Methionine adenosyltransferase
From Proteopedia
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<StructureSection load='1o9t' size='350' side='right' caption='The rat S-adenosylmethionine synthetase complex with methionine, phosphate, ATP (stick model), Mg+2 (green), phosphate and K+ (purple) ions (PDB entry [[1o9t]])' scene='49/493038/Cv/4'> | <StructureSection load='1o9t' size='350' side='right' caption='The rat S-adenosylmethionine synthetase complex with methionine, phosphate, ATP (stick model), Mg+2 (green), phosphate and K+ (purple) ions (PDB entry [[1o9t]])' scene='49/493038/Cv/4'> | ||
== Function == | == Function == | ||
- | '''S-adenosylmethionine synthetase''' or (MAT) catalyzes the conversion of methionine and ATP to S-adenosylmethionine (AdoMet), pyrophosphate (PPi) and orthophosphate (Pi). AdoMet is a methyl donor. The catalytic entity of MAT is a dimer. MAT cofactors are Mg+2 (or Co+2) and K+ ions<ref>PMID:8611562</ref>. | + | '''S-adenosylmethionine synthetase''' or '''S-adenosylmethionine transferase''' (MAT) catalyzes the conversion of methionine and ATP to S-adenosylmethionine (AdoMet), pyrophosphate (PPi) and orthophosphate (Pi). AdoMet is a methyl donor. The catalytic entity of MAT is a dimer. MAT cofactors are Mg+2 (or Co+2) and K+ ions<ref>PMID:8611562</ref>. |
== Relevance == | == Relevance == |
Revision as of 09:06, 13 March 2022
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3D structures of S-adenosylmethionine synthetase
13-March-2022
References
- ↑ Takusagawa F, Kamitori S, Markham GD. Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution. Biochemistry. 1996 Feb 27;35(8):2586-96. PMID:8611562 doi:http://dx.doi.org/10.1021/bi952604z
- ↑ Mato JM, Alvarez L, Ortiz P, Mingorance J, Duran C, Pajares MA. S-adenosyl-L-methionine synthetase and methionine metabolism deficiencies in cirrhosis. Adv Exp Med Biol. 1994;368:113-7. PMID:7741002
- ↑ Gonzalez B, Pajares MA, Hermoso JA, Guillerm D, Guillerm G, Sanz-Aparicio J. Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism. J Mol Biol. 2003 Aug 8;331(2):407-16. PMID:12888348
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