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L-homocysteine + betaine
L-methionine + dimethylglycine
L-homocysteine + betaine
dimethylglycine + L-methionine
-
-
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
L-homocysteine + betaine
L-methionine + dimethylglycine
-
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
-
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
reduced BHMT activity in cirrhotic livers may explain the elevated plasma homocysteine levels in cirrhosis
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
folate-independent remethylation of homocysteine
-
-
?
L-homocysteine + betaine
L-methionine + dimethylglycine
-
this reaction processes 25% of the cellular L-homocysteine in an in vitro model
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
-
-
?
N,N,N-trimethylglycine + L-homocysteine
N,N-dimethylglycine + L-methionine
-
i.e. betaine, involved in betaine metabolism
-
-
?
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actinomycin D
leads to a decay of Bhmt mRNA, irrespective of the ambient osmolarity, at 120 min after addition, Bhmt mRNA levels are significantly decreased under hyperosmotic conditions, compared with the Bhmt mRNA levels found under the respective normo- or hypoosmotic condition
Pinanyl N,N,N-trimethylaminomethane boronate
-
substrate analogue
S-adenosyl-L-ethionine
-
irreversible, S-adenosyl-L-homocysteine and L-homocysteine prevent, but not DL-homocysteine, GSH, DTT or L-cysteine
S-adenosyl-L-homocysteine
-
non-linear/competitive to homocysteine, mixed/non-competitive to betaine
S-adenosyl-L-methionine
-
irreversible, S-adenosyl-L-homocysteine and L-homocysteine prevent, not DL-homocysteine, GSH, DTT or L-cysteine
additional information
-
hyperosmotic NaCl, hyperosmotic raffinose but not hyperosmotic urea suppresses Bhmt mRNA expression, suggesting that cell shrinkage rather than increased ionic strength or hyperosmolarity per se is the trigger, osmosensitivity of Bhmt mRNA expression is impaired by inhibitors of tyrosine kinases and cyclic nucleotide-dependent kinases
-
additional information
hyperosmotic NaCl, hyperosmotic raffinose but not hyperosmotic urea suppresses Bhmt mRNA expression, suggesting that cell shrinkage rather than increased ionic strength or hyperosmolarity per se is the trigger, osmosensitivity of Bhmt mRNA expression is impaired by inhibitors of tyrosine kinases and cyclic nucleotide-dependent kinases
-
additional information
-
product inhibition
-
additional information
-
product inhibition
-
additional information
-
not inhibitory: taurine, cysteic acid, cysteine sulfinate, sulfate, glycine, L-serine, L-threonine
-
additional information
-
insulin decreases the abundance of BHMT mRNA and the rate of de novo mRNA transcription of the gene in H4IIE cells, plays a direct role in the regulation of BHMT transcription
-
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A119G
1.9fold reduced turnover-number for betaine and L-homocysteine, 1.6fold reduced KM-value for L-homocysteine, 1.1fold decrease in Km-value for betaine
C186A
1.8fold reduced turnover-number for betaine and L-homocysteine, 4.3fold reduced KM-value for L-homocysteine, 1.8fold increase in Km-value for betaine
C186S
2.3fold reduced turnover-number for betaine and L-homocysteine, 1.4fold reduced KM-value for L-homocysteine, 111.6fold decrease in Km-value for betaine
D26A
2.7fold reduced turnover-number for betaine and L-homocysteine, 1.7fold reduced KM-value for L-homocysteine, 3.5fold increase in Km-value for betaine
D26I
67fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 6.5fold lower than the wild-type value
E159G
60fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 61.2fold lower than the wild-type value
E159K
170fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 169.7fold lower than the wild-type value
E21A
2.3fold reduced turnover-number for betaine and L-homocysteine, 6fold reduced KM-value for L-homocysteine, 2.4fold reduced Km-value for betaine
E21K
1.6fold reduced turnover-number for betaine and L-homocysteine, 1.4fold reduced KM-value for L-homocysteine, 1.7fold reduced Km-value for betaine
F74A
1.9fold reduced turnover-number for betaine and L-homocysteine, 1.9fold reduced KM-value for L-homocysteine, 2.9fold increase in Km-value for betaine
T184G
2.4fold reduced turnover-number for betaine and L-homocysteine, 3.19fold reduced KM-value for L-homocysteine, 1.6fold increase in Km-value for betaine
T73G
3.1fold reduced turnover-number for betaine and L-homocysteine, 2.2fold reduced KM-value for L-homocysteine, 1.3fold reduced Km-value for betaine
Y77A
14fold reduced turnover-number for betaine and L-homocysteine, maximal velocity is 13.7fold lower than the wild-type value
R346A
-
shows alterations in the association state
W352A
-
shows alterations in the association state
Y363A
-
shows alterations in the association state
additional information
-
changes at positions E159 and Y77 show the largest decreases in activity, but D26 and F74 seem to have a role in betaine binding, whereas E21 and C186 also influence L-homocysteine binding
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Finkelstein, J.D.; Harris, B.J.; Kyle, W.E.
Methionine metabolism in mammals: kinetic study of betaine-homocysteine methyltransferase
Arch. Biochem. Biophys.
153
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1972
Rattus norvegicus
brenda
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292
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Rattus norvegicus, Rattus norvegicus Sprague-Dawley
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Finkelstein, J.D.; Martin, J.J.
Inactivation of betaine-homocysteine methyltransferase by adenosylmethionine and adenosylethionine
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118
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Rattus norvegicus
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Methionine metabolism in mammals: regulatory effects of S-adenosylhomocysteine
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165
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Rattus norvegicus
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Crystallization and preliminary x-ray study of recombinant betaine-homocysteine S-methyltransferase from rat liver
Acta Crystallogr. Sect. D
58
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2002
Rattus norvegicus
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Delgado-Reyes, C.V.; Wallig, M.A.; Garrow, T.A.
Immunohistochemical detection of betaine-homocysteine S-methyltransferase in human, pig, and rat liver and kidney
Arch. Biochem. Biophys.
393
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Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Gonzalez, B.; Campillo, N.; Garrido, F.; Gasset, M.; Sanz-Aparicio, J.; Pajares, M.A.
Active-site-mutagenesis study of rat liver betaine-homocysteine S-methyltransferase
Biochem. J.
370
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Rattus norvegicus (O09171)
brenda
Garrido, F.; Gasset, M.; Sanz-Aparicio, J.; Alfonso, C.; Pajares, M.A.
Rat liver betaine homocysteine S-methyltransferase equilibrium unfolding: insights into intermediate structure through tryptophan substitutions
Biochem. J.
391
589-599
2005
Rattus norvegicus
brenda
Forestier, M.; Banninger, R.; Reichen, J.; Solioz, M.
Betaine homocysteine methyltransferase: gene cloning and expression analysis in rat liver cirrhosis
Biochim. Biophys. Acta
1638
29-34
2003
Rattus norvegicus
brenda
Gonzalez, B.; Pajares, M.A.; Martinez-Ripoll, M.; Blundell, T.L.; Sanz-Aparicio, J.
Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding
J. Mol. Biol.
338
771-782
2004
Rattus norvegicus (O09171)
brenda
Ratnam, S.; Wijekoon, E.P.; Hall, B.; Garrow, T.A.; Brosnan, M.E.; Brosnan, J.T.
Effects of diabetes and insulin on betaine-homocysteine S-methyltransferase expression in rat liver
Am. J. Physiol. Endocrinol. Metab.
290
E933-E939
2006
Rattus norvegicus
brenda
Nieman, K.M.; Hartz, C.S.; Szegedi, S.S.; Garrow, T.A.; Sparks, J.D.; Schalinske, K.L.
Folate status modulates the induction of hepatic glycine N-methyltransferase and homocysteine metabolism in diabetic rats
Am. J. Physiol. Endocrinol. Metab.
291
E1235-E1242
2006
Rattus norvegicus
brenda
Schaefer, C.; Hoffmann, L.; Heldt, K.; Lornejad-Schaefer, M.R.; Brauers, G.; Gehrmann, T.; Garrow, T.A.; Haeussinger, D.; Mayatepek, E.; Schwahn, B.C.; Schliess, F.
Osmotic regulation of betaine homocysteine-S-methyltransferase expression in H4IIE rat hepatoma cells
Am. J. Physiol. Gastrointest. Liver Physiol.
292
G1089-G1098
2007
Mus musculus, Rattus norvegicus, Rattus norvegicus (O09171)
brenda
Sparks, J.D.; Collins, H.L.; Chirieac, D.V.; Cianci, J.; Jokinen, J.; Sowden, M.P.; Galloway, C.A.; Sparks, C.E.
Hepatic very-low-density lipoprotein and apolipoprotein B production are increased following in vivo induction of betaine-homocysteine S-methyltransferase
Biochem. J.
395
363-371
2006
Rattus norvegicus
brenda
Pajares, M.A.; Perez-Sala, D.
Betaine homocysteine S-methyltransferase: just a regulator of homocysteine metabolism?
Cell. Mol. Life Sci.
63
2792-2803
2006
Cavia porcellus, Homo sapiens, Macaca mulatta, Mesocricetus auratus, Mus musculus, Mus musculus C57/BL6J, Ovis aries, Rattus norvegicus, Sus scrofa
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
Kharbanda, K.K.; Vigneswara, V.; McVicker, B.L.; Newlaczyl, A.U.; Bailey, K.; Tuma, D.; Ray, D.E.; Carter, W.G.
Proteomics reveal a concerted upregulation of methionine metabolic pathway enzymes, and downregulation of carbonic anhydrase-III, in betaine supplemented ethanol-fed rats
Biochem. Biophys. Res. Commun.
381
523-527
2009
Rattus norvegicus
brenda
Ohuchi, S.; Morita, T.; Mori, M.; Sugiyama, K.
Hepatic cystathionine beta-synthase activity does not increase in response to methionine supplementation in rats fed a low casein diet: association with plasma homocysteine concentrations
J. Nutr. Sci. Vitaminol.
55
178-185
2009
Rattus norvegicus
brenda
Fridman, O.; Morales, A.V.; Bortoni, L.E.; Turk-Noceto, P.C.; Prieto, E.A.
Corticoadrenal activity in rat regulates betaine-homocysteine S-methyltransferase expression with opposite effects in liver and kidney
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37
115-123
2012
Rattus norvegicus
brenda
Ahn, C.W.; Jun, D.S.; Na, J.D.; Choi, Y.J.; Kim, Y.C.
Alleviation of hepatic fat accumulation by betaine involves reduction of homocysteine via up-regulation of betaine-homocysteine methyltransferase (BHMT)
Biochem. Biophys. Res. Commun.
477
440-447
2016
Rattus norvegicus
brenda
Saande, C.J.; Pritchard, S.K.; Worrall, D.M.; Snavely, S.E.; Nass, C.A.; Neuman, J.C.; Luchtel, R.A.; Dobiszewski, S.; Miller, J.W.; Vailati-Riboni, M.; Loor, J.J.; Schalinske, K.L.
Dietary egg protein prevents hyperhomocysteinemia via upregulation of hepatic betaine-homocysteine S-methyltransferase activity in folate-restricted rats
J. Nutr.
149
1369-1376
2019
Rattus norvegicus
brenda
Garrido, F.; Pacheco, M.; Vargas-Martinez, R.; Velasco-Garcia, R.; Jorge, I.; Serrano, H.; Portillo, F.; Vazquez, J.; Pajares, M.A.
Identification of hepatic protein-protein interaction targets for betaine homocysteine S-methyltransferase
PLoS ONE
13
e0199472
2018
Rattus norvegicus (O09171), Rattus norvegicus
brenda