1972
DOI: 10.1016/s0021-9258(19)45067-9
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Competing Methyltransferase Systems

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Cited by 262 publications
(32 citation statements)
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“…It is likely that SAHH activity would be elevated in WFX hens, because PEMT generates a large volume of SAH [ 30 , 63 , 64 ]. SAH inhibits methyltransferases such as PEMT [ 30 , 36 ]; therefore, SAHH hyperactivation would complement PEMT hyperactivation. Adenosine was elevated 4-fold on average in WFX hens, while dAMP (a molecule that is readily synthesized from adenosine) was slightly elevated in WFX hens ( Figure 4 D).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…It is likely that SAHH activity would be elevated in WFX hens, because PEMT generates a large volume of SAH [ 30 , 63 , 64 ]. SAH inhibits methyltransferases such as PEMT [ 30 , 36 ]; therefore, SAHH hyperactivation would complement PEMT hyperactivation. Adenosine was elevated 4-fold on average in WFX hens, while dAMP (a molecule that is readily synthesized from adenosine) was slightly elevated in WFX hens ( Figure 4 D).…”
Section: Resultsmentioning
confidence: 99%
“…When evaluating this model, notice the “carbon donor” molecules (highlighted in red) that feed single-carbon units into one-carbon metabolism. For an in-depth look at one-carbon metabolism, we refer the reader to our expanded model shown in Supplementary Materials, Figure S1 [ 13 , 17 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 ].…”
Section: Introductionmentioning
confidence: 99%
“…Although glycine N-methyltransferase represents only one of numerous methyl-transferring enzymes, its capacity to utilize S-adenosylmethionine in liver is approximately the same as the synthesizing capacity of methionine adenosyltransferase (Kerr, 1974). It is noteworthy that the concentrations of glycine (1 mM) and S-adenosylmethionine (50M) in the liver correspond to the respective Km values of glycine N-methyltransferase (Kerr, 1972(Kerr, , 1974, whereas the methionine concentration (40-80,M) is significantly lower than the corresponding Km value of methionine adenosyltransferase (for references see Eloranta et al, 1976b). Thus it is obvious that when the concentration of methionine is increased, the rate of S-adenosylmethionine synthesis in liver is increased more than its utilization by glycine N-methyltransferase.…”
Section: Discussionmentioning
confidence: 99%
“…Competing methyltransferases may be involved in the control of its utilization. At least in the liver, glycine N-methyltransferase is such an enzyme, owing to its high activity and fairly good resistance to the inhibitory effect of S-adenosylhomocysteine (Kerr, 1972). The accumulation of S-adenosylmethionine does not seem to cause any significant changes in the synthesis and accumulation of polyamines.…”
Section: Discussionmentioning
confidence: 99%
“…whereas GNMT is almost insensitive due to its high K i AdoHcy (138,171). An additional mechanism of control for GNMT is provided by MTHF inhibition (384), allowing preservation of AdoMet when its levels are low and remethylation through MTR is needed.…”
Section: Selected Examples Of Genes and Enzymes Of Transmethylationmentioning
confidence: 99%