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betaine aldehyde + phenazine methosulfate
glycine-betaine + ?
-
-
-
-
?
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
choline + 2,6-dichlorophenolindophenol
betaine aldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
choline + acceptor + phenazine methosulfate
betaine aldehyde + ?
-
-
-
-
?
choline + coenzyme Q1
betaine aldehyde + reduced coenzyme Q1
-
mitochondrial oxidation of choline
-
?
choline + p-benzoquinone
betaine aldehyde + reduced p-benzoquinone
-
-
-
-
r
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
additional information
?
-
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
-
four electron oxidation with betaine aldehyde as intermediate, provides glycine-betaine as compatible solute
-
-
?
choline + 2 acceptor + H2O
glycine-betaine + 2 reduced acceptor + H+
-
four electron oxidation with betaine aldehyde as intermediate
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: 2,6-dichlorophenolindophenol
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
choline is the sole substrate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
relation of plasma choline and betaine to cardiovascular risk factors, mitochondrial choline dehydrogenase pathway
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
effects of food-deprivation on betaine accumulation and the levels of betaine synthesizing enzymes
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
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
-
cytochrome c, particulate enzyme: 3.1% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: 2,6-dichlorophenolindophenol
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor ferricyanide, particulate enzyme: 112% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor 2,6-dichlorophenolindophenol, particulate enzyme: 3.2% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor: phenazine methosulfate, 100% relative activity
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
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
-
cytochrome c, particulate enzyme: 3.1% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor ferricyanide, particulate enzyme: 112% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor 2,6-dichlorophenolindophenol, particulate enzyme: 3.2% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor: phenazine methosulfate, 100% relative activity
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
-
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor: ubiquinone-2
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
the enzyme can use only choline and betaine aldehyde
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor O2: 73% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: 2,6-dichlorophenolindophenol
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor 2,6-dichlorophenolindophenol: 27% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
absolute requirement for an electron acceptor other than O2
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
reverse reaction at 5.2% of forward reaction
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
cytochrome c, ferricyanide, methylene blue and 2,6-dichlorophenolindophenol show no direct reaction with the enzyme
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor methylene blue: 4% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
coenzyme Q, primary electron acceptor in vivo
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor cytochrome c: 63% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor: phenazine methosulfate, 100% relative activity
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: phenazine methosulfate
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
not: 2-dimethylaminoethanol, monoethanolamine
-
r
choline + acceptor
betaine aldehyde + reduced acceptor
-
electron acceptor: p-benzoquinone
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
-
acceptor ferricyanide: 42% relative activity to phenazine methosulfate
-
?
choline + acceptor
betaine aldehyde + reduced acceptor
connects choline to the respiratory chain
-
-
?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
-
-
-
?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
-
-
-
?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
-
-
-
?
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
-
-
-
-
r
choline + phenazine methosulfate
betaine aldehyde + reduced phenazine methosulfate
-
-
-
-
r
additional information
?
-
-
the enzyme is responsible for the two-step choline oxidation to betaine together with the betaine-homocysteine methyltransferase
-
-
?
additional information
?
-
the enzyme is specific for choline or betaine aldehyde as substrate, substrate specificity, overview
-
-
?
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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
Choline metabolism and risk of breast cancer in a population-based study.
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.
Pancreatic Neoplasms
The role of the folate pathway in pancreatic cancer risk.
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.
Starvation
The accumulation and synthesis of betaine in winter skate (Leucoraja ocellata).
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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
downregulation of CHDH expression abolishes the colocalization of MAP1LC3B/LC3B (LC3) with mitochondria
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
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
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
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
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
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
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
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)
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
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
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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
Rattus norvegicus (Q6UPE0), Homo sapiens (Q8NE62), Homo sapiens
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
Mus musculus (Q8BJ64), Homo sapiens (Q8NE62)
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