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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Methionine adenosyltransferase I, alpha

AdoMet, S-adenosylmethionine synthetase, MAT1A, Methionine adenosyltransferase, SAMS, AdoMet synthetase
enzyme that catalyzes the formation of S-adenosylmethionine [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: CAN, ACID, STEP, V1a, HAD
Papers using AdoMet antibodies
Chemo-enzymatic detection of protein isoaspartate using protein isoaspartate methyltransferase and hydrazine trapping
Uversky Vladimir N., In PLoS ONE, 2007
... H] AdoMet) was purchased from PerkinElmer Life Sciences ...
Maturation of [NiFe]-hydrogenases in Escherichia coli
Thauer Rudolf K. et al., In Archaea, 2006
... Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase ...
Repair of Isoaspartate Formation Modulates the Interaction of Deamidated 4E-BP2 with mTORC1 in Brain*
Sonenberg Nahum et al., In The Journal of Biological Chemistry, 2004
... AdoMet (81.9 Ci/mmol) and unlabeled AdoMet were purchased from PerkinElmer Life Sciences and Sigma, ...
Crystallography & NMR system: A new software suite for macromolecular structure determination
Lin Hening et al., In Nature, 1997
... Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase ...
Papers on AdoMet
Statin intolerance.
März et al., Augsburg, Germany. In Curr Opin Lipidol, Dec 2015
This review article summarizes the current concepts of the diagnosis and clinical work-up of patients with statin-associated muscle symptoms (SAMS).
The Mechanisms of Generation, Recognition, and Erasure of DNA 5-Methylcytosine and Thymine Oxidations.
Cheng et al., Atlanta, United States. In J Biol Chem, Sep 2015
An array of AdoMet-dependent methyltransferases, Fe(II)- and α-ketoglutarate-dependent dioxygenases, base excision glycosylases, and sequence-specific transcription factors is responsible for changing, maintaining, and interpreting the modification status of specific regions of chromatin.
Statin-associated muscle symptoms: impact on statin therapy-European Atherosclerosis Society Consensus Panel Statement on Assessment, Aetiology and Management.
European Atherosclerosis Society Consensus Panel et al., Hartford, United States. In Eur Heart J, Jun 2015
Statin-associated muscle symptoms (SAMS) are one of the principal reasons for statin non-adherence and/or discontinuation, contributing to adverse cardiovascular outcomes.
SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes.
Drennan et al., Cambridge, United States. In J Biol Chem, Mar 2015
S-Adenosylmethionine (SAM, also known as AdoMet) radical enzymes use SAM and a [4Fe-4S] cluster to catalyze a diverse array of reactions.
Mudd's disease (MAT I/III deficiency): a survey of data for MAT1A homozygotes and compound heterozygotes.
Blom et al., Taipei, Taiwan. In Orphanet J Rare Dis, 2014
MAT1A encodes the subunit that forms two methionine adenosyltransferase isoenzymes, tetrameric MAT I and dimeric MAT III, that catalyze the conversion of methionine and ATP to S-adenosylmethionine (AdoMet).
[Relationship between Arsenic (+3 Oxidation State) Methyltransferase Genetic Polymorphisms and Methylation Capacity of Inorganic Arsenic].
Iwata et al., Japan. In Nihon Eiseigaku Zasshi, 2014
Genetic polymorphisms such as single nucleotide polymorphisms (SNPs) in arsenic (+3 oxidation state) methyltransferase (AS3MT), which can methylate arsenic compounds using S-adenosyl-l-methionine (AdoMet), have been reported to modify arsenic methylation.
S-adenosylmethionine in liver health, injury, and cancer.
Mato et al., Los Angeles, United States. In Physiol Rev, 2012
Biosynthesis of AdoMet requires the enzyme methionine adenosyltransferase (MAT).
Role of transcriptional and posttranscriptional regulation of methionine adenosyltransferases in liver cancer progression.
Pascale et al., Sassari, Italy. In Hepatology, 2012
we found for the first time a post-transcriptional regulation of MAT1A and MAT2A by AUF1 and HuR in hepatocellular carcinoma.
Proteomic analysis of human hepatoma cells expressing methionine adenosyltransferase I/III: Characterization of DDX3X as a target of S-adenosylmethionine.
Corrales et al., Pamplona, Spain. In J Proteomics, 2012
Human Dead-box protein 3 (DDX3X), a RNA helicase regulating RNA splicing, export, transcription and translation was down-regulated upon MAT1A expression.
Radical-mediated enzymatic methylation: a tale of two SAMS.
Liu et al., Urbana, United States. In Acc Chem Res, 2012
Methylation is an essential and ubiquitous reaction that plays an important role in a wide range of biological processes.
Inhibition of human methionine adenosyltransferase 1A transcription by coding region methylation.
Lu et al., Los Angeles, United States. In J Cell Physiol, 2012
Methylation of the MAT1A coding region can inhibit gene transcription. This represents a key mechanism for decreased MAT1A expression in hepatocellular carcinoma.
Methionine adenosyltransferase 1A gene deletion disrupts hepatic very low-density lipoprotein assembly in mice.
Aspichueta et al., Bilbao, Spain. In Hepatology, 2011
MAT1A is required for normal VLDL assembly and plasma lipid homeostasis in mice. Impaired VLDL synthesis, mainly due to SAMe deficiency, contributes to NAFLD development in MAT1A-KO mice.
Methionine adenosyltransferase 2A/2B and methylation: gene sequence variation and functional genomics.
Weinshilboum et al., Rochester, United States. In Drug Metab Dispos, 2011
Coexpression of MAT2A and MAT2B in COS-1 cells resulted in significantly increased MAT enzyme activity.
7 Non-histone protein lysine methyltransferases: Structure and catalytic roles.
Houtz et al., Lexington, United States. In Enzymes, 2005
Other than the obvious commonality in the AdoMet substrate cofactor and methyl group transfer, these enzymes do not have common structural features, polypeptide substrate specificity, or protein sequence.
6 Structure of SET domain protein lysine methyltransferases.
Wilson et al., London, United Kingdom. In Enzymes, 2005
The structure of the SET domain is such that peptide substrates bind on one surface, whereas the AdoMet cofactor binds on the opposite side of the domain.
16 Inhibition of mammalian protein methyltransferases by 5'-methylthioadenosine (MTA): A mechanism of action of dietary same?
Clarke, Los Angeles, United States. In Enzymes, 2005
This chapter reviews recent evidence that points to an important role for MTA as an intermediary in the beneficial pharmaceutical action of orally ingested S-adenosyl-l-methionine (AdoMet, SAMe).
13 Protein L-isoaspartyl, D-aspartyl O-methyltransferases: Catalysts for protein repair.
O'Connor, Boston, United States. In Enzymes, 2005
Structurally, PIMTs are members of the class I family of AdoMet-dependent methyltransferases.
Structure and catalytic mechanism of the human histone methyltransferase SET7/9.
Gamblin et al., London, United Kingdom. In Nature, 2003
The target lysine accesses the active site of the enzyme and the S-adenosyl-l-methionine (AdoMet) cofactor by inserting its side chain into a narrow channel that runs through the enzyme, connecting the two surfaces.
Crystal structure and functional analysis of the histone methyltransferase SET7/9.
Xiao et al., London, United Kingdom. In Cell, 2002
Furthermore, we show how the cofactor AdoMet binds to this domain and present biochemical data supporting the role of invariant residues in catalysis, binding of AdoMet, and interactions with the peptide substrate.
Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase.
Cheng et al., Atlanta, United States. In Cell, 2002
AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression.
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