AdoMet MTase explained

Symbol:SAM-dependent_MTases
SAM-dependent MTases superfamily
Ecod:2003.1.5
Interpro:IPR029063
Symbol:AdoMet_MTase
AdoMet_MTase
Pfam:PF07757
Pfam Clan:CL0063
Interpro:IPR011671

S-adenosylmethionine-dependent methyltransferase (SAM-MTase or AdoMet-MTase) is a conserved protein domain and protein superfamily.[1] SAM-MTase proteins are methyltransferases.[2] There are five protein families within SAM-MTase,

SAM-MTases use S-adenosyl-L-methionine as a substrate for methylation, creating the product S-adenosyl-L-homocysteine.[3]

Structure and subgroups

All SAM-MTases contain a structurally conserved SAM-binding domain consisting of a central seven-stranded beta-sheet that is flanked by three alpha-helices per side of the sheet.[4]

A review published in 2003 divides all methyltransferases into 5 main classes based on the structure of their catalytic domain (fold):[5]

Notes and References

  1. Wang . Jiyao . Chitsaz . Farideh . Derbyshire . Myra K. . Gonzales . Noreen R. . Gwadz . Marc . Lu . Shennan . Marchler . Gabriele H. . Song . James S. . Thanki . Narmada . Yamashita . Roxanne A. . Yang . Mingzhang . Zhang . Dachuan . Zheng . Chanjuan . Lanczycki . Christopher J. . Marchler-Bauer . Aron . 2023-01-06 . The conserved domain database in 2023 . Nucleic Acids Research . 51 . D1 . D384–D388 . 10.1093/nar/gkac1096 . 1362-4962 . 9825596 . 36477806.
  2. Knizewski L, Ginalski K . July 2006 . DUF1613 is a novel family of eucaryotic AdoMet-dependent methyltransferases . Cell Cycle . 5 . 14 . 1580–2 . 10.4161/cc.5.14.2978 . 16861910 . free.
  3. Web site: CDD Conserved Protein Domain Family: AdoMet_MTases . 2023-12-07 . www.ncbi.nlm.nih.gov.
  4. Martin . Jennifer L . McMillan . Fiona M . 2002-12-01 . SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold . Current Opinion in Structural Biology . 12 . 6 . 783–793 . 10.1016/s0959-440x(02)00391-3 . 1879-033X . 12504684.
  5. Schubert . Heidi L . Blumenthal . Robert M . Cheng . Xiaodong . 2003-06-01 . Many paths to methyltransfer: a chronicle of convergence . Trends in Biochemical Sciences . 28 . 6 . 329–335 . 10.1016/s0968-0004(03)00090-2 . 0968-0004 . 2758044 . 12826405.