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Information on EC 1.1.99.1 - choline dehydrogenase
for references in articles please use BRENDA:EC1.1.99.1
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.99 With unknown physiological acceptors
1.1.99.1 choline dehydrogenase
IUBMB Comments
A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) . The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
choline dehydrogenase, chdh, chodh, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CHD
CHDH
ChoDH
choline dehydrogenase
choline oxidase
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-
-
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choline-cytochrome c reductase
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-
-
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choline:(acceptor) oxidoreductase
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-
-
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dehydrogenase, choline
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-
-
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oxidase, choline
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-
-
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CHD
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
choline + acceptor = betaine aldehyde + reduced acceptor
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-
-
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choline + acceptor = betaine aldehyde + reduced acceptor
pingpong BiBi steady state kinetic mechanism of partially purified rat CHD
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
choline degradation I, glycine betaine biosynthesis I (Gram-negative bacteria)
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SYSTEMATIC NAME
IUBMB Comments
choline:acceptor 1-oxidoreductase
A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [4]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria.
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CAS REGISTRY NUMBER
COMMENTARY
9028-67-5
identical with CAS Reg. No. of EC 1.1.3.17
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + phenazine methosulfate
glycine-betaine + ?
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Substrates: -
Products: -
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?
choline + 2,6-dichlorophenolindophenol
betaine aldehyde + reduced 2,6-dichlorophenolindophenol
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Substrates: -
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r
choline + acceptor + phenazine methosulfate
betaine aldehyde + ?
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Substrates: -
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?
choline + coenzyme Q1
betaine aldehyde + reduced coenzyme Q1
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Substrates: mitochondrial oxidation of choline
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?
choline + p-benzoquinone
betaine aldehyde + reduced p-benzoquinone
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Substrates: -
Products: -
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r
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
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Substrates: four electron oxidation with betaine aldehyde as intermediate, provides glycine-betaine as compatible solute
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?
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
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Substrates: four electron oxidation with betaine aldehyde as intermediate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: 2,6-dichlorophenolindophenol
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: choline is the sole substrate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: relation of plasma choline and betaine to cardiovascular risk factors, mitochondrial choline dehydrogenase pathway
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
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r
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: effects of food-deprivation on betaine accumulation and the levels of betaine synthesizing enzymes
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?
choline + acceptor
betaine aldehyde + reduced acceptor
-
Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
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r
choline + acceptor
betaine aldehyde + reduced acceptor
-
Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor 3-(4,5-dimethylthiazolyl-2-)-2,5-diphenyltetrazolium bromide, particulate enzyme: 12.4% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: cytochrome c, particulate enzyme: 3.1% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: 2,6-dichlorophenolindophenol
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor ferricyanide, particulate enzyme: 112% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor 2,6-dichlorophenolindophenol, particulate enzyme: 3.2% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor: phenazine methosulfate, 100% relative activity
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor 3-(4,5-dimethylthiazolyl-2-)-2,5-diphenyltetrazolium bromide, particulate enzyme: 12.4% relative activity to phenazine methosulfate
Products: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: cytochrome c, particulate enzyme: 3.1% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor ferricyanide, particulate enzyme: 112% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor 2,6-dichlorophenolindophenol, particulate enzyme: 3.2% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor: phenazine methosulfate, 100% relative activity
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?
choline + acceptor
betaine aldehyde + reduced acceptor
-
Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor: ubiquinone-2
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: the enzyme can use only choline and betaine aldehyde
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r
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor O2: 73% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: 2,6-dichlorophenolindophenol
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor 2,6-dichlorophenolindophenol: 27% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: absolute requirement for an electron acceptor other than O2
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r
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: reverse reaction at 5.2% of forward reaction
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r
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: cytochrome c, ferricyanide, methylene blue and 2,6-dichlorophenolindophenol show no direct reaction with the enzyme
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor methylene blue: 4% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: coenzyme Q, primary electron acceptor in vivo
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r
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor cytochrome c: 63% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: acceptor: phenazine methosulfate, 100% relative activity
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: phenazine methosulfate
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r
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: not: 2-dimethylaminoethanol, monoethanolamine
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r
choline + acceptor
betaine aldehyde + reduced acceptor
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Substrates: electron acceptor: p-benzoquinone
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?
choline + acceptor
betaine aldehyde + reduced acceptor
-
Substrates: acceptor ferricyanide: 42% relative activity to phenazine methosulfate
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: connects choline to the respiratory chain
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
-
Substrates: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
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r
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
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?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
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?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
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?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
-
Substrates: -
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r
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
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r
additional information
?
-
-
Substrates: the enzyme is responsible for the two-step choline oxidation to betaine together with the betaine-homocysteine methyltransferase
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?
additional information
?
-
Substrates: the enzyme is specific for choline or betaine aldehyde as substrate, substrate specificity, overview
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
-
Substrates: four electron oxidation with betaine aldehyde as intermediate, provides glycine-betaine as compatible solute
Products: -
Products: -
?
choline + coenzyme Q1
betaine aldehyde + reduced coenzyme Q1
-
Substrates: mitochondrial oxidation of choline
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for the two-step choline oxidation to betaine together with the betaine-homocysteine methyltransferase
Products: -
Products: -
?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
Products: -
Products: -
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
Substrates: -
Products: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
Products: -
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r
choline + acceptor
betaine aldehyde + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
Products: -
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r
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: connects choline to the respiratory chain
Products: -
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?
choline + acceptor
betaine aldehyde + reduced acceptor
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme requires no readily dissociable coenzyme for activity
-
additional information
-
the enzyme requires no readily dissociable coenzyme for activity
-
additional information
-
FAD and pyrroloquinoline quinone has no effect on activity
-
additional information
oxygen is not the preferred electron acceptor even though the enzyme is able to utilize it. Phenazine methosulfate can act as artificial cofactor. Cytochrome c and ferricyanide give poor activity
-
additional information
the enzyme has 3 functional domains, named FAD/NAD(P)-binding domain 1 (FB1, residues 39 to 326), FAD-linked reductase domain (RD, residues 333 to 515) and FAD/NAD(P)-binding domain 2 (FB2, residues 511 to 574)
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme expression is not affected by methionine or choline intake in liver, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme expression is not affected by methionine or choline intake in liver, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles.
Amyotrophic Lateral Sclerosis
Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles.
Breast Neoplasms
Choline dehydrogenase polymorphism rs12676 is a functional variation and is associated with changes in human sperm cell function.
Breast Neoplasms
Dietary choline and betaine intake, choline-metabolising genetic polymorphisms and breast cancer risk: a case-control study in China.
Breast Neoplasms
The HOXB13:IL17BR expression index is a prognostic factor in early-stage breast cancer.
Breast Neoplasms
The Prognostic Biomarkers HOXB13, IL17BR, and CHDH Are Regulated by Estrogen in Breast Cancer.
Choline Deficiency
Choline dehydrogenase polymorphism rs12676 is a functional variation and is associated with changes in human sperm cell function.
Choline Deficiency
Common genetic polymorphisms affect the human requirement for the nutrient choline.
Coronary Artery Disease
Cystathionine beta-synthase 844Ins68 polymorphism is not associated with the levels of homocysteine and cysteine in an Indian population.
Endometriosis
Polymorphic variants of folate and choline metabolism genes and the risk of endometriosis-associated infertility.
Fetal Death
Polymorphic variants of genes involved in choline pathway and the risk of intrauterine fetal death.
Frontotemporal Dementia
Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles.
Hyperhomocysteinemia
Single nucleotide polymorphisms in homocysteine metabolism pathway genes: association of CHDH A119C and MTHFR C677T with hyperhomocysteinemia.
Hypernatremia
Renal inner medullary choline dehydrogenase activity: characterization and modulation.
Metabolic Syndrome
Divergent associations of plasma choline and betaine with components of metabolic syndrome in middle age and elderly men and women.
Neoplasms
The HOXB13:IL17BR expression index is a prognostic factor in early-stage breast cancer.
Neoplasms
The Prognostic Biomarkers HOXB13, IL17BR, and CHDH Are Regulated by Estrogen in Breast Cancer.
Obesity
CHDH-PNPLA3 Gene-Gene Interactions Predict Insulin Resistance in Children with Obesity.
Parkinson Disease
Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles.
Pulmonary Disease, Chronic Obstructive
Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles.
Squamous Cell Carcinoma of Head and Neck
A Metabolic Gene Signature to Predict Overall Survival in Head and Neck Squamous Cell Carcinoma.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
population-based study, unfavorable cardiovascular risk factor profile associated with high choline and low betaine concentrations, choline and betaine associated in opposite directions with key components of metabolic syndrome, disruption of mitochondrial choline dehydrogenase pathway
additional information
-
population-based study, unfavorable cardiovascular risk factor profile associated with high choline and low betaine concentrations, choline and betaine associated in opposite directions with key components of metabolic syndrome, disruption of mitochondrial choline dehydrogenase pathway
additional information
-
effects of food deprivation on betaine accumulation, betaine of marginal importance as an intracellular osmolyte in this species
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
increase in the specific activity of the enzyme with choline at alkaline pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
CHDH transcripts and protein are found in oocytes. CHDH becomes highly active during oocyte meiotic maturation and is inactive after fertilization. Endogenous betaine is present at low levels in germinal vesicle stage mouse oocytes before ovulation and reaches high levels in the mature, ovulated egg
brenda
additional information
additional information
CHD is predominantly active in the two main detoxifying organs liver and kidney
brenda
additional information
-
CHD is predominantly active in the two main detoxifying organs liver and kidney
brenda
additional information
-
almost no activity is detected in brain and skeletal muscle
brenda
additional information
CHD is predominantly active in the two main detoxifying organs liver and kidney
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
a nuclear-encoded, membrane-located, mitochondrial enzyme. Human CHD is not an integral membrane protein, but associated to the membrane
brenda
a nuclear-encoded, membrane-located, mitochondrial enzyme
brenda
CHDH appears to have a mitochondria-targeting sequence at its N-terminus (residues 1 to 38). CHDH is found on both the outer and inner membranes of mitochondria in resting cells. Upon induction of mitophagy, CHDH accumulates on the outer membrane in a mitochondrial potential-dependent manner. CHDH accumulates on the outer membrane following mitochondrial damage. Topology of CHDH in the mitochondrial membrane and mechanism by which CHDH translocates across the mitochondrial membranes, overview
brenda
-
metabolic organization of betaine synthesis comparable to those of other vertebrates
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glucose-methanol-choline (GMC) enzyme oxidoreductase enzyme superfamily, members of the family contain a glycine box. Other members of the family all use FAD as cofactor, overall structures and active sites of members of the GMC oxidoreductase enzyme superfamily, overview
evolution
the enzyme belongs to the glucose-methanol-choline (GMC) enzyme oxidoreductase enzyme superfamily, members of the family contain a glycine box. Other members of the family all use FAD as cofactor, overall structures and active sites of members of the GMC oxidoreductase enzyme superfamily, overview
malfunction
-
deletion of choline dehydrogenase results in diminished sperm motility with abnormal mitochondrial morphology, but does not affect fetal viability or alter growth or liver, kidney, or muscle function. Loss of choline dehydrogenase activity results in decreased testicular betaine and increased choline and phosphocholine concentrations. Mitochondrial changes are also detected in liver, kidney, heart, and testis tissues. Chdh-deficient mice have increased plasma total homocysteine
malfunction
-
mutant sperm produced by men who are show polymorphisms rs12676 have 40% and 73% lower ATP concentrations, respectively, in their sperm than controls. Variation rs12676 is associated with decreased CHDH protein in sperm and hepatocytes. A second single-nucleotide polymorphism located in the coding region of IL17BR, rs1025689, is linked to altered sperm motility characteristics and changes in choline metabolite concentrations in sperm
malfunction
the enzyme is associated with male infertility. Absence of CHD enzyme activity causes diminished sperm motility, and mitochondrial alterations are described in testis as well as liver, kidney and heart. Impairments in human CHD activity are associated with homocysteinuria, an accumulation of homocysteine that represents an independent risk factor for cardiovascular diseases. It exists a correlation between high concentrations of choline, low concentrations of glycine betaine in blood and a high-risk profile for cardiovascular disease. Choline deficiency the brain may degrade the membrane phospholipids of the neurons in order to recycle choline for the production of acetylcholine. Localization of Leu78 is relevant to the polymorphism rs12676 associated with male infertility and increased risk factor for breast cancer, on the surface of the enzyme
malfunction
the enzyme is associated with male infertility. Absence of CHD enzyme activity causes diminished sperm motility, and mitochondrial alterations are described in testis as well as liver, kidney and heart. Impairments in human CHD activity are associated with homocysteinuria, an accumulation of homocysteine that represents an independent risk factor for cardiovascular diseases. It exists a correlation between high concentrations of choline, low concentrations of glycine betaine in blood and a high-risk profile for cardiovascular disease. Choline deficiency the brain may degrade the membrane phospholipids of the neurons in order to recycle choline for the production of acetylcholine. Choline is involved in the global hypomethylation of hepatic DNA of rats fed a low choline diet, different rate of development of the hippocampus in the fetal brains of rodent models in the case of low and high maternal choline intake. The folate content in the liver of choline deficient rats decreases by 31% compared to control rats
malfunction
knockdown of CHDH expression impairs CCCP-induced mitophagy and PARK2/parkin-mediated clearance of mitochondria in mammalian cells, including HeLa cells. Conversely, overexpression of CHDH accelerates PARK2-mediated mitophagy
malfunction
downregulation of CHDH expression abolishes the colocalization of MAP1LC3B/LC3B (LC3) with mitochondria
metabolism
in Escherichia coli, the biosynthetic pathway for the production of glycine betaine from choline involves choline dehydrogenase (betA), betaine aldehyde dehydrogenase (betB), a putative regulator (betI) and a choline transporter (betT), the genes are clustered in the bet operon
metabolism
in Escherichia coli, the biosynthetic pathway for the production of glycine betaine from choline involves choline dehydrogenase (betA), catalyzing the first step of the biosynthetic pathway, and betaine aldehyde dehydrogenase (betB), a putative regulator (betI) and a choline transporter (betT), the genes are clustered in the bet operon
metabolism
-
in Escherichia coli, the biosynthetic pathway for the production of glycine betaine from choline involves choline dehydrogenase (betA), betaine aldehyde dehydrogenase (betB), a putative regulator (betI) and a choline transporter (betT), the genes are clustered in the bet operon
-
physiological function
the enzyme oxidizes choline. The regulation of the concentration of choline in tissues and blood is very important as choline plays key roles in different pathways. Choline is involved in the epigenetic regulation of gene expression through DNA methylation, in the biosynthesis of lipoproteins and membrane phospholipids and in the biosynthesis of the neurotransmitter acetylcholine. It is therefore important for the integrity of cell membranes, lipid metabolism and nerve function. Choline is considered an important nutrient for fetal and brain development, and choline is a constituent of phospholipids involved in signal transduction, such as phosphatidylcholine and plasmalogen, and of the phospholipid platelet activating factor. The metabolism of choline is also interrelated with the metabolism of folate. CHD is important for the catabolic utilization of choline when the latter is administered as a pharmacological agent, because choline is involved in the stimulation of cholinergic neuronal activity and in restoring phosphatidylcholine levels in the neuronal membrane, thus displaying a neuroprotective action relevant for diseases such as memory and cognitive deficits. CHD, predominantly active in the two main detoxifying organs liver and kidney, determines the half-life of choline in blood. The metabolic oxidation of choline is related to the risk of developing breast cancer
physiological function
the enzyme oxidizes choline. The regulation of the concentration of choline in tissues and blood is very important as choline plays key roles in different pathways. Choline is involved in the epigenetic regulation of gene expression through DNA methylation, in the biosynthesis of lipoproteins and membrane phospholipids and in the biosynthesis of the neurotransmitter acetylcholine. It is therefore important for the integrity of cell membranes, lipid metabolism and nerve function. Choline is considered an important nutrient for fetal and brain development, and choline is a constituent of phospholipids involved in signal transduction, such as phosphatidylcholine and plasmalogen, and of the phospholipid platelet activating factor. The metabolism of choline is also interrelated with the metabolism of folate. CHD is important for the catabolic utilization of choline when the latter is administered as a pharmacological agent, because choline is involved in the stimulation of cholinergic neuronal activity and in restoring phosphatidylcholine levels in the neuronal membrane, thus displaying a neuroprotective action relevant for diseases such as memory and cognitive deficits. CHD, predominantly active in the two main detoxifying organs liver and kidney, determines the half-life of choline in blood. The metabolic oxidation of choline is related to the risk of developing breast cancer
physiological function
pivotal role of CHDH in mitophagy. CHDH is required for mitophagy in which CHDH interacts with SQSTM1, a mitophagic adaptor molecule, and subsequently facilitates the recruitment of MAP1LC3B/LC3B (LC3) into the mitochondria. CHDH is not a substrate of PARK2 but interacts with SQSTM1 independently of PARK2 to recruit SQSTM1 into depolarized mitochondria. The FB1 domain of CHDH is exposed to the cytosol and is required for the interaction with SQSTM1, and overexpression of the FB1 domain only in cytosol reduces CCCP-induced mitochondrial degradation via competitive interaction with SQSTM1. CHDH is required for PARK2-mediated mitophagy for the recruitment of SQSTM1 and LC3 onto the mitochondria for cargo recognition. CHDH overexpression enhances CCCP-induced clearance of mitochondria. But the expression level of CHDH does not affect the stability of PINK1 protein, although CCCP treatment stabilizes PINK1 in mitochondria. Mitophagic activity of CHDH is independent of CDH enzyme activity
physiological function
in SN4741 dopaminergic cells, CHDH plays a role during mitophagy triggered by 1-methyl-4-phenylpyridinium (MPPC), a Parkinsonism-causing reagent. Like CCCP, treatment with MPPC induces a significant level (30.0%) of colocalization of MAP1LC3B/LC3B (LC3) with mitochondria in SN4741 cells. CHDH is essential in the mitophagy of SN4741 dopaminergic neurons following exposure to MPPC
additional information
rapid turnover of choline when administered as a drug, about 50% of injected choline are directly eliminated via liver and kidney. Structure homology modeling
additional information
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rapid turnover of choline when administered as a drug, about 50% of injected choline are directly eliminated via liver and kidney. Structure homology modeling
additional information
rapid turnover of choline when administered as a drug, about 50% of injected choline are directly eliminated via liver and kidney. Structure homology modeling
additional information
CHDH appears to have a mitochondria-targeting sequence at its N-terminus (residues 1 to 38) and 3 functional domains, named FAD/NAD(P)-binding domain 1 (FB1, residues 39 to 326), FAD-linked reductase domain (RD, residues 333 to 515) and FAD/NAD(P)-binding domain 2 (FB2, residues 511 to 574)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
145000
-
calculated from density gradient profiles and comparison with catalase
61848
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
CHD contains an N-terminal cleavable mitochondrial targeting presequence of 34 amino acids and two cleavage sites may be present for recognition and processing by mitochondrial processing protease and inner membrane protease, mature CHD begins with amino acid 35
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G233T
-
naturally occuring mutation, identificatin of polymorphism rs12676, a non-synonymous SNP located in the CHDH coding region, which is associated with altered sperm motility patterns and dysmorphic mitochondrial structure in sperm, and is associated with increased susceptibility to dietary choline deficiency and risk of breast cancer, phenotye, overview
L78X
localization of Leu78, which is relevant to the polymorphism rs12676 associated with male infertility and increased risk factor for breast cancer, on the surface of the enzyme. Such a replacement of a hydrophobic residue with a positively charge one would locally alter the polarity of the enzyme surface, perhaps decreasing the stability of the enzyme
additional information
construction of a series of CHDH deletion mutants in HeLa cells. Overexpression of the CHDH-RDDELTA or CHDHFB2DELTA mutants induces colocalization of GFP-LC3 with Mito-RFP as effectively as wild-type CHDH, but the CHDH-FB1DELTA mutant fails to do so. Knockdown of CHDH expression impairs CCCP-induced mitophagy and PARK2/parkin-mediated clearance of mitochondria in mammalian cells, including HeLa cells. Conversely, overexpression of CHDH accelerates PARK2-mediated mitophagy. Overexpression of the FB1 domain only in cytosol reduces CCCP-induced mitochondrial degradation via competitive interaction with SQSTM1
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
detergents, e.g. Brij 58, Triton X-100, cholate, deoxycholate or beta-octylglucoside stabilize
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high instability of the enzyme once it is removed from the inner mitochondrial membrane
high instability of the enzyme once it is removed from the inner mitochondrial membrane
high instability of the enzyme once it is removed from the inner mitochondrial membrane
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, pH 7.4 as mitochondrial acetone powder, 20% loss of activity after 6 days
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5°C, pH 7.4, complete loss of activity, partially purified enzyme, 5-6 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, using Triton-treatment, chloroform-treatment and column chromatography on Sepharose 6B
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recombnant enzyme from Escherichia coli strain M15 by ammonium sulfate fractionation and anion exchange chromatography
using 0.5% Brij 58 treatment, column chromatography on DEAE-cellulose and gel filtration on Toyopearl HW-60S
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using column chromatography of the chemically modified enzyme with 5,5'-dithiobis(2-nitrobenzoic acid) on DEAE-Sepharose CL-6B and choline-Sepharose 4B with C3-spacer, subsequent release of the thionitrobenzoate with dithiothreitol, and a second column chromatography on DEAE-Sepharose CL-6B in the presence of 0.1% Triton X-100
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene betA, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strain JM109
gene betA, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strain M15/pREP4, subcloning in strain JM109
gene Chdh, DNA and amino acid sequence determination and analysis, polymorphism rs12676 genotyping, overview
-
gene CHDH, recombinant expression of wild-type and truncated mutant enzymes, enzyme overexpression in HeLa cells
transformed with the chimeric betA gene from Escherichia coli to betaine-producing tobacco
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
liver samples from Chdh-deficient mice have 37% of the CHDH activity measured in wild type samples
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
population-based study, relation of plasma choline and betaine to smoking, physical activity, BMI, percent body fat, waist circumference, blood pressure, serum lipids and glucose
diagnostics
study of prognostic biomarkers for breast cancer identifies the expression of CHD among three human genes controlled by estrogens, and shows that this is a strong predictor of the outcome of treatment with tamoxifen in early-stage (ER)-positive breast cancer patients
diagnostics
study of prognostic biomarkers for breast cancer identifies the expression of CHD among three human genes controlled by estrogens, and shows that this is a strong predictor of the outcome of treatment with tamoxifen in early-stage (ER)-positive breast cancer patients
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ameyama, M.; Shinagawa, E.; Matsushita, K.; Takimoto, K.; Nakashima, K.; Adachi, O.
Mammalian choline dehydrogenase is a quinoprotein
Agric. Biol. Chem.
49
3623-3626
1985
Canis lupus familiaris
-
brenda
Rendina, G.; Singer, T.P.
Studies on choline dehydrogenase
J. Biol. Chem.
234
1605-1610
1959
Rattus norvegicus
brenda
Barrett, M.C.; Dawson, A.P.
The reaction of choline dehydrogenase with some electron acceptors
Biochem. J.
151
677-683
1975
Rattus norvegicus
brenda
Tsuge, H.; Nakano, Y.; Onishi, H.; Futamura, Y.; Ohashi, K.
A novel purification and some properties of rat liver mitochondrial choline dehydrogenase
Biochim. Biophys. Acta
614
274-284
1980
Rattus norvegicus
brenda
Nagasawa, T.; Mori, N.; Tani, Y.; Ogata, K.
Characterization of choline dehydrogenase from Pseudomonas aeruginosa A-16
Agric. Biol. Chem.
40
2077-2084
1976
Pseudomonas aeruginosa, Pseudomonas aeruginosa A-16
-
brenda
Nagasawa, T.; Kawabata, Y.; Tani, Y.; Ogata, K.
Choline dehydrogenase of Pseudomonas aeruginosa A-16
Agric. Biol. Chem.
39
1513-1514
1975
Pseudomonas aeruginosa, Pseudomonas aeruginosa A-16
-
brenda
Bater, A.J.; Venables, W.A.
The characterisation of inducible dehydrogenases specific for the oxidation of D-alanine, allohydroxy-D-proline, choline and sarcosine as peripheral membrane proteins in Pseudomonas aeruginosa
Biochim. Biophys. Acta
468
209-226
1977
Pseudomonas aeruginosa
brenda
Russell, R.; Scopes, R.K.
Use of hydrophobic chromatography for purification of the membrane-located choline dehydrogenase from a Pseudomonas strain
Bioseparation
4
279-284
1994
Pseudomonas aeruginosa, Pseudomonas aeruginosa C10
brenda
Holmstrom, K.O.; Somersalo, S.; Mandal, A.; Palva, T.E.; Welin, B.
Improved tolerance to salinity and low temperature in transgenic tobacco producing glycine betaine
J. Exp. Bot.
51
177-185
2000
Nicotiana tabacum
brenda
Gadda, G.; McAllister-Wilkins, E.E.
Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata
Appl. Environ. Microbiol.
69
2126-2132
2003
Halomonas elongata
brenda
Huang, S.; Lin, Q.
Functional expression and processing of rat choline dehydrogenase precursor
Biochem. Biophys. Res. Commun.
309
344-350
2003
Rattus norvegicus (Q6UPE0)
brenda
Slow, S.; Garrow, T.A.
Liver choline dehydrogenase and kidney betaine-homocysteine methyltransferase expression are not affected by methionine or choline intake in growing rats
J. Nutr.
136
2279-2283
2006
Rattus norvegicus
brenda
Treberg, J.R.; Driedzic, W.R.
The accumulation and synthesis of betaine in winter skate (Leucoraja ocellata)
Comp. Biochem. Physiol. A
147
475-483
2007
Leucoraja ocellata
brenda
Konstantinova, S.V.; Tell, G.S.; Vollset, S.E.; Nygard, O.; Bleie, O.; Ueland, P.M.
Divergent associations of plasma choline and betaine with components of metabolic syndrome in middle age and elderly men and women
J. Nutr.
138
914-920
2008
Homo sapiens (Q8NE62), Homo sapiens
brenda
Clow, K.A.; Treberg, J.R.; Brosnan, M.E.; Brosnan, J.T.
Elevated tissue betaine contents in developing rats are due to dietary betaine, not to synthesis
J. Nutr.
138
1641-1646
2008
Rattus norvegicus
brenda
Duan, X.; Song, Y.; Yang, A.; Zhang, J.
The transgene pyramiding tobacco with betaine synthesis and heterologous expression of AtNHX1 is more tolerant to salt stress than either of the tobacco lines with betaine synthesis or AtNHX1
Physiol. Plant.
135
281-295
2009
Escherichia coli
brenda
Johnson, A.R.; Craciunescu, C.N.; Guo, Z.; Teng, Y.W.; Thresher, R.J.; Blusztajn, J.K.; Zeisel, S.H.
Deletion of murine choline dehydrogenase results in diminished sperm motility
FASEB J.
24
2752-2761
2010
Mus musculus
brenda
Rajan, L.; Joseph, T.; Thampuran, N.; James, R.
Functional characterization and sequence analysis of choline dehydrogenase from Escherichia coli
Genet. Eng. Biotechnol. J.
2010
0000
2010
Escherichia coli (A7LLT8), Escherichia coli TCJAR023 (A7LLT8)
-
brenda
Johnson, A.R.; Lao, S.; Wang, T.; Galanko, J.A.; Zeisel, S.H.
Choline dehydrogenase polymorphism rs12676 is a functional variation and is associated with changes in human sperm cell function
PLoS ONE
7
e36047
2012
Homo sapiens
brenda
AnbuRajan, L.; Sindhuja, S.; Rajalakshmi, Y.; Umashankar, V.
Cloning of choline dehydrogenase from Escherichia coli: its polynucleotide and polypeptide analysis
Res. J. Microbiol.
6
297-303
2011
Escherichia coli (C1KFX7)
-
brenda
Salvi, F.; Gadda, G.
Human choline dehydrogenase medical promises and biochemical challenges
Arch. Biochem. Biophys.
537
243-252
2013
Homo sapiens (Q8NE62), Homo sapiens, Rattus norvegicus (Q6UPE0)
brenda
Park, S.; Choi, S.G.; Yoo, S.M.; Son, J.H.; Jung, Y.K.
Choline dehydrogenase interacts with SQSTM1/p62 to recruit LC3 and stimulate mitophagy
Autophagy
10
1906-1920
2014
Homo sapiens (Q8NE62), Mus musculus (Q8BJ64)
brenda
McClatchie, T.; Meredith, M.; Ouedraogo, M.O.; Slow, S.; Lever, M.; Mann, M.R.W.; Zeisel, S.H.; Trasler, J.M.; Baltz, J.M.
Betaine is accumulated via transient choline dehydrogenase activation during mouse oocyte meiotic maturation
J. Biol. Chem.
292
13784-13794
2017
Mus musculus (Q8BJ64), Mus musculus
brenda
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