Search results for "GNMT"

showing 4 items of 4 documents

Insights on the origin of catalysis on glycine N-methyltransferase from computational modeling.

2018

The origin of enzyme catalysis remains a question of debate despite much intense study. We report a QM/MM theoretical study of the SN2 methyl transfer reaction catalyzed by a glycine N-methyltransferase (GNMT) and three mutants to test whether recent experimental observations of rate-constant reductions and variations in inverse secondary α-3H kinetic isotope effects (KIEs) should be attributed to changes in the methyl donor−acceptor distance (DAD): is catalysis due to a compression effect? Semiempirical (AM1) and DFT (M06-2X) methods were used to describe the QM subset of atoms, while OPLS-AA and TIP3P classical force fields were used for the protein and water molecules, respectively. The …

Chemistry(all)Static ElectricityMolecular ConformationGlycine N-Methyltransferase010402 general chemistry01 natural sciencesenzyme catalysisQM/MMBiochemistryArticleCatalysisEnzyme catalysisCatalysisColloid and Surface ChemistryComputational chemistryKinetic isotope effectMolecule/dk/atira/pure/subjectarea/asjc/1600/dk/atira/pure/subjectarea/asjc/1300/1303/dk/atira/pure/subjectarea/asjc/1500/1505biology010405 organic chemistryChemistryActive siteGeneral ChemistryGlycine N-methyltransferase0104 chemical sciencesKineticsGNMTBiocatalysisbiology.proteinQuantum TheorySN2 reaction/dk/atira/pure/subjectarea/asjc/1500/1503
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Fatty Liver and Fibrosis in Glycine N-Methyltransferase Knockout Mice Is Prevented by Nicotinamide

2010

Deletion of glycine N-methyltransferase (GNMT), the main gene involved in liver S-adenosylmethionine (SAM) catabolism, leads to the hepatic accumulation of this molecule and the development of fatty liver and fibrosis in mice. To demonstrate that the excess of hepatic SAM is the main agent contributing to liver disease in GNMT knockout (KO) mice, we treated 1.5-month-old GNMT-KO mice for 6 weeks with nicotinamide (NAM), a substrate of the enzyme NAM N-methyltransferase. NAM administration markedly reduced hepatic SAM content, prevented DNA hypermethylation, and normalized the expression of critical genes involved in fatty acid metabolism, oxidative stress, inflammation, cell proliferation, …

Liver CirrhosisNiacinamidemedicine.medical_specialtyPathologyS-AdenosylmethionineCirrhosisGene ExpressionGlycine N-MethyltransferaseBiologyArticleLiver diseasechemistry.chemical_compoundMiceFibrosisInternal medicinemedicineAnimalsRas signalingMice KnockoutDNA methylationHepatologyFatty acid metabolismFatty livermedicine.diseaseGlycine N-methyltransferaseFatty LiverEndocrinologyJAK/STAT signalingchemistryGNMThepatocytesHepatic fibrosisGene Deletion
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Reduced mRNA abundance of the main enzymes involved in methionine metabolism in human liver cirrhosis and hepatocellular carcinoma

2000

Abstract Background/Aims: It has been known for at least 50 years that alterations in methionine metabolism occur in human liver cirrhosis. However, the molecular basis of this alteration is not completely understood. In order to gain more insight into the mechanisms behind this condition, mRNA levels of methionine adenosyltransferase ( MAT1A ), glycine methyltransferase ( GNMT ), methionine synthase ( MS ), betaine homocysteine methyltransferase ( BHMT ) and cystathionine β-synthase ( CBS ) were examined in 26 cirrhotic livers, five hepatocellular carcinoma (HCC) tissues and ten control livers. Methods: The expression of the above-mentioned genes was determined by quantitative RT-PCR analy…

Liver Cirrhosismedicine.medical_specialtyCarcinoma HepatocellularMethyltransferaseBetaine—homocysteine S-methyltransferaseMethylationHepatocarcinemachemistry.chemical_compoundMethionineInternal medicinemedicineHumansRNA MessengerMethionine synthasePromoter Regions GeneticDNA methylationMethionineHepatologybiologyLiver NeoplasmsMethionine Adenosyltransferasemedicine.diseaseCystathionine beta synthaseEnzymesIsoenzymesEndocrinologyCirrhosisLiverchemistryMethionine AdenosyltransferaseGNMTbiology.proteinHypermethioninemia
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Catalysis in glycine N-methyltransferase: testing the electrostatic stabilization and compression hypothesis.

2006

Glycine N-methyltransferase (GNMT) is an S-adenosyl-l-methionine dependent enzyme that catalyzes glycine transformation to sarcosine. Here, we present a hybrid quantum mechanics/molecular mechanics (QM/MM) computational study of the reaction compared to the counterpart process in water. The process takes place through an SN2 mechanism in both media with a transition state in which the transferring methyl group is placed in between the donor (SAM) and the acceptor (the amine group of glycine). Comparative analysis of structural, electrostatic, and electronic characteristics of the in-solution and enzymatic transition states allows us to get a deeper insight into the origins of the enzyme's c…

S-AdenosylmethionineSarcosinebiologyChemistryStereochemistryHydrogen bondStatic ElectricityActive siteGlycine N-MethyltransferaseBiochemistryAcceptorGlycine N-methyltransferaseTransition stateCatalysischemistry.chemical_compoundModels ChemicalGNMTbiology.proteinMethyl groupBiochemistry
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