ホモシステイン-S-メチル基転移酵素、ホモシステイン-S-メチルトランスフェラーゼ
WordNet
- the 19th letter of the Roman alphabet (同)s
PrepTutorEJDIC
- sulfurの化学記号 / {略}South[ern]
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/06/22 15:14:26」(JST)
[Wiki en表示]
homocysteine S-methyltransferase |
Identifiers |
EC number |
2.1.1.10 |
CAS number |
9012-40-2 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / EGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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In enzymology, a homocysteine S-methyltransferase (EC 2.1.1.10) is an enzyme that catalyzes the chemical reaction
- S-methylmethionine + L-homocysteine 2 L-methionine
Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of L-methionine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-homocysteine S-methyltransferase. Other names in common use include S-adenosylmethionine homocysteine transmethylase, S-methylmethionine homocysteine transmethylase, adenosylmethionine transmethylase, methylmethionine:homocysteine methyltransferase, adenosylmethionine:homocysteine methyltransferase, homocysteine methylase, homocysteine methyltransferase, homocysteine transmethylase, L-homocysteine S-methyltransferase, S-adenosyl-L-methionine:L-homocysteine methyltransferase, S-adenosylmethionine-homocysteine transmethylase, and S-adenosylmethionine:homocysteine methyltransferase. This enzyme participates in methionine metabolism.
References
- Balish E, Shapiro SK (1967). "Methionine biosynthesis in Escherichia coli: induction and repression of methylmethionine(or adenosylmethionine):homocysteine methyltransferase". Arch. Biochem. Biophys. 119 (1): 62–8. doi:10.1016/0003-9861(67)90429-8. PMID 4861151.
- Shapiro SK (1958). "Adenosylmethionine-homocysteine transmethylase". Biochim. Biophys. Acta 29 (2): 405–409. doi:10.1016/0006-3002(58)90199-9. PMID 13572358.
- Shapiro SK; Yphantis DA (1959). "Assay of S-methylmethionine and S-adenosylmethionine homocysteine transmethylases". Biochim. Biophys. Acta 36: 241–244. doi:10.1016/0006-3002(59)90089-7. PMID 14445542.
Transferase: one carbon transferases (EC 2.1)
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2.1.1: Methyl- |
N- |
- Histamine N-methyltransferase
- Phenylethanolamine N-methyltransferase
- Amine N-methyltransferase
- Phosphatidylethanolamine N-methyltransferase
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O- |
- 5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase
- Catechol-O-methyl transferase
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Homocysteine |
- Betaine-homocysteine methyltransferase
- Homocysteine methyltransferase
- Methionine synthase
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Other |
- Phosphatidyl ethanolamine methyltransferase
- DNMT3B
- Histone methyltransferase
- Thymidylate synthase
- DNA methyltransferase
- Thiopurine methyltransferase
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2.1.2: Hydroxymethyl-,
Formyl- and Related |
Hydroxymethyltransferase |
- Serine hydroxymethyltransferase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
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Formyltransferase |
- Phosphoribosylglycinamide formyltransferase
- Inosine monophosphate synthase
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Other |
- Glutamate formimidoyltransferase
- Aminomethyltransferase
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2.1.3: Carboxy-
and Carbamoyl |
Carboxy |
- methylmalonyl-CoA carboxytransferase
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Carbamoyl |
- Aspartate carbamoyltransferase
- Ornithine carbamoyltransferase
- Oxamate carbamoyltransferase
- Putrescine carbamoyltransferase
- 3-hydroxymethylcephem carbamoyltransferase
- Lysine carbamoyltransferase
- N-acetylornithine carbamoyltransferase
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2.1.4: Amidine |
- Arginine:glycine amidinotransferase
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Enzymes
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Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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English Journal
- Specific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferase.
- Mládková J1, Hladílková J, Diamond CE, Tryon K, Yamada K, Garrow TA, Jungwirth P, Koutmos M, Jiráček J.
- Proteins.Proteins.2014 Jun 4. doi: 10.1002/prot.24619. [Epub ahead of print]
- Betaine-homocysteine S-methyltransferase (BHMT) is a zinc-dependent methyltransferase that uses betaine as the methyl donor for the remethylation of homocysteine to form methionine. This reaction supports S-adenosylmethionine biosynthesis, which is required for hundreds of methylation reactions in h
- PMID 24895213
- Structural analysis of a fungal methionine synthase with substrates and inhibitors.
- Ubhi D1, Kago G1, Monzingo AF1, Robertus JD2.
- Journal of molecular biology.J Mol Biol.2014 Apr 17;426(8):1839-47. doi: 10.1016/j.jmb.2014.02.006. Epub 2014 Feb 11.
- The cobalamin-independent methionine synthase from Candida albicans, known as Met6p, is a 90-kDa enzyme that consists of two (βα)8 barrels. The active site is located between the two domains and has binding sites for a zinc ion and substrates L-homocysteine and 5-methyl-tetrahydrofolate-glutamate3
- PMID 24524835
- Differential proteomic profiling reveals regulatory proteins and novel links between primary metabolism and spinosad production in Saccharopolyspora spinosa.
- Yang Q, Ding X1, Liu X, Liu S, Sun Y, Yu Z, Hu S, Rang J, He H, He L, Xia L.
- Microbial cell factories.Microb Cell Fact.2014 Feb 21;13(1):27. doi: 10.1186/1475-2859-13-27.
- BACKGROUND: Saccharopolyspora spinosa is an important producer of antibiotic spinosad with clarified biosynthesis pathway but its complex regulation networks associated with primary metabolism and secondary metabolites production almost have never been concerned or studied before. The proteomic anal
- PMID 24555503
Japanese Journal
- L-serine attenuate steatosis by suppression of hyperhomocysteinemia
- Hepatic Cystathionine β-Synthase Activity Does Not Increase in Response to Methionine Supplementation in Rats Fed a Low Casein Diet : Association with Plasma Homocysteine Concentrations
- Journal of nutritional science and vitaminology 55(2), 178-185, 2009-04-01
- NAID 10025970986
- High Casein Diet Decreases Plasma Homocysteine Concentration in Rats
- Journal of nutritional science and vitaminology 55(1), 22-30, 2009-02
- NAID 110007110612
Related Links
- This gene encodes a cytosolic enzyme that catalyzes the conversion of betaine and homocysteine to dimethylglycine and methionine, respectively. Defects in this gene could lead to hyperhomocyst(e)inemia, but such a ...
- S-methylmethionine: homocysteine methyltransferase EC:2.1.1.10 from Escherichia coli accepts selenohomocysteine as a substrate. S-methylmethionine is an abundant plant product that can be utilised for methionine biosynthesis [PMID: 9882684
★リンクテーブル★
[★]
- 英
- homocysteine S-methyltransferase
- 同
- ホモシステイン-S-メチル基転移酵素
- 関
- ホモシステイン
- 5-メチルテトラヒドロ葉酸ホモシステイン-S-メチルトランスフェラーゼ
- 5-メチルテトラヒドロ葉酸ホモシステイン-S-メチル基転移酵素
- 5-methyltetrahydrofolate-homocysteine S-methyltransferase
[★]
5-メチルテトラヒドロ葉酸ホモシステイン-S-メチル基転移酵素、5-メチルテトラヒドロ葉酸ホモシステイン-S-メチルトランスフェラーゼ
- 関
- methionine synthase、methionine synthetase
[★]
ベタイン・ホモシステイン-S-メチル基転移酵素、ベタイン・ホモシステイン-S-メチルトランスフェラーゼ
- 関
- betaine-homocysteine methyltransferase
[★]
メチルトランスフェラーゼ、メチル基転移酵素、メチル化酵素
[★]
[★]
メチルトランスフェラーゼ