the conversion of dietary provitamin A carotenoids to vitamin A in the small intestine
-
-
-
additional information
?
-
-
beta-carotene but not all-trans-retinol is converted to all-trans-retinoic acid in mature adipocytes
-
-
-
additional information
?
-
-
BCMO is also active with alpha-carotene, beta-apo-8'-carotenal, and beta-apo-4'-carotenal. The hydrophobicity of residue 108 specifically affects the affinity of beta-carotene 15,15'-monooxygenase for substrates with two ionone rings. Residue 108 may be related to the indirect interaction with the second ionone ring of the substrates with two ionone rings, comparison with apo-carotenoid 15,15'-oxygenase, EC 1.14.99.41, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
conversion of the plant product beta-carotene into a product necessary for the growth and life of the animal organism
-
?
beta-carotene + O2
retinal
show the reaction diagram
Q9JJS6
crucial enzyme in development and metabolism that governs the de novo entry of vitamin A from plant-derived precursors, enzyme may play a critical role in gastrulation
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-, Q9HAY6
the enzyme catalyzes the first step in the synthesis of vitamin A from dietary carotenoids. May also play a role in peripheral vitamin A synthesis from plasma-borne provitamin A carotenoids
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
the enzyme is responsible for providing vertebrates with vitamin A by catalyzing oxidative cleavage of beta-carotene at its central double bond to two molecules of retinal in intestinal cells
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
Q9JJS6
enzyme may play a critical role in gastrulation
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
Q9I993
key enzyme in the metabolism of beta,beta-carotene to vitamin A
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
enzyme plays an important role in retinoid synthesis. BCDO may also be a candidate gene for retinal degenerative disease
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
key enzyme in metabolism of provitamin A carotenoids to retinal
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
the enzyme catalyzes the first step in conversion of dietary provitamin A carotenoids to vitamin A. The finding that the enzyme is expressed in all epithelia examined leads to the suggestion that BCO1 may be important for local synthesis of vitamin A, constituting a back-up pathway of vitamin A synthesis during times of insufficient dietary intake of vitamin A
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
the enzyme catalyzes the first step of vitamin A biosynthesis from provitamin A carotenoids
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-, Q90WH4
the enzyme is essential for pattern formation and differentation during zebrafish embryogenesis
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
two molecules retinal are formed
-
-
?
beta-carotene + O2
retinal
show the reaction diagram
-
two molecules retinal are formed
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
BCMO1 is a key enzyme in the pathway of retinoid synthesis from carotenoids, and is responsible for metabolically limiting the amount of intact beta-carotene that can be absorbed by mice from their diet, regulation of BCMO1 activity, overview
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
BCMO1 is a key enzyme in the pathway of retinoid synthesis from carotenoids, regulation of BCMO1 activity, overview
-
-
?
beta-carotene + O2
all-trans-retinal
show the reaction diagram
-
beta-carotene is stored in the fat
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-
-
-
?
beta-carotene + O2
2 retinal
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
beta-carotene but not all-trans-retinol is converted to all-trans-retinoic acid in mature adipocytes
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
activates; maximal activation, 5.8fold, at 1 mM
Fe2+
-
activates
Iron
-
the iron-dependent enzyme is sensitive to copper status in vivo
Iron
Q9JJS6
required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,1'-biphenyl
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
13-cis-retinal
-
-
15,15'-Dehydro-beta-apo-10'-carotenol
-
inhibits reaction with beta-apo-10'-carotenol
2,2'-dipyridyl
-
-
2,2'-dipyridyl
-
-
2,2'-dipyridyl
-
slight inhibition
2,6-di-tert-butyl-4-methylphenol
-
0.001 mM, strong mixed-type inhibition
3,5-di-tert-butyltoluene
-
-
8-hydroxyquinoline
-
-
9-cis retinoic acid
-
suppresses the upregulation by vitamin A deficiency
9-cis-retinal
-
-
all-trans retinal
-
-
all-trans retinoic acid
-
suppresses the upregulation by vitamin A deficiency
apo-8'-carotenal
-
-
-
astaxanthin
-
competitive
beta-carotene
-
-
butylated hydroxyanisole
-
moderate inhibition
canthaxanthin
-
mixed inhibition
curcumin
-
moderate inhibition
Desferrioxamine
-
noncompetitive inhibitor
Diphenylamine
-
non-competitive inhibition
EDTA
-
0.02 mM, very slight inhibition
EDTA
-
slight inhibition
Fe2+
-
4 mM, 60% inhibition
-
fenretinide
-
selectively inhibits the anti-adipogenic effects of beta,beta-carotene via inhibition of BCMO
iodoacetate
-
-
lutein
-
competitive
luteolin
-
remarkable noncompetitive inhibition
n-propyl gallate
-
moderate inhibition
Na-arsenite
-
-
-
nordihydroguaiaretic acid
-
moderate inhibition
o-Iodosobenzoate
-
-
p-hydroxymercuribenzoate
-
-
PCMB
-
reversed by glutathione
phenanthrene
-
-
phloretin
-
remarkable noncompetitive inhibition
quercetin
-
remarkable noncompetitive inhibition
retinyl acetate
-
-
Rhamnetin
-
remarkable noncompetitive inhibition
SDS
-
required for maximal activity
Sodium glycocholate
-
-
zeaxanthin
-
non-competitive
Lycopene
-
competitive
additional information
-
catechol structure of the ring B and a planar flavone structure are essential for inhibition
-
additional information
-
no inhibition by cyanide
-
additional information
-
influence of different types of fats on intestinal and hepatic BCMO1 activity, overview
-
additional information
-
no inhibition by EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-S-octyl-beta-D-thioglucopyranoside
-
detergent required, maximal activity at 1% w/v
apo-12'-carotenal
-
-
-
glycocholate
-
plus lecithin, stimulates
GSH
-
activates
GSH
-
stimulates
GSH
-
thiol-dependent enzyme
hexadecyl trimethyl ammonium bromide
-
stimulates
lecithin
-
plus glycocholate, stimulates
lecithin
-
egg or plant lecithin stimulates
linoleic acid
-
stimulates
lysolecithin
-
lysolecithin, stimulates
octyl beta-glucoside
-
detergent required
oleyl acid phosphate
-
stimulates
palmitic acid
-
stimulates
SDS
-
2-6 mg, stimulates
SDS
-
stimulates
SDS
-
detergent required, low activation
Sodium cholate
-
detergent required
sodium dodecyl phosphate
-
stimulates
Sodium glycocholate
-
optimum concentration is 6 mM
sphingomyelin
-
stimulates
Triton X-100
-
detergent required
Tween 20
-
stimulates
Tween 40
-
stimulates
Tween 80
-
stimulates
type I cellular retinol-binding protein
-
i.e. RBP1, RBP1, but not RBP2, is required for the transport of water-insoluble substrates of retinoid pathway enzymes, e.g. of BCMO1, into the cell, and acts as an intracellular sensor of retinoid status that, when present as apo-RBP1, stimulates BCMO1 activity and the conversion of carotenoids to retinoids
-
Monoolein
-
significant stimulation
additional information
-
the enzyme is completely inactive in absence of any added bile salt or detergent
-
additional information
-
maximal reaction by addition of an appropriate combination of detergent and bile salt, SDS, and egg lecithin
-
additional information
-
influence of different types of fats on intestinal and hepatic BCMO1 activity, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0092
-
10'-apo-beta-carotenal
-
-
0.0035
-
13-cis-beta-carotene
-
-
0.0077
-
8'-apo-beta-carotenal
-
-
0.0085
-
8'-apo-beta-carotenal
-
-
0.0057
-
all-trans-beta-carotene
-
-
0.0062
-
alpha-carotene
-
-
0.02213
-
alpha-carotene
-
-
0.37
-
alpha-carotene
-
-
0.0095
-
beta,beta-carotene
-
-
0.067
-
beta-apo-10'-carotenol
-
-
-
0.18
-
beta-apo-4'carotenal
-
-
0.19
-
beta-apo-8'carotenal
-
-
0.00052
0.0059
beta-carotene
-
pH 7.7, 37C
0.0009
-
beta-carotene
Q9JJS6
mutant E140A, pH 8.0, 37C
0.0012
-
beta-carotene
Q9JJS6
wild-type, pH 8.0, 37C
0.0013
0.0056
beta-carotene
-
pH 7.8-8.2, 37C
0.0016
-
beta-carotene
-
-
0.0023
-
beta-carotene
Q9JJS6
mutant E450A, pH 8.0, 37C
0.0027
-
beta-carotene
Q9JJS6
mutant H58A, pH 8.0, 37C
0.0033
-
beta-carotene
-
intestinal enzyme
0.0033
-
beta-carotene
-
-
0.0033
-
beta-carotene
Q9JJS6
mutant E314A, pH 8.0, 37C
0.0047
-
beta-carotene
Q9JJS6
mutant D52A, pH 8.0, 37C
0.006
0.031
beta-carotene
-
pH 7.5-8.0, 37C, recombinant enzyme
0.006
-
beta-carotene
-
pH 7.5-8.0, 37C, recombinant enzyme
0.0071
-
beta-carotene
-
-
0.0104
-
beta-carotene
-
-
0.0123
-
beta-carotene
-
mutant R267S
0.0179
-
beta-carotene
-
mutant R267S
0.0183
-
beta-carotene
-
wild-type
0.0195
-
beta-carotene
-
R267S/R267S double mutant
0.026
-
beta-carotene
-
-
0.026
-
beta-carotene
-
pH 7.5-8.0, 37C, recombinant enzyme
0.028
-
beta-carotene
-
T381L mutant
0.03
-
beta-carotene
-
pH 8.0, 37C, recombinant wild-type enzyme
0.031
-
beta-carotene
-
wild-type
0.088
-
beta-carotene
-
pH 8.0, 37C, recombinant mutant K108L
0.215
-
beta-carotene
-
pH 8.0, 37C, recombinant mutant K108F
0.0067
-
beta-cryptoxanthin
-
-
0.03
-
beta-cryptoxanthin
-
-
0.29
-
beta-cryptoxanthin
-
-
0.69
-
gamma-Carotene
-
-
additional information
-
additional information
-
Michaelis-Menten kinetics of wild-type enzyme and mutants K108L and K108F with beta-carotene and beta-apo-8'-carotenal, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00817
-
alpha-carotene
-
-
0.0083
-
alpha-carotene
-
-
0.015
-
beta-apo-4'-carotenal
-
-
0.0183
-
beta-apo-8'-carotenal
-
-
0.0001
-
beta-carotene
-
-
0.00867
-
beta-carotene
-
-
0.011
-
beta-carotene
-
-
0.0275
-
beta-carotene
-
-
0.0395
-
beta-carotene
-
pH 8.0, 37C, recombinant mutant K108L
0.04
-
beta-carotene
-
pH 8.0, 37C, recombinant mutant K108F
0.046
-
beta-carotene
-
pH 8.0, 37C, recombinant wild-type enzyme
0.0333
-
beta-cryptoxanthin
-
-
0.668
-
beta-cryptoxanthin
-
-
0.0082
-
gamma-Carotene
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.17
-
beta-carotene
-
pH 8.0, 37C, recombinant mutant K108F
7863
0.45
-
beta-carotene
-
pH 8.0, 37C, recombinant mutant K108L
7863
1.52
-
beta-carotene
-
pH 8.0, 37C, recombinant wild-type enzyme
7863
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00079
-
2,6-di-tert-butyl-4-methylcatechol
-
-
-
0.1187
-
3,5-di-tert-butyltoluene
-
-
0.0474
-
butylated hydroxyanisole
-
-
0.0016
-
canthaxanthin
-
-
0.0169
-
curcumin
-
-
0.0133
-
luteolin
-
-
0.0099
-
phloretin
-
-
0.0058
-
Rhamnetin
-
-
0.0078
-
zeaxanthin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.6e-05
-
-
-
0.001
-
-
R267S/A379V double mutant
0.0023
-
-
wild-type
0.01
-
-
crude extract
0.16
-
-
purification step His-Trap HP
0.32
-
-
purification step Resource Q
0.51
-
-
pH 9.0, 36C
1.97
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
activity assay
7.6
-
-
activity assay
7.7
-
-
assay at
7.8
8.2
-
-
7.8
-
-
reaction with beta-apo-10'-carotenol
8
-
-
activity assay
8
-
-
activity assay
8
-
-
activity assay
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8.5
-
pH 7.0: about 60% of maximal activity, pH 8.5: about 75% of maximal activity
7
9
-
pH 7.0: about 50% of maximal activity, pH 9.0: about 35% of maximal activity, reaction with beta-apo-10'-carotenol
8.5
-
-
70% of maximum activity
10
-
-
70% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28
-
-
activity assay
28
-
-
activity assay
37
-
-
assay at
37
-
-
assay at
37
-
-
activity assay
37
-
-
activity assay
37
-
-
activity assay
37
-
-
-
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
22% of maximum activity
45
-
-
14% of maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
a preadipocyte cell line
Manually annotated by BRENDA team
-
human kidney cell line
Manually annotated by BRENDA team
C1L3B1, C7C6F6, -
;
Manually annotated by BRENDA team
Rattus norvegicus Zucker
-
-
-
Manually annotated by BRENDA team
-
steroidogenic cells
Manually annotated by BRENDA team
-
lower levels
Manually annotated by BRENDA team
-
intestinal cell line Caco-2/subclone TC7; when TC7 cells are maintained in serum-free medium, activity is increased 8.2fold after 19 days of postconfluence
Manually annotated by BRENDA team
-
intestinal cell line Caco-2/subclone TC7
Manually annotated by BRENDA team
-
for cloning of full-length BCMO1, RNA is isolated from Caco-2/TC7 cells
Manually annotated by BRENDA team
-
glandular cell
Manually annotated by BRENDA team
-
lower levels
Manually annotated by BRENDA team
-
in epithelial cells of the mucosa, quantitative RT-PCR expression analysis, and in situ hybridization
Manually annotated by BRENDA team
-
mRNA is abundant at embryonic day 7, with lower expression at embryonic days 11, 13 and 15
Manually annotated by BRENDA team
-
of several tissues including stomach, intestine, colon, prostate glands, and endometrium
Manually annotated by BRENDA team
-
expression is eye-dependent
Manually annotated by BRENDA team
Clarias batrachus, Domania subtryug
-
mucosa
Manually annotated by BRENDA team
-
mucosa; pylorus to the lower ileum
Manually annotated by BRENDA team
-
activity is 20-30% greater in vitamin-A deficient animals than in the controls
Manually annotated by BRENDA team
-
high levels of BCO mRNA, highest level in jejunum
Manually annotated by BRENDA team
-
highest expression in duodenum, mRNA level in ileum is markedly low
Manually annotated by BRENDA team
-
activity detected in two subclones of Caco-2, PF11 and TC7. When TC7 cells are maintained in serum-free medium, activity is increased 8.2fold after 19 days of postconfluence. No activity detected in IPEC-1, HepG2, HL60, Wurzburg, or parent Caco-2, PF11 and TC7
Manually annotated by BRENDA team
-
high expression, expression in small intestine is increased by vitamin A deficiency. Upregulation is suppressed by all-trans retinoic acid or 9-cis retinoic acid
Manually annotated by BRENDA team
-
activity of enzyme in intestinal mucosa is higher after feeding with oleic acid or eicosapentanoic acid than with linoleic acid
Manually annotated by BRENDA team
Rattus norvegicus Zucker
-
-
-
Manually annotated by BRENDA team
-
of the squamous epithelium of skin
Manually annotated by BRENDA team
-
high levels of BCO mRNA
Manually annotated by BRENDA team
-
only marginal activity
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
elevated levels of mRNA
Manually annotated by BRENDA team
-
high level, in distal and proximal tubular structures
Manually annotated by BRENDA team
-
high level, in distal and proximal tubular structures
Manually annotated by BRENDA team
-
high levels of BCO mRNA
Manually annotated by BRENDA team
-
expression is increased by feeding animals with a PPARalpha/gamma agonist
Manually annotated by BRENDA team
-
parenchymal cell
Manually annotated by BRENDA team
-
high expression, expression is suppressed by all-trans retinoic acid
Manually annotated by BRENDA team
-
diffuse distribution in the lobules, quantitative RT-PCR expression analysis and in situ hybridization
Manually annotated by BRENDA team
-
elevated levels of mRNA
Manually annotated by BRENDA team
-
high level
Manually annotated by BRENDA team
-
high expression, expression is increased by vitamin A deficiency. Upregulation is suppressed by all-trans retinoic acid or 9-cis retinoic acid
Manually annotated by BRENDA team
-
elevated levels of mRNA
Manually annotated by BRENDA team
-
of stomach
Manually annotated by BRENDA team
-
predominantly expressed in ocellus photoreceptor cells of the larva
Manually annotated by BRENDA team
-
low levels of BCO mRNA
Manually annotated by BRENDA team
-
steroidogenic cells
Manually annotated by BRENDA team
-
lower levels
Manually annotated by BRENDA team
-
cell that make up exocrine glands
Manually annotated by BRENDA team
-
glandular cell
Manually annotated by BRENDA team
-
low levels of BCO mRNA
Manually annotated by BRENDA team
-
enzyme is highly expressed in retinal pigment epithelium
Manually annotated by BRENDA team
-
low levels of BCO mRNA
Manually annotated by BRENDA team
-
keratinocytes of the squamous epithelium
Manually annotated by BRENDA team
-
mucosa, glandular cells
Manually annotated by BRENDA team
-
low levels of BCO mRNA
Manually annotated by BRENDA team
-
steroidogenic cells
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
Leydig and Sertoli cells
Manually annotated by BRENDA team
-
Leydig and Sertoli cells
Manually annotated by BRENDA team
additional information
-
no expression in lung
Manually annotated by BRENDA team
additional information
-
no activity is detected in adult stomach tissue
Manually annotated by BRENDA team
additional information
-
enzyme activity is similar in the duodenum, but pigmented animals have higher enzyme activity in the liver, eevnthough not high enough to prevent the storage of beta-carotene in adipose tissues
Manually annotated by BRENDA team
additional information
-
BCMO1 expression in the exocrine portion of the pancreas, epidermis of the skin, and ciliary body pigment epithelia and RPE of the eye
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
gel filtration
57800
-
-
theoretical
60000
-
-
determined by SDS-PAGE
61210
-
-
theoretical, plus hexahistidine tag
62000
-
-
theoretical
62000
-
-
determined by SDS-PAGE and Western Blot analysis
63000
-
-
determined by SDS-PAGE
63400
-
-
theoretical, His-tagged protein
63400
-
-
theoretical
64000
-
-
determined by SDS-PAGE and Western Blot analysis
65000
-
-
determined by SDS-PAGE
230000
-
-
gel filtration
240000
-
-
determined by gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 63859, calculation from nucleotide sequence
?
-
x * 64000, SDS-PAGE
?
-
x * 63000, SDS-PAGE
?
-
x * 64686, calculated, x * 65000, SDS-PAGE
?
-
x * 240000, recombinant enzyme
?
-
x * 64000, recombinant enzyme
?
-
x * 63000, recombinant enzyme
?
-
x * 100000-200000
?
-
x * 100000-20000
tetramer
-
-
homotetramer
-
4 * 60000
additional information
-
BCMO three-dimensional structure, with entrance of active tunnel and the hydrophobic patch, including Pro101, Cys102, Ile105, Phe106, Lys108, Leu258, Thr262, and Tyr264, modelling, overview
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52
-
-
3 min, no effect
64
-
-
55 seconds, complete inactivation of intestinal enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
loss of activity during concentration by ultrafiltration or (NH4)2SO4 precipitation as well as during dialysis
-
carotenoids stabilize the enzyme during the isolation from small intestinal mucosa
-
liver enzyme may be frozen and thawed repeatedly without loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, as (NH4)2SO4 precipitate, 25-55%, for one month without considerable loss in activity
-
-20C, 40% glycerol and presence of protease inhibitors, enzyme purified by metal affinity chromatography is stable for several weeks
Q9JJS6
-20C, as (NH4)2SO4 precipitate, 25-55%, for one month without considerable loss in activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by affinity chromatography
-
by His-Trap HP affinity and Resource Q ion exchange chromatography
-
affinity purified via the His-tag
-
recombinant enzyme from Escherichia coli by affinity and anion exchange chromatography
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
using a His-Trap HP affinity chromatography column
-
using a HiTrap Chelating HP column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
tissue-specific quantitative RT-PCR expression analysis
-
-
-, Q90WH4
for expression in Escherichia coli cells, genetically engineered to produce beta-carotene
Q9VFS2
into the vectors pCRII TOPO and pBAD-TOPO for expression in Escherichia coli XL1-blue cells
-
expression in Escherichia coli and in CHO cells
-
into the vector pET-24a+ for expression in Escherichia coli ER2566 cells
-
baculovurus expressed
-
BCMO gene, DNA and mino acid sequence determination and analysis, expression in Escherichia coli strain ER2566
-
EST library screening, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
-
expression by an baculovirus/Spodoptera frugiperda 9 insect cell system
-
identification of ligand binding sites on the bcmo1 promoter, transcriptional regulation, overview
-
into a Flag fusion-modified mammalian expression vector pcDNA3 and into the bacterial vectors pET-15b and pGEX-4T2
-
into the pCR Blunt vector and subsequently into the pTrcHis vector for sequencing and expression in Escherichia coli cells
-
into the vector pET-24b+ for expression in Escherichia coli ER2566 cells
-
expression in Escherichia coli
-
for expression in Escherichia coli cells, genetically engineered to produce beta-carotene
-
gene bcmo1, quantitative real time PCR expression analysis. The murine Bcmo1 promoter contains a DR1-type peroxisome proliferator-response element that binds Ppargamma/Rxr heterodimers. Recombinant expression of Bcmo1 in Escherichia coli
-
the proximal promoter of the mouse Bcm gene contains a PPRE site that specifically binds PPARgamma and regulates transcriptional expression of Bcm. This element is functional in vitro and confers peroxisome proliferator responsiveness, using specific PPARgamma and RXR agonists
-
gene bcmo1, DNA and amino acid sequence determination and analysis; gene bco2, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, genotyping, overview
C1L3B1, C7C6F6, -
from intestinal cDNA library
-
gene BCM, quantitative expression analysis, overview
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
all-trans-retinal does not affect liver bcmo1 expression
-
all-trans-retinal at 0.001 mM suppresses bcmo1 expression
-
beta-carotene and all-trans-retinal at 10-100 nM induces bcmo1 expression
-
Isx, intestine specific homeobox, participates in the maintenance of vitamin A by regulating Bcmo1 expression in the intestine
-
Bcmo1 expression is induced during adipocyte differentiation
-
BCM gene expression in the liver and intestines of puromycin aminonucleoside-treated rats is decreased
-
all-trans-retinal suppresses liver, lung and testis bcmo1 expression, and 9-cis-retinal in lung and testis, in vitamin A-deficient rats
-
BCM gene expression in the kidney of puromycin aminonucleoside-treated rats is increased
-
intestinal BCM gene expresssion is increased in obese and dyslipedemic rats
-
intestinal BCM gene expresssion is increased in obese and dyslipedemic rats
Rattus norvegicus Zucker
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A379V
-
single nucleotide polymorphism, allele frequency 24%, recombinant mutant
A379V
-
naturally occuring polymorphism, the mutation causes 33% reduced BCMO1 activity compared to wild-type in vitro and 32% reduced conversion of beta-carotene after a pharmacological dose in female volunteers
K108F
-
site-directed mutagenesis, the mutant shows highly decreased affinity for substrates with ionone rings at both ends, such as alpha-carotene, beta-carotene, and beta-cryptoxanthin, and a 7.2fold increased Km for beta-carotene compared to the wild-type enzyme. But the mutation has little effect on the affinity of the enzyme for substrates with one ionone ring and one open-chain end, such as beta-apo-4'-carotenal and beta-apo-8'-carotenal
K108L
-
site-directed mutagenesis, the mutant shows highly decreased affinity for substrates with ionone rings at both ends, such as alpha-carotene, beta-carotene, and beta-cryptoxanthin, and a 2.9fold increased Km for beta-carotene compared to the wild-type enzyme. But the mutation has little effect on the affinity of the enzyme for substrates with one ionone ring and one open-chain end, such as beta-apo-4'-carotenal and beta-apo-8'-carotenal
N329T
-
naturally occuring polymorphism
R228C
-
naturally occuring polymorphism
R267S
-
single nucleotide polymorphism, allele frequency 42%, recombinant mutant
R267S
-
naturally occuring polymorphism, the mutation does not show any effect on BCMO1 activity in vitro and in vivo
R267S/A379V
-
recombinant double mutant, reveals a reduced catalytic activity by 57%
R267S/A379V
-
naturally occuring polymorphism, the mutation causes 57% reduced BCMO1 activity compared to wild-type in vitro and 69% reduced conversion of beta-carotene after a pharmacological dose in female volunteers
R537K
-
naturally occuring polymorphism
T170M
-
naturally occuring polymorphism, the mutant shows 90% reduced BCMO1 activity compared to wild-type in vitro causing hypercarotenemia and hypovitaminose A
T381L
-
mutant, shows 1.5fold higher catalytic efficiency for beta-carotene and 1.7fold higher retinal production than the wild-type
T381L
-
naturally occuring polymorphism, the mutant shows 75% increased BCMO1 activity compared to wild-type in vitro
T382P
-
naturally occuring polymorphism
Y236S
-
naturally occuring polymorphism
D52A
Q9JJS6
more than 50% loss of activity
D52A/E140A
Q9JJS6
no enzymatic activity
E140A
Q9JJS6
more than 50% loss of activity
E314A
Q9JJS6
little reduction in enzymatic activity
E405A
Q9JJS6
no enzymatic activity
E450A
Q9JJS6
little reduction in enzymatic activity
E457A
Q9JJS6
about 80% loss of activity
E469A
Q9JJS6
about 50% decrease in activity, cells are bleached when left growing overnight
H172A
Q9JJS6
no enzymatic activity
H174A
Q9JJS6
little reduction in enzymatic activity
H237A
Q9JJS6
no enzymatic activity
H308A
Q9JJS6
no enzymatic activity
H309A
Q9JJS6
little reduction in enzymatic activity
H49A
Q9JJS6
little reduction in enzymatic activity
H514A
Q9JJS6
no enzymatic activity
additional information
-
targeted knockdown of enzyme results in microphthalmia at larval stages. Photoreceptors in the central retina show shortened outer segments, and electron dense debris in their intermembranal space. The number of phagosomes is increased and cell death is frequently observed in the outer nuclear layer. The number of Mller cells is significantly reduced in the inner nuclear layer
H58A
Q9JJS6
little reduction in enzymatic activity
additional information
-
phenotype of enzyme-deficient mice, beta-carotene conversion is blocked in BCMO1-deficient mice, comparison of plasma retinol and liver retinyl esters of wild-type, heterozygous and homozygous BCMO1-deficient mice, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
reconstitution of recombinant Bcmo1 from Escherichia coli in micelles formed by n-octyl-beta-D-thioglucopyranoside
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
BCMO function in mammalian cells is analyzed by a retinoic acid receptor assay, which responds to the metabolic conversion of beta-carotene to retinoic acid in vivo, this tool can be used to screen more active BCMO for the industrial and pharmacological purpose of retinal production from beta-carotene
synthesis
-
production of retinal from beta-carotene using recombinant enzyme. The optimum pH, temperature, substrate and detergent concentrations, and enzyme amount for effective retinal production are 9.0, 37C, 200 mg per ml beta-carotene, 5% w/v Tween 40, and 0.2 U per ml enzyme, respectively. Under optimum conditions, the recombinant enzyme produces 72 mg per ml retinal in a 15 h reaction time, with a conversion yield of 36% w/w
diagnostics
C1L3B1, C7C6F6, -
genotyping AI rams for c.196C-T can be used in selection against the yellow fat trait
medicine
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Modulation of intestinal beta-carotene uptake and its conversion to vitamin A using specific fatty acids. Improved absorption and metabolism of beta-carotene by feeding mixed micelles with oleic acid or eicosapentanoic acid compared with linoleic acid
medicine
-
changes in the metabolism of retinol and beta-carotene might have an important role in the protection against the development of nephrosis
medicine
-
BCM gene expression in the liver and intestine might affect retinol levels in type 2 diabetes