Information on EC 1.1.99.1 - choline dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.99.1
-
RECOMMENDED NAME
GeneOntology No.
choline dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
choline + acceptor = betaine aldehyde + reduced acceptor
show the reaction diagram
-
-
-
-
choline + acceptor = betaine aldehyde + reduced acceptor
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
choline degradation I
-
glycine betaine biosynthesis I (Gram-negative bacteria)
-
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CHD
-
-
-
-
CHDH
-
-
CHDH
-
-
ChoDH
Q8NE62
-
choline dehydrogenase
-
-
choline dehydrogenase
-
-
choline oxidase
-
-
-
-
choline-cytochrome c reductase
-
-
-
-
choline:(acceptor) oxidoreductase
-
-
-
-
dehydrogenase, choline
-
-
-
-
oxidase, choline
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-67-5
identical with CAS Reg. No. of EC 1.1.3.17
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isolated from a finfish, gene betA
UniProt
Manually annotated by BRENDA team
isolated from salted shark, Scoliodon sp., gene betA
UniProt
Manually annotated by BRENDA team
Escherichia coli TCJAR023
isolated from a finfish, gene betA
UniProt
Manually annotated by BRENDA team
halophil
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene Chdh
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa A-16
A-16 strain
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa C10
C10 strain
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
metabolism
A7LLT8
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
C1KFX7
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
Escherichia coli TCJAR023
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + phenazine methosulfate
glycine-betaine + ?
show the reaction diagram
-
-
-
-
?
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
show the reaction diagram
-
four electron oxidation with betaine aldehyde as intermediate, provides glycine-betaine as compatible solute, four electron oxidation with betaine aldehyde as intermediate
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Q6UPE0
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Q8NE62
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor: ubiquinone-2
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
the enzyme can use only choline and betaine aldehyde
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor 3-(4,5-dimethylthiazolyl-2-)-2,5-diphenyltetrazolium bromide, particulate enzyme: 12.4% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor O2: 73% relative activity to phenazine methosulfate
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
cytochrome c, particulate enzyme: 3.1% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: 2,6-dichlorophenolindophenol
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: 2,6-dichlorophenolindophenol
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: 2,6-dichlorophenolindophenol
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor 2,6-dichlorophenolindophenol: 27% relative activity to phenazine methosulfate
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
absolute requirement for an electron acceptor other than O2
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor ferricyanide, particulate enzyme: 112% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
reverse reaction at 5.2% of forward reaction
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
cytochrome c, ferricyanide, methylene blue and 2,6-dichlorophenolindophenol show no direct reaction with the enzyme
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor 2,6-dichlorophenolindophenol, particulate enzyme: 3.2% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor methylene blue: 4% relative activity to phenazine methosulfate
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
coenzyme Q, primary electron acceptor in vivo
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor cytochrome c: 63% relative activity to phenazine methosulfate, acceptor: phenazine methosulfate, 100% relative activity
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor: phenazine methosulfate, 100% relative activity
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate, choline is the sole substrate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
not: 2-dimethylaminoethanol, monoethanolamine
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
electron acceptor: p-benzoquinone
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
acceptor ferricyanide: 42% relative activity to phenazine methosulfate
-
-
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Q6UPE0
connects choline to the respiratory chain
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
effects of food-deprivation on betaine accumulation and the levels of betaine synthesizing enzymes
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Q8NE62
relation of plasma choline and betaine to cardiovascular risk factors, mitochondrial choline dehydrogenase pathway
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Pseudomonas aeruginosa C10
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Pseudomonas aeruginosa A-16
-
acceptor 3-(4,5-dimethylthiazolyl-2-)-2,5-diphenyltetrazolium bromide, particulate enzyme: 12.4% relative activity to phenazine methosulfate, cytochrome c, particulate enzyme: 3.1% relative activity to phenazine methosulfate, acceptor ferricyanide, particulate enzyme: 112% relative activity to phenazine methosulfate, acceptor 2,6-dichlorophenolindophenol, particulate enzyme: 3.2% relative activity to phenazine methosulfate, acceptor: phenazine methosulfate, 100% relative activity
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Pseudomonas aeruginosa A-16
-
-
-
?
choline + acceptor + phenazine methosulfate
betaine aldehyde + ?
show the reaction diagram
-
-
-
-
?
choline + coenzyme Q1
betaine aldehyde + reduced coenzyme Q1
show the reaction diagram
-
mitochondrial oxidation of choline
-
-
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
show the reaction diagram
A7LLT8
-
-
-
?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
show the reaction diagram
C1KFX7
-
-
-
?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
show the reaction diagram
Escherichia coli TCJAR023
A7LLT8
-
-
-
?
additional information
?
-
-
the enzyme is responsible for the two-step choline oxidation to betaine together with the betaine-homocysteine methyltransferase
-
-
-
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
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
show the reaction diagram
-
four electron oxidation with betaine aldehyde as intermediate, provides glycine-betaine as compatible solute
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Q8NE62
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
show the reaction diagram
Q6UPE0
connects choline to the respiratory chain
-
-
?
choline + coenzyme Q1
betaine aldehyde + reduced coenzyme Q1
show the reaction diagram
-
mitochondrial oxidation of choline
-
-
additional information
?
-
-
the enzyme is responsible for the two-step choline oxidation to betaine together with the betaine-homocysteine methyltransferase
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
coenzyme Q
-
primary electron acceptor in vivo
phenazine methosulfate
-
-
pyrroloquinoline quinone
-
as prosthetic group
pyrroloquinoline quinone
-
-
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
iron sulfur cluster
Q6UPE0
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-Dimethylaminoethanol
-
-
AgNO3
-
1 mM causes 100% inhibition
Benzyltrimethylammonium chloride
-
slight
Betaine aldehyde
-
choline dehydrogenase activity
Betaine hydrochloride
-
slight
CuSO4
-
1 mM causes 100% inhibition
Dimethylglycine
-
slight
DL-3-hydroxybutyrate
-
at 16.7 mM acts as weak inhibitor
DL-Carnitine hydrochloride
-
slight
HgCl2
-
1 mM causes 100% inhibition
iodoacetic acid
-
-
KCN
-
1 mM inhibits
Mercuric acetate
-
-
MnCl2
-
1 mM causes 100% inhibition
NaCN
-
1 mM inhibits
p-chloromercuribenzoate
-
-
Phenyltriethylammonium iodide
-
slight
Semicarbazide
-
-
Tetra-n-butylammonium iodide
-
slight
Tetra-n-propylammonium iodide
-
slight
Tetraethylammonium iodide
-
slight
Tetramethylammonium iodide
-
slight
Triethylbenzylammonium iodide
-
slight
Monoethanolamine
-
-
additional information
-
the enzyme expression is not affected by methionine or choline intake in liver, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
as prosthetic group
coenzyme Q
-
primary electron acceptor in vivo
additional information
-
the enzyme expression is not affected by methionine or choline intake in liver, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
2,6-dichlorophenol-indophenol
-
at 10 mM choline
3.1
-
Betaine aldehyde
-
at 1 mM phenazine methosulfate
2
-
choline
-
in the presence of 0.05 mM phenazine methosulfate
7
-
choline
-
electron acceptor: phenazine methosulfate
0.83
-
p-benzoquinone
-
at 10 mM choline
0.14
-
phenazine methosulfate
-
-
0.18
-
phenazine methosulfate
-
at 10 mM choline
1.1
-
phenazine methosulfate
-
with choline
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
2-Dimethylaminoethanol
-
inhibits the enzyme competitively
3.3
-
Betaine aldehyde
-
inhibits the oxidation of choline competitively
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.041
-
Q6UPE0
enzyme from rat liver mitochondria
0.047
-
Q6UPE0
recombinant enzyme from yeast mitochondria
1.8
-
-
purified enzyme, pH 7.0, 25C
additional information
-
-
effects of food deprivation on betaine accumulation, betaine of marginal importance as an intracellular osmolyte in this species
additional information
-
Q8NE62
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
A7LLT8
assay at
7.6
8.2
-
crude enzyme extract
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
10
-
about 50% of activity maximum at pH 7.5 and pH 10.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.45
-
A7LLT8
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q8NE62
choline and betaine levels
Manually annotated by BRENDA team
-
major site of betaine synthesis
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
major site of betaine synthesis
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
additional information
-
almost no activity is detected in brain and skeletal muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
peripheral membrane protein
Manually annotated by BRENDA team
Pseudomonas aeruginosa C10
-
-
-
Manually annotated by BRENDA team
Q6UPE0
inner membrane
Manually annotated by BRENDA team
-
metabolic organization of betaine synthesis comparable to those of other vertebrates
Manually annotated by BRENDA team
Pseudomonas aeruginosa A-16
-
;
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60000
70000
-
gel filtration
145000
-
-
calculated from density gradient profiles and comparison with catalase
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
? * 62000, SDS-PAGE
?
-
x * 61848, sequence calculation
?
Escherichia coli TCJAR023
-
x * 61848, sequence calculation
-
monomer
-
1 * 66000, SDS-PAGE
monomer
Pseudomonas aeruginosa C10
-
1 * 66000, SDS-PAGE
-
additional information
C1KFX7
secondary structure analysis, overview
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
9.5
-
10 min, 37C, stable
additional information
-
-
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
10 min, pH 8.3, 10% loss of activity
37
-
-
10 min, pH 8.0-9.5, stable
40
-
-
10 min, pH 8.3, 50% loss of activity
50
-
-
10 min, pH 8.3, 100% loss of activity
60
-
-
3 min, pH 7, 63% inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
detergents, e.g. Brij 58, Triton X-100, cholate, deoxycholate or beta-octylglucoside stabilize
-
25 cycles of freezing/thawing cause 40% loss of activity
-
glycerol, 30%, stabilizes partially purified enzyme
-
repeated freezing and thawing: rapid loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, phosphate buffer, pH 7.0, 2 M sorbitol, 20% glycerol
-
-20C , stable
-
5C, pH 7.4, complete loss of activity, partially purified enzyme, 5-6 days
-
-15C, 50% loss of activity, 1 month
-
-15C, pH 7.4 as mitochondrial acetone powder, 20% loss of activity after 6 days
-
-15C, pH 7.4 in extracts, 13% loss of activity after 6 days
-
-20C, stable, partially purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using 0.5% Brij 58 treatment, column chromatography on DEAE-cellulose and gel filtration on Toyopearl HW-60S
-
recombnant enzyme from Escherichia coli strain M15 by ammonium sulfate fractionation and anion exchange chromatography
A7LLT8
partial, using Triton-treatment, chloroform-treatment and column chromatography on Sepharose 6B
-
using column chromatography on thio-hexyl and on an anion exchanger
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene betA, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strain JM109
C1KFX7
gene betA, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in Escherichia coli strain M15/pREP4, subcloning in strain JM109
A7LLT8
expressed in Escherichia coli OrigamiB(DE3)pLysS
-
gene Chdh, DNA and amino acid sequence determination and analysis, polymorphism rs12676 genotyping, overview
-
transformed with the chimeric betA gene from Escherichia coli to betaine-producing tobacco
-
expressed in Saccharomyces cerevisiae INVSC2as GFP fusion protein
Q6UPE0
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
liver samples from Chdh-deficient mice have 37% of the CHDH activity measured in wild type samples
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Q8NE62
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