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5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid
-
5-[3-(R,S)-3-amino-3-(hydroxyphosphorylpropyl)sulfanyl]-3,3-dimethylpentanoic acid
-
5-[3-(R,S)-3-amino-3-(hydroxyphosphorylpropyl)sulfanyl]pentanoic acid
-
H2O2
causes a loss of catalytic Zn and a correlative loss of activity, irreversible
methyl methanethiosulfonate
causes a loss of catalytic Zn and a correlative loss of activity. Addition of beta-mercaptoethanol and exogenous Zn after methyl methanethiosulfonate treatment restores activity
S-(delta-Carboxybutyl)-DL-homocysteine
-
(2S,11RS)-5-thia-2,11-diamino-8,8-dimethyldodecanedioic acid
-
more than 90% inhibition at 0.02 mM
(2S,11RS)-5-thia-2,11-diaminododecanedioic acid
-
about 60% inhibition at 0.02 mM
(2S,11S)-5,8-dithia-2,11-diaminododecanedioic acid
-
about 60% inhibition at 0.02 mM
(2S,5RS,8RS,11S)-5,8-dithia-2,11-diaminododecanedioic acid 5,8-dioxide
-
about 20% inhibition at 0.02 mM
(2S,8RS,11RS)-5-thia-2,11-diamino-8-methyldodecanedioic acid
-
competitive, more than 90% inhibition at 0.02 mM
(R,S)-2-(3-amino-3-carboxy-propylsulfanyl)-benzoic acid
-
ca. 43% inhibition at 0.02 mM
(R,S)-2-amino-4-(2-carboxy-ethyldisulfanyl)-butyric acid
-
ca. 30% inhibition at 0.02 mM
(R,S)-2-amino-4-(2-carboxymethylsulfanyl-ethylsulfanyl)-butyric acid
-
100% inhibition at 0.02 mM, very potent inhibitor and one of the strongest ever reported
(R,S)-2-amino-4-(2-carboxymethylsulfinyl-ethylsulfanyl)-butyric acid
-
ca. 90% inhibition at 0.02 mM
(R,S)-2-amino-4-(2-phosphonomethoxy-ethylsulfanyl)-butyrate
-
ca. 26% inhibition at 0.02 mM
(R,S)-2-amino-4-(3-carboxy-propylsulfanyl)-butyric acid
-
ca. 20% inhibition at 0.02 mM
(R,S)-2-amino-4-(4-carboxymethyl-benzylsulfanyl)-butyric acid
-
ca. 10% inhibition at 0.02 mM
(R,S)-2-amino-4-(4-phosphono-butylsulfanyl)-butyric acid
-
ca. 98% inhibition at 0.02 mM
(R,S)-2-amino-4-methylsulfanylmethylsulfanyl-butyric acid
-
ca. 21% inhibition at 0.02 mM
(R,S)-2-amino-4-[(phosphonomethyl-carbamoyl)-methylsulfanyl]-butyrate
-
ca. 9% inhibition at 0.02 mM
(R,S)-3-(3-amino-3-carboxy-propylsulfanyl)-benzoic acid
-
ca. 13% inhibition at 0.02 mM
(R,S)-4-(3-amino-3-carboxy-propylsulfanyl)-benzoic acid
-
ca. 99% inhibition at 0.02 mM
(R,S)-5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid
-
100% inhibition at 0.02 mM, very potent inhibitor and one of the strongest ever reported, competitive inhibition with respect to betaine binding
(R,S)-5-(3-amino-3-carboxy-propylsulfinyl)-pentanoic acid
-
ca. 97% inhibition at 0.02 mM
(R,S)-5-(3-amino-3-carboxy-propylsulfonyl)-pentanoic acid
-
ca. 29% inhibition at 0.02 mM
(R,S)-6-(3-amino-3-carboxy-propylsulfanyl)-hexanoic acid
-
100% inhibition at 0.02 mM, very potent inhibitor and one of the strongest ever reported
(R,S,R,S)-2-amino-4-(2-amino-2-carboxy-ethylsulfinyl)-butyric acid
-
ca. 10% inhibition at 0.02 mM
(RS)-2-amino-4-[(2-carboxyethylthio)methylthio]butanoic acid
-
97.6% inhibition at 0.02 mM
(RS)-2-amino-4-[(3-carboxypropyl)disulfanyl]butanoic acid
-
19.1% inhibition at 0.02 mM
(RS)-2-amino-4-[2-(carboxymethylamino)ethylthio]butanoic acid
-
37.1% inhibition at 0.02 mM
(RS)-2-amino-4-[2-(R)-(1-carboxyethylamino)ethylthio]butanoic acid
-
15.5% inhibition at 0.02 mM
(RS)-2-amino-4-[2-(S)-(1-carboxyethylamino)ethylthio]butanoic acid
-
19.8% inhibition at 0.02 mM
(RS)-2-amino-4-[2-[(carboxymethyl)(methyl)amino]ethylthio]-butanoic acid
-
98.5% inhibition at 0.02 mM
(RS)-2-amino-4-[3-[(carboxymethyl)(methyl)amino]propylthio]butanoic acid
-
79.01% inhibition at 0.02 mM
(RS)-2-amino-5-(3-carboxypropylthio)pentanoic acid
-
5.4% inhibition at 0.02 mM
(RS)-2-aminodecanedioic acid
-
2.11% inhibition at 0.02 mM
(RS)-2-[[2-(3-amino-3-carboxypropylthio)ethyl]dimethylammonium]acetate
-
23.8% inhibition at 0.02 mM
(RS)-2-[[3-(3-amino-3-carboxypropylthio)propyl]dimethylammonio]acetate
-
3.3% inhibition at 0.02 mM
(RS)-5-(3-amino-3-carboxypropoxy)pentanoic acid
-
9.8% inhibition at 0.02 mM
(RS)-5-(3-amino-3-carboxypropylselanyl)pentanoic acid
-
complete inhibition at 0.02 mM
(RS)-5-(3-amino-3-carboxypropylthio)-3,3-dimethylpentanoic acid
-
highly potent inhibitor of BHMT, complete inhibition at 0.02 mM
(RS)-5-(3-amino-3-carboxypropylthio)-3-methylpentanoic acid
-
highly potent inhibitor of BHMT, complete inhibition at 0.02 mM
3,3-Dimethylbutyrate
-
competitive to betaine
5-[(3-amino-3-carboxypropyl)sulfanyl]pentanoic acid
-
complete inhibition at 0.02 mM
Ac-Val-Ala-Leu-His-NH2
-
0.1 mM, 25.9% inhibition
Ac-Val-DL-Ala-psi[(PO2-)-CH2]-DL-Leu-His-NH2
-
0.1 mM, 57.4% inhibition
Ac-Val-DL-Phe-psi[(PO2-)-CH2]-DL-Ala-His-NH2
-
0.1 mM, 8.7% inhibition
Ac-Val-DL-Phe-psi[(PO2-)-CH2]-DL-Leu-His-NH2
-
0.1 mM, 53.7% inhibition
AdoMet
-
weak inhibitor, at 2 mM: 24% inhibition
dimethylsulfoniopropionate
-
weak inhibitor, at 2 mM: 29% inhibition
Isovalerate
-
competitive to betaine
L-Asp
-
10 mM Asp inhibits BHMT
S-(delta-Carboxybutyl)-DL-homocysteine
S-(delta-carboxybutyl)-L-homocysteine
S-adenosyl-L-methionine
-
no effect on recombinant enzyme
Val-DL-Ala-psi[(PO2-)-CH2]-DL-Leu-His-NH2
-
0.1 mM, 70.6% inhibition
Val-DL-Phe-psi[(PO2-)-CH2]-DL-Leu-His-NH2
-
0.1 mM, 80.3% inhibition
Butyrate
-
-
Butyrate
-
moderate, competitive to betaine
dimethylglycine
-
at 0.2 mM: 80% inhibition, at 2 mM: 97% inhibition
dimethylglycine
-
weak inhibitor, at 2 mM: 11% inhibition
dimethylsulfonioacetate
-
at 2 mM: 79% inhibition
dimethylsulfonioacetate
-
weak inhibitor, at 2 mM: 20% inhibition
methionine
-
at 2 mM: 60% inhibition
methionine
-
weak inhibitor at 2 mM: 15% inhibition
S-(delta-Carboxybutyl)-DL-homocysteine
-
-
S-(delta-Carboxybutyl)-DL-homocysteine
-
strong
S-(delta-carboxybutyl)-L-homocysteine
-
at 0.05 mM: 97% inhibition, at 0.5 mM: total inhibition
S-(delta-carboxybutyl)-L-homocysteine
-
weak inhibitor, at 0.5 mM: 26% inhibition
additional information
-
product inhibition
-
additional information
-
no inhibition by sarcosine
-
additional information
-
no inhibition by sarcosine
-
additional information
-
not inhibitory: S-(gamma-carboxypropyl)-DL-homocysteine, S-(beta-carboxyethyl)-DL-homocysteine
-
additional information
-
not inhibitory: methionine or ethionine
-
additional information
-
no inhibition by Ac-Val-DL-Ala-psi[(PO2-)-CH2]-DL-Leu-Cys-NH2, Ac-DL-Ala-psi[(PO2-)-CH2]-DL-Leu-NH2, Ac-Val-DL-Ala-psi[(PO2-)-CH2]-DL-Leu-His
-
additional information
-
not inhibited by (R)-5-(2-amino-2-carboxy-ethylsulfanyl)-pentanoic acid, (R,S)-4-allylsulfanyl-2-amino-butyric acid and (R,S)-2-amino-4-[(phosphonomethyl-carbamoyl)-methylsulfanyl]-butyric acid ester
-
additional information
S-adenosylmethionine decreases BHMT mRNA levels in dose- and time-dependent manner, down-regulates BHMT expression in part by inducing nuclear factor kappaB, which acts as a repressor for the human BHMT gene, the inhibitor is nuclear factor kappaB dependent. 5'-methylthioadenosine decreases BHMT mRNA levels in dose- and time-dependent manner, down-regulates BHMT expression in part by inducing nuclear factor kappaB, which acts as a repressor for the human BHMT gene, the inhibitor has nuclear factor kappaB dependent and -independent mechanisms
-
additional information
-
S-adenosylmethionine decreases BHMT mRNA levels in dose- and time-dependent manner, down-regulates BHMT expression in part by inducing nuclear factor kappaB, which acts as a repressor for the human BHMT gene, the inhibitor is nuclear factor kappaB dependent. 5'-methylthioadenosine decreases BHMT mRNA levels in dose- and time-dependent manner, down-regulates BHMT expression in part by inducing nuclear factor kappaB, which acts as a repressor for the human BHMT gene, the inhibitor has nuclear factor kappaB dependent and -independent mechanisms
-
additional information
-
not inhibited by (RS)-2-[[(3-amino-3-carboxypropylthio)methyl]dimethylammonium] acetate and (RS)-2-amino-4-[2-(2-carboxyethylamino)ethylthio]butanoic acid
-
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Abruptio Placentae
Polymorphisms in methionine synthase reductase and betaine-homocysteine S-methyltransferase genes: risk of placental abruption.
Adenoma
Twenty-four non-synonymous polymorphisms in the one-carbon metabolic pathway and risk of colorectal adenoma in the Nurses' Health Study.
Anencephaly
Neural tube defects and folate pathway genes: family-based association tests of gene-gene and gene-environment interactions.
Atherosclerosis
Betaine:homocysteine methyltransferase--a new assay for the liver enzyme and its absence from human skin fibroblasts and peripheral blood lymphocytes.
betaine-homocysteine s-methyltransferase deficiency
Betaine-homocysteine S-methyltransferase deficiency causes increased susceptibility to noise-induced hearing loss associated to plasma hyperhomocysteinemia.
betaine-homocysteine s-methyltransferase deficiency
Homocysteinemia in mice with genetic betaine homocysteine S-methyltransferase deficiency is independent of dietary folate intake.
betaine-homocysteine s-methyltransferase deficiency
Mouse betaine-homocysteine S-Methyltransferase deficiency reduces body fat via increasing energy expenditure and impairing lipid synthesis and enhancing glucose oxidation in white adipose tissue.
Breast Neoplasms
Dietary choline and betaine intake, choline-metabolising genetic polymorphisms and breast cancer risk: a case-control study in China.
Breast Neoplasms
The plasma peptides of breast versus ovarian cancer.
Carcinoma
L-arginine-glycine amidinotransferase, betaine-homocysteine S-methyltransferase, and neuropolypeptide H3 are diminished in renal clear cell carcinoma of humans.
Carcinoma, Hepatocellular
A splicing variant leads to complete loss of function of betaine-homocysteine methyltransferase (BHMT) gene in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Deletion of betaine-homocysteine S-methyltransferase in mice perturbs choline and 1-carbon metabolism, resulting in fatty liver and hepatocellular carcinomas.
Carcinoma, Hepatocellular
Downregulation of betaine homocysteine methyltransferase (BHMT) in hepatocellular carcinoma associates with poor prognosis.
Carcinoma, Hepatocellular
Dynamic regulation of hepatic lipid droplet properties by diet.
Carcinoma, Hepatocellular
Osmotic regulation of betaine homocysteine-S-methyltransferase expression in H4IIE rat hepatoma cells.
Carcinoma, Hepatocellular
Reduced mRNA abundance of the main enzymes involved in methionine metabolism in human liver cirrhosis and hepatocellular carcinoma.
Cardiovascular Diseases
Betaine homocysteine S-methyltransferase: just a regulator of homocysteine metabolism?
Cardiovascular Diseases
The betaine/GABA transporter and betaine: roles in brain, kidney, and liver.
Choline Deficiency
Common genetic polymorphisms affect the human requirement for the nutrient choline.
Cleft Lip
Are the betaine-homocysteine methyltransferase (BHMT and BHMT2) genes risk factors for spina bifida and orofacial clefts?
Cleft Lip
New evidence for the role of cystathionine beta-synthase in non-syndromic cleft lip with or without cleft palate.
Cleft Palate
Are the betaine-homocysteine methyltransferase (BHMT and BHMT2) genes risk factors for spina bifida and orofacial clefts?
Cleft Palate
New evidence for the role of cystathionine beta-synthase in non-syndromic cleft lip with or without cleft palate.
Colonic Neoplasms
Alteration of gene expression in rat colon mucosa after exercise.
Coronary Artery Disease
Investigations of a common genetic variant in betaine-homocysteine methyltransferase (BHMT) in coronary artery disease.
cystathionine beta-synthase deficiency
Mice deficient in cystathionine beta synthase display altered homocysteine remethylation pathway.
Diabetes Mellitus
Betaine ameliorates impaired steroidogenesis and apoptosis in mice granulosa cells induced by high glucose concentration.
Down Syndrome
Betaine-homocysteine methyltransferase 742G>A polymorphism and risk of down syndrome offspring in a Brazilian population.
Endometriosis
Polymorphic variants of folate and choline metabolism genes and the risk of endometriosis-associated infertility.
Fatty Liver
Choline deprivation induces hyperhomocysteinemia in rats fed low methionine diets.
Fatty Liver
Deletion of betaine-homocysteine S-methyltransferase in mice perturbs choline and 1-carbon metabolism, resulting in fatty liver and hepatocellular carcinomas.
Fatty Liver
Dynamic regulation of hepatic lipid droplet properties by diet.
Fatty Liver
Effect of transgenic extrahepatic expression of betaine-homocysteine methyltransferase on alcohol or homocysteine-induced fatty liver.
Fatty Liver
Liver Proteome Analysis in a Rodent Model of Alcoholic Steatosis.
Fatty Liver
Liver proteome analysis in a rodent model of alcoholic steatosis.
Fatty Liver
Liver proteomics in progressive alcoholic steatosis.
Hearing Loss, Noise-Induced
Betaine-homocysteine S-methyltransferase deficiency causes increased susceptibility to noise-induced hearing loss associated to plasma hyperhomocysteinemia.
Hernia, Umbilical
Folate and vitamin B12-related genes and risk for omphalocele.
Homocystinuria
Betaine analogues alter homocysteine metabolism in rats.
Homocystinuria
Mice deficient in cystathionine beta synthase display altered homocysteine remethylation pathway.
Homocystinuria
Taurine alleviates repression of betaine-homocysteine S-methyltransferase and significantly improves the efficacy of long-term betaine treatment in a mouse model of cystathionine ?-synthase-deficient homocystinuria.
Hyperhomocysteinemia
Betaine-homocysteine methyltransferase (BHMT): genomic sequencing and relevance to hyperhomocysteinemia and vascular disease in humans.
Hyperhomocysteinemia
Betaine-homocysteine S-methyltransferase deficiency causes increased susceptibility to noise-induced hearing loss associated to plasma hyperhomocysteinemia.
Hyperhomocysteinemia
Dietary Egg Protein Prevents Hyperhomocysteinemia via Upregulation of Hepatic Betaine-Homocysteine S-Methyltransferase Activity in Folate-Restricted Rats.
Hyperhomocysteinemia
Effects of betaine supplementation and choline deficiency on folate deficiency-induced hyperhomocysteinemia in rats.
Hyperhomocysteinemia
Effects of hyperhomocysteinemia and betaine-homocysteine S-methyltransferase inhibition on hepatocyte metabolites and the proteome.
Hyperhomocysteinemia
Exercise prevents hyperhomocysteinemia in a dietary folate-restricted mouse model.
Hyperhomocysteinemia
Hyperhomocysteinemia in polycystic ovary syndrome: decreased betaine-homocysteine methyltransferase and cystathionine ?-synthase-mediated homocysteine metabolism.
Hyperhomocysteinemia
Inhibition of betaine-homocysteine S-methyltransferase causes hyperhomocysteinemia in mice.
Hyperhomocysteinemia
Inhibition of betaine-homocysteine S-methyltransferase in rats causes hyperhomocysteinemia and reduces liver cystathionine ?-synthase activity and methylation capacity.
Hyperhomocysteinemia
Suppression effects of betaine-enriched spinach on hyperhomocysteinemia induced by guanidinoacetic acid and choline deficiency in rats.
Hyperhomocysteinemia
Triiodothyronine treatment attenuates the induction of hepatic glycine N-methyltransferase by retinoic acid and elevates plasma homocysteine concentrations in rats.
Hyperthyroidism
The impact of B vitamins on the functioning of methylation cycle in the liver and the kidneys of hyper- and hypothyroid rats.
Hypothyroidism
SULPHUR-CONTAINING AMINO ACIDS METABOLISM IN EXPERIMENTAL HYPER- AND HYPOTHYROIDISM IN RATS.
Hypothyroidism
The impact of B vitamins on the functioning of methylation cycle in the liver and the kidneys of hyper- and hypothyroid rats.
Insulin Resistance
Extra Virgin Olive Oils Increase Hepatic Fat Accumulation and Hepatic Antioxidant Protein Levels in APOE(-/-)() Mice.
Insulin Resistance
The Heme Oxygenase System Selectively Modulates Proteins Implicated in Metabolism, Oxidative Stress and Inflammation in Spontaneously Hypertensive Rats.
Ischemic Stroke
Early-onset ischaemic stroke: analysis of 58 polymorphisms in 17 genes involved in methionine metabolism.
Kidney Failure, Chronic
Betaine analogues alter homocysteine metabolism in rats.
Liver Cirrhosis
Betaine homocysteine methyltransferase: gene cloning and expression analysis in rat liver cirrhosis.
Liver Diseases
Dynamic regulation of hepatic lipid droplet properties by diet.
Lung Injury
Alleviation of paraquat-induced oxidative lung injury by betaine via regulation of sulfur-containing amino acid metabolism despite the lack of betaine-homocysteine methyltransferase (BHMT) in the lung.
Lymphoma, B-Cell
Betaine ameliorates impaired steroidogenesis and apoptosis in mice granulosa cells induced by high glucose concentration.
Meningomyelocele
Neural tube defects and folate pathway genes: family-based association tests of gene-gene and gene-environment interactions.
Neoplasms
A splicing variant leads to complete loss of function of betaine-homocysteine methyltransferase (BHMT) gene in hepatocellular carcinoma.
Neoplasms
Betaine ameliorates impaired steroidogenesis and apoptosis in mice granulosa cells induced by high glucose concentration.
Neoplasms
Down-regulation of metabolic proteins in hepatocellular carcinoma with portal vein thrombosis.
Neoplasms
Proteomic differences between hepatocellular carcinoma and non-tumorous liver tissue investigated by a combined 2D-DIGE and label-free quantitative proteomics study.
Obesity
Are genetic variants of the methyl group metabolism enzymes risk factors predisposing to obesity?
Polycystic Ovary Syndrome
Hyperhomocysteinemia in polycystic ovary syndrome: decreased betaine-homocysteine methyltransferase and cystathionine ?-synthase-mediated homocysteine metabolism.
Spinal Dysraphism
Are the betaine-homocysteine methyltransferase (BHMT and BHMT2) genes risk factors for spina bifida and orofacial clefts?
Spinal Dysraphism
Common variant in betaine-homocysteine methyltransferase (BHMT) and risk for spina bifida.
Starvation
Degradation of glycinebetaine by betaine-homocysteine methyltransferase in Aphanothece halophytica: effect of salt downshock and starvation.
Stroke
Early-onset ischaemic stroke: analysis of 58 polymorphisms in 17 genes involved in methionine metabolism.
Thrombosis
Betaine:homocysteine methyltransferase--a new assay for the liver enzyme and its absence from human skin fibroblasts and peripheral blood lymphocytes.
Thrombosis
Down-regulation of metabolic proteins in hepatocellular carcinoma with portal vein thrombosis.
Vascular Diseases
Betaine-homocysteine methyltransferase (BHMT): genomic sequencing and relevance to hyperhomocysteinemia and vascular disease in humans.
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0.000093
5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0011
5-[3-(R,S)-3-amino-3-(hydroxyphosphorylpropyl)sulfanyl]-3,3-dimethylpentanoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.005
5-[3-(R,S)-3-amino-3-(hydroxyphosphorylpropyl)sulfanyl]pentanoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000096
(R,S)-2-amino-4-(2-carboxymethylsulfanyl-ethylsulfanyl)-butyric acid
Homo sapiens
-
-
0.0057
(R,S)-2-amino-4-(4-phosphono-butylsulfanyl)-butyric acid
Homo sapiens
-
-
0.007
(R,S)-4-(3-amino-3-carboxy-propylsulfanyl)-benzoic acid
Homo sapiens
-
-
0.000087
(R,S)-5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid
Homo sapiens
-
-
0.005
(R,S)-5-(3-amino-3-carboxy-propylsulfinyl)-pentanoic acid
Homo sapiens
-
-
0.0002
(R,S)-6-(3-amino-3-carboxy-propylsulfanyl)-hexanoic acid
Homo sapiens
-
-
0.00326
(RS)-2-amino-4-[(2-carboxyethylthio)methylthio]butanoic acid
Homo sapiens
-
in 50 mM potassium phosphate buffer, at pH 7.5, at 37°C
0.0025
(RS)-2-amino-4-[2-[(carboxymethyl)(methyl)amino]ethylthio]-butanoic acid
Homo sapiens
-
in 50 mM potassium phosphate buffer, at pH 7.5, at 37°C
0.000649
(RS)-5-(3-amino-3-carboxypropylselanyl)pentanoic acid
Homo sapiens
-
in 50 mM potassium phosphate buffer, at pH 7.5, at 37°C
0.000084
(RS)-5-(3-amino-3-carboxypropylthio)-3,3-dimethylpentanoic acid
Homo sapiens
-
in 50 mM potassium phosphate buffer, at pH 7.5, at 37°C
0.000139
(RS)-5-(3-amino-3-carboxypropylthio)-3-methylpentanoic acid
Homo sapiens
-
in 50 mM potassium phosphate buffer, at pH 7.5, at 37°C
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D26A
almost 3fold decrease in stimulation by K+
DELTA325-406
truncation mutatnt does not express well in Escherichia coli and is inactive
DELTA371-406
truncation mutant does not express well in Escherichia coli and is inactive
E159A
complete loss of activity
E159Q
complete loss of activity
E266A
near-normal catalytic activity
G27S
no stimulation by K+
G28S
very small decrease in stimulation by K+
H338A
normal or near-normal ability to bind zinc, 10% of the wild-type activity
N364A
normal or near-normal ability to bind zinc, near-normal catalytic activity
P362A
normal or near-normal ability to bind zinc, near-normal catalytic activity
P365A
normal or near-normal ability to bind zinc, near-normal catalytic activity
R346A
normal or near-normal ability to bind zinc, negligible activity, elution as dimer, aberrant crosslinking properties
R361A
normal or near-normal ability to bind zinc, near-normal catalytic activity
W352A
negligible activity, elution as dimer, aberrant crosslinking properties
Y363A
normal or near-normal ability to bind zinc, near-normal catalytic activity
A66V
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups
Arg16Cys
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups, Km (mM): 0.0139 (betaine), 0.0076 (L-homocysteine)
Arg239Gln
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups, Km (mM): 0.012 (betaine), 0.0158 (L-homocysteine)
C104A
-
site-directed mutagenesis is used to investigate whether the loss of the DMSA-Asp activity of BHMT when in the absence of a reducing agent is due to the oxidation of an essential thiol within the protein. By individual mutation of each of the five Cys residues not involved in Zn binding to Ala, it is shown that the resulting mutants are as active as wild-type enzyme when in the presence of beta-mercaptoethanol with the DMSA-Asp assay
C131A
-
site-directed mutagenesis is used to investigate whether the loss of the DMSA-Asp activity of BHMT when in the absence of a reducing agent is due to the oxidation of an essential thiol within the protein. By individual mutation of each of the five Cys residues not involved in Zn binding to Ala, it is shown that the resulting mutants are as active as wild-type enzyme when in the presence of beta-mercaptoethanol with the DMSA-Asp assay
C186A
-
site-directed mutagenesis is used to investigate whether the loss of the DMSA-Asp activity of BHMT when in the absence of a reducing agent is due to the oxidation of an essential thiol within the protein. By individual mutation of each of the five Cys residues not involved in Zn binding to Ala, it is shown that the resulting mutants are as active as wild-type enzyme when in the presence of beta-mercaptoethanol with the DMSA-Asp assay
C201A
-
site-directed mutagenesis is used to investigate whether the loss of the DMSA-Asp activity of BHMT when in the absence of a reducing agent is due to the oxidation of an essential thiol within the protein. By individual mutation of each of the five Cys residues not involved in Zn binding to Ala, it is shown that the resulting mutants are as active as wild-type enzyme when in the presence of beta-mercaptoethanol with the DMSA-Asp assay
C217A
-
the mutation reduces zinc binding by 95% while abrogating catalytic activity, the mutation has no effect on the fold increase of GST-BHMT proteolytic fragment in the absence of nutrients
C256A
-
site-directed mutagenesis is used to investigate whether the loss of the DMSA-Asp activity of BHMT when in the absence of a reducing agent is due to the oxidation of an essential thiol within the protein. By individual mutation of each of the five Cys residues not involved in Zn binding to Ala, it is shown that the resulting mutants are as active as wild-type enzyme when in the presence of beta-mercaptoethanol with the DMSA-Asp assay
Cys217Ala
-
complete loss of activity, reduction in zinc binding, identification of zinc binding motif
Cys299Ala
-
complete loss of activity, reduction in zinc binding, identification of zinc binding motif
Cys300Ala
-
complete loss of activity, reduction in zinc binding, identification of zinc binding motif
G199S
-
in vascular patients with hyperhomocysteinemia
G742A
-
in an ongoing, multicenter, case-control study including women with a clinical diagnosis of abruption an association between the homozygous mutant form of BHMT (742G to A) polymorphism and an increased risk for placental abruption is shown
Gly199Ser
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups, Km (mM): 0.0139 (betaine), 0.0206 (L-homocysteine)
Pro197Ser
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups, Km (mM): 0.0213 (betaine), 0.0216 (L-homocysteine)
R239Q
-
no significant association with the severity and extent of hyperhomocysteinemia
T218M
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups
V155F
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups
V237M
-
nonsynonymous SNP identified using 240 DNA samples from four ethnic groups
W352A
-
the mutation disrupts stable BHMT multimerization, the mutant ablates catalytic activity
additional information
both BHMT transfectants of HepG2 cells and primary mouse hepatocytes with suppressed BHMT are generated. Expression of BHMT in HepG2 cells ameliorates the homocysteine metabolism and inhibits homocysteine-induced glucose-regulated protein 78 (GRP78) and C/EBP-homologous protein (CHOP) and homocysteine-induced cell death. A betaine treatment protects primary mouse hepatocytes from a homocysteine-induced increase in GRP78 and cell death. Homocysteine induces greater CHOP expression (2.7fold) in BHMT small interfering RNA -transfected cells than in a control (1.9fold). Homocysteine-induced cell death is increased by 40% in the siRNA-treated cells in comparison with the control. Apolipoprotein B (apoB) expression is higher and triglycerides and cholesterol is lower in HepG2 expressing BHMT. In primary mouse hepatocytes, homocysteine induces the accumulation of triglycerides and cholesterol, which is reduced in the presence of betaine
additional information
-
random mutagenesis of zinc binding motif, Gly214 is essential
additional information
deletion mutants ranging from -2698 to +33, construct -347/+33 has maximal promoter activity, inhibition in promoter activity by S-adenosylmethionine or 5'-methylthioadenosine most pronounced within this construct, cycloleucine treatment increases the reporter activity driven by the BHMT promoter construct -347/+33 but does not block the ability of 5'-methylthioadenosine to inhibit the BHMT promoter activity and blocks the conversion of 5'-methylthioadenosine into S-adenosylmethionine
additional information
-
deletion mutants ranging from -2698 to +33, construct -347/+33 has maximal promoter activity, inhibition in promoter activity by S-adenosylmethionine or 5'-methylthioadenosine most pronounced within this construct, cycloleucine treatment increases the reporter activity driven by the BHMT promoter construct -347/+33 but does not block the ability of 5'-methylthioadenosine to inhibit the BHMT promoter activity and blocks the conversion of 5'-methylthioadenosine into S-adenosylmethionine
additional information
-
betaine-homocysteine methyltransferase transgenic (Tg) mice are generated. BHMT transgenic mice are resistant to alcohol or high methionine low folate diet-induced hyperhomocysteinemia and liver steatosis indicating that peripheral metabolism of homocysteine protects the liver without a direct effect of BHMT in the liver
additional information
S-adenosylmethionine and 5-methylthioadenosine treatment of HepG2 cells result in a dose- and time-dependent decrease in BHMT mRNA levels, which parallels their effects on the BHMT promoter activity. Maximal suppression is observed with BHMT promoter construct -347/+33, containing a number of NF-kappaB binding sites. S-adenosylmethionine and 5-methylthioadenosine treatment increases NF-kappaB nuclear binding and NF-kappaB-driven luciferasece activities, and increases nuclear binding activity of multiple histone deacetylase co-repressors to the NF-kappaB sites. Overexpression of p50 and p65 decreases BHMT promoter activity, while blocking NF-kappaB activation increases BHMT expression and promoter activity, and prevents S-adenosylmethionine but not 5-methylthioadenosines ability to inhibit BHMT expression
additional information
-
S-adenosylmethionine and 5-methylthioadenosine treatment of HepG2 cells result in a dose- and time-dependent decrease in BHMT mRNA levels, which parallels their effects on the BHMT promoter activity. Maximal suppression is observed with BHMT promoter construct -347/+33, containing a number of NF-kappaB binding sites. S-adenosylmethionine and 5-methylthioadenosine treatment increases NF-kappaB nuclear binding and NF-kappaB-driven luciferasece activities, and increases nuclear binding activity of multiple histone deacetylase co-repressors to the NF-kappaB sites. Overexpression of p50 and p65 decreases BHMT promoter activity, while blocking NF-kappaB activation increases BHMT expression and promoter activity, and prevents S-adenosylmethionine but not 5-methylthioadenosines ability to inhibit BHMT expression
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Homo sapiens, Mus musculus
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Homo sapiens (Q93088), Homo sapiens
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