メチオニンアデノシルトランスフェラーゼ
WordNet
- a crystalline amino acid containing sulfur; found in most proteins and essential for nutrition
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/10/06 07:58:06」(JST)
[Wiki en表示]
| methionine adenosyltransferase I, alpha |
| Identifiers |
| Symbol |
MAT1A |
| Entrez |
4143 |
| HUGO |
6903 |
| OMIM |
250850 |
| RefSeq |
NM_000429 |
| UniProt |
Q00266 |
| Other data |
| Locus |
Chr. 10 q22 |
| methionine adenosyltransferase II, alpha |
| Identifiers |
| Symbol |
MAT2A |
| Entrez |
4144 |
| HUGO |
6904 |
| OMIM |
601468 |
| RefSeq |
NM_005911 |
| UniProt |
P31153 |
| Other data |
| Locus |
Chr. 2 p11.2 |
| methionine adenosyltransferase II, beta |
| Identifiers |
| Symbol |
MAT2B |
| Entrez |
27430 |
| HUGO |
6905 |
| OMIM |
605527 |
| RefSeq |
NM_013283 |
| UniProt |
Q9NZL9 |
| Other data |
| Locus |
Chr. 5 q34-q35 |
Methionine adenosyltransferase is an enzyme which catalyses the synthesis of S-adenosylmethionine (SAM) from methionine and ATP.
Conserved motifs in the 3'UTR of MAT2A mRNA
A computational comparative analysis of vertebrate genome sequences have identified a cluster of 6 conserved hairpin motifs in the 3'UTR of the MAT2A messenger RNA (mRNA) transcript.[1] The predicted hairpins (named A-F) have strong evolutionary conservation and 3 of the predicted RNA structures (hairpins A, C and D) have been confirmed by in-line probing analysis. No structural changes were observed for any of the hairpins in the presence of metabolites SAM, S-adenosylhomocysteine or L-Methioninine. They are proposed to be involved in transcript stability and their functionality is currently under investigation.[1]
References
- ^ a b Parker, B. J.; Moltke, I.; Roth, A.; Washietl, S.; Wen, J.; Kellis, M.; Breaker, R.; Pedersen, J. S. (2011). "New families of human regulatory RNA structures identified by comparative analysis of vertebrate genomes". Genome Research 21 (11): 1929–1943. doi:10.1101/gr.112516.110. PMC 3205577. PMID 21994249. //www.ncbi.nlm.nih.gov/pmc/articles/PMC3205577/. edit
External links
- Methionine+adenosyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 2.5.1.6
|
Transferases: alkyl and aryl (EC 2.5)
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| 2.5.1 |
- Dimethylallyltranstransferase
- Thiaminase I
- Methionine adenosyltransferase
- Riboflavin synthase
- Dihydropteroate synthase
- Spermidine synthase
- Glutathione S-transferase
- Farnesyl-diphosphate farnesyltransferase
- Spermine synthase
- Alkylglycerone phosphate synthase
- Farnesyltransferase
- Geranylgeranyltransferase type 1
- Porphobilinogen deaminase
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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Metabolism: amino acid metabolism · synthesis and catabolism enzymes (essential in CAPS)
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| K→acetyl-CoA |
|
LYSINE→
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- Saccharopine dehydrogenase
- Glutaryl-CoA dehydrogenase
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LEUCINE→
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- Branched chain aminotransferase
- Branched-chain alpha-keto acid dehydrogenase complex
- Isovaleryl coenzyme A dehydrogenase
- Methylcrotonyl-CoA carboxylase
- Methylglutaconyl-CoA hydratase
- 3-hydroxy-3-methylglutaryl-CoA lyase
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|
|
TRYPTOPHAN→
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- Indoleamine 2,3-dioxygenase/Tryptophan 2,3-dioxygenase
- Arylformamidase
- Kynureninase
- 3-hydroxyanthranilate oxidase
- Aminocarboxymuconate-semialdehyde decarboxylase
- Aminomuconate-semialdehyde dehydrogenase
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|
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PHENYLALANINE→tyrosine→
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(see below)
|
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|
| G |
|
G→pyruvate
→citrate
|
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glycine→serine→
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- Serine hydroxymethyltransferase
- Serine dehydratase
- glycine→creatine: Guanidinoacetate N-methyltransferase
- Creatine kinase
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alanine→
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cysteine→
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threonine→
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- L-threonine dehydrogenase
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G→glutamate→
α-ketoglutarate
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HISTIDINE→
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- Histidine ammonia-lyase
- Urocanate hydratase
- Formiminotransferase cyclodeaminase
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proline→
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- Proline oxidase
- Pyrroline-5-carboxylate reductase
- 1-Pyrroline-5-carboxylate dehydrogenase/ALDH4A1
- PYCR1
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arginine→
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- Ornithine aminotransferase
- Ornithine decarboxylase
- Agmatinase
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→alpha-ketoglutarate→TCA
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Other
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- cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase
- Glutathione synthetase
- Gamma-glutamyl transpeptidase
- glutamate→glutamine: Glutamine synthetase
- Glutaminase
|
|
|
|
G→propionyl-CoA→
succinyl-CoA
|
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VALINE→
|
- Branched chain aminotransferase
- Branched-chain alpha-keto acid dehydrogenase complex
- Enoyl-CoA hydratase
- 3-hydroxyisobutyryl-CoA hydrolase
- 3-hydroxyisobutyrate dehydrogenase
- Methylmalonate semialdehyde dehydrogenase
|
|
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ISOLEUCINE→
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- Branched chain aminotransferase
- Branched-chain alpha-keto acid dehydrogenase complex
- 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
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|
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METHIONINE→
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- generation of homocysteine: Methionine adenosyltransferase
- Adenosylhomocysteinase
- regeneration of methionine: Methionine synthase/Homocysteine methyltransferase
- Betaine-homocysteine methyltransferase
- conversion to cysteine: Cystathionine beta synthase
- Cystathionine gamma-lyase
|
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THREONINE→
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→succinyl-CoA→TCA
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- Propionyl-CoA carboxylase
- Methylmalonyl CoA epimerase
- Methylmalonyl-CoA mutase
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G→fumarate
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PHENYLALANINE→tyrosine→
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- Phenylalanine hydroxylase
- Tyrosine aminotransferase
- 4-Hydroxyphenylpyruvate dioxygenase
- Homogentisate 1,2-dioxygenase
- Fumarylacetoacetate hydrolase
- tyrosine→melanin: Tyrosinase
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G→oxaloacetate
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asparagine→aspartate→
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- Asparaginase/Asparagine synthetase
- Aspartate transaminase
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- Facile chemoenzymatic strategies for the synthesis and utilization of s-adenosyl-L-methionine analogues.
- Singh S1, Zhang J, Huber TD, Sunkara M, Hurley K, Goff RD, Wang G, Zhang W, Liu C, Rohr J, Van Lanen SG, Morris AJ, Thorson JS.Author information 1Center for Pharmaceutical Research and Innovation, College of Pharmacy, University of Kentucky, Lexington, KY 40536 (USA); Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY 40536 (USA). ssingh555@uky.edu.AbstractA chemoenzymatic platform for the synthesis of S-adenosyl-L-methionine (SAM) analogues compatible with downstream SAM-utilizing enzymes is reported. Forty-four non-native S/Se-alkylated Met analogues were synthesized and applied to probing the substrate specificity of five diverse methionine adenosyltransferases (MATs). Human MAT II was among the most permissive of the MATs analyzed and enabled the chemoenzymatic synthesis of 29 non-native SAM analogues. As a proof of concept for the feasibility of natural product "alkylrandomization", a small set of differentially-alkylated indolocarbazole analogues was generated by using a coupled hMAT2-RebM system (RebM is the sugar C4'-O-methyltransferase that is involved in rebeccamycin biosynthesis). The ability to couple SAM synthesis and utilization in a single vessel circumvents issues associated with the rapid decomposition of SAM analogues and thereby opens the door for the further interrogation of a wide range of SAM utilizing enzymes.
- Angewandte Chemie (International ed. in English).Angew Chem Int Ed Engl.2014 Apr 7;53(15):3965-9. doi: 10.1002/anie.201308272. Epub 2014 Mar 11.
- A chemoenzymatic platform for the synthesis of S-adenosyl-L-methionine (SAM) analogues compatible with downstream SAM-utilizing enzymes is reported. Forty-four non-native S/Se-alkylated Met analogues were synthesized and applied to probing the substrate specificity of five diverse methionine adenosy
- PMID 24616228
- Dietary L-methionine supplementation mitigates gamma-radiation induced global DNA hypomethylation: Enhanced metabolic flux towards S-adenosyl-L-methionine (SAM) biosynthesis increases genomic methylation potential.
- Batra V1, Verma P2.Author information 1Radiation Biology and Health Sciences Division, Bhabha Atomic Research Centre, Mumbai - 400 085, India. Electronic address: batravipen@gmail.com.2Radiation Biology and Health Sciences Division, Bhabha Atomic Research Centre, Mumbai - 400 085, India.AbstractThe objective of this study was to examine the effect of 60Co-gamma (γ) radiation on modulation of genomic DNA methylation, if any, of mice maintained (6 weeks) on normal control diet (NCD) and L-methionine supplemented diet (MSD). To elucidate the possible underlying mechanism(s), we exposed the animals to γ-radiation (2, 3 and 4 Gy) and investigated the profile of downstream metabolites and enzymes involved in S-adenosyl-L-methionine (SAM) generation. Liver samples were also subjected to histopathological examinations. Compared to NCD fed and irradiated animals, hepatic folate, choline and L-methionine levels decreased moderately, while hepatic SAM levels increased in MSD fed and irradiated animals. Under these conditions, a marked modulation of methionine adenosyltransferase (MAT) and L-methionine synthase (MSase) activities was observed. Concomitant with increase in liver SAM pool, increased DNA methyltransferase (dnmt) activity in MSD fed mice indicated enhanced metabolic flux towards DNA methylation. Further results showed that genomic DNA methylation and 5-methyl-2'-deoxy cytidine residues were maintained at normal levels in MSD fed and irradiated mice compared to NCD fed and irradiated animals. In conclusion, our results suggest that increasing supply of preformed methyl groups, via dietary L-methionine supplementation might significantly increase methylation potential of radiation stress compromised DNA methylation cycle.
- Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association.Food Chem Toxicol.2014 Apr 7. pii: S0278-6915(14)00177-X. doi: 10.1016/j.fct.2014.03.040. [Epub ahead of print]
- The objective of this study was to examine the effect of 60Co-gamma (γ) radiation on modulation of genomic DNA methylation, if any, of mice maintained (6 weeks) on normal control diet (NCD) and L-methionine supplemented diet (MSD). To elucidate the possible underlying mechanism(s), we exposed the a
- PMID 24721433
- Alterations in the metabolomics of sulfur-containing substances in rat kidney by betaine.
- Kim YC1, Kwon do Y, Kim JH.Author information 1College of Pharmacy, Seoul National University, San 56-1 Shinrim-Dong, Kwanak-Ku, Seoul, 151-742, Korea, youckim@snu.ac.kr.AbstractEarlier studies have shown that betaine administration may modulate the metabolism of sulfur amino acids in the liver. In this study, we determined the changes in the metabolomics of sulfur-containing substances induced by betaine in the kidney, the other major organ actively involved in the transsulfuration reactions. Male rats received betaine (1 %) in drinking water for 2 weeks before killing. Betaine intake did not affect betaine-homocysteine methyltransferase activity or its protein expression in the renal tissue. Expression of methionine synthase was also unchanged. However, methionine levels were increased significantly both in plasma and kidney. Renal methionine adenosyltransferase activity and S-adenosylmethionine concentrations were increased, but there were no changes in S-adenosylhomocysteine, homocysteine, cysteine levels or cystathionine β-synthase expression. γ-Glutamylcysteine synthetase expression or glutathione levels were not altered, but cysteine dioxygenase and taurine levels were decreased significantly. In contrast, betaine administration induced cysteine sulfinate decarboxylase and its metabolic product, hypotaurine. These results indicate that the metabolomics of sulfur-containing substances in the kidney is altered extensively by betaine, although the renal capacity for methionine synthesis is unresponsive to this substance unlike that of the liver. It is suggested that the increased methionine availability due to an enhancement of its uptake from plasma may account for the alterations in the metabolomics of sulfur-containing substances in the kidney. Further studies need to be conducted to clarify the physiological/pharmacological significance of these findings.
- Amino acids.Amino Acids.2014 Apr;46(4):963-8. doi: 10.1007/s00726-013-1660-4. Epub 2014 Jan 4.
- Earlier studies have shown that betaine administration may modulate the metabolism of sulfur amino acids in the liver. In this study, we determined the changes in the metabolomics of sulfur-containing substances induced by betaine in the kidney, the other major organ actively involved in the transsu
- PMID 24390397
Japanese Journal
- O-2-181 肝臓におけるMethionine adenosyltransferaseのアイソザイム発現の変化について(肝 研究3,一般演題(口演),第63回日本消化器外科学会総会)
- A Fermented Substance from Aspergillus phoenicis Reduces Liver Fibrosis Induced by Carbon Tetrachloride in Rats
- FANG Hsun-Lang,LAI Jinn-Jsyy,LIN Wei-Lii,LIN Wen-Chuan
- Bioscience, biotechnology, and biochemistry 71(5), 1154-1161, 2007-05-23
- … Real-time quantitative reverse transcriptase-polymerase chain reaction (RT-qPCR) analysis showed that FSAP treatment increased the expression of matrix metalloproteinase 13 and decreased the expression of methionine adenosyltransferase 2A, collagen (α1)(I), collagen (α1)(III), transforming growth factor-β1, and tissue inhibitor of metalloproteinase 1. …
- NAID 10027514322
Related Links
- Methionine adenosyltransferase is an enzyme which catalyses the synthesis of S -adenosylmethionine (SAM) from methionine and ATP. [edit] Conserved motifs in the 3'UTR of MAT2A mRNA. A computational comparative analysis of ...
- MAT2A) encode for methionine adenosyltransferase, an essential enzyme responsible for S-adenosylmethi- onine (SAMe) biosynthesis. MAT1A is expressed in liver, whereas MAT2A is widely distributed. In liver, increased MAT2A expression ...
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