Entry Name (R)-S-adenosyl-L-methionine hydrolase (adenosine-forming);
Class Hydrolases;BRITE hierarchy
Sysname (R)-S-adenosyl-L-methionine hydrolase (adenosine-forming)
Reaction(IUBMB) (R)-S-adenosyl-L-methionine + H2O = adenosine + L-methionine [RN:
R12098 ]
Reaction(KEGG) Substrate Product Comment The enzyme, found in bacteria and archaea, is involved in removing the (R) isomer of S-adenosyl-L-methionine from the cell. It catalyses a nucleophilic attack of water at the C5' carbon of S-adenosyl-L-methionine to generate adenosine and L-methionine.
History EC 3.13.2.3 created 2018 as EC 3.13.1.8, transferred 2022 to EC 3.13.2.3
Orthology K22205 S-adenosyl-L-methionine hydrolase (adenosine-forming)
Genes FRA : Francci3_0478 Francci3_1909
FRE : Franean1_2242 Franean1_6138
FRI : FraEuI1c_4802 FraEuI1c_6318
BALA : DSM104299_05760(salL)
SBAE : DSM104329_05685(salL)
LET : O77CONTIG1_02834(salL)
NSPH : BDGGKGIB_04083(salL)
LEK : hrd7_06850 hrd7_22330
LCRE : Pla8534_09140(salL)
MGOT : MgSA37_02994(salL_2)
KOS : KORDIASMS9_03322(flA)
ASAC : ATHSA_0596 ATHSA_0655
» show all Taxonomy Reference Authors Eustaquio AS, Harle J, Noel JP, Moore BS
Title S-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved bacterial and archaeal protein related to SAM-dependent halogenases.
Journal Sequence Reference Authors Deng H, McMahon SA, Eustaquio AS, Moore BS, Naismith JH, O'Hagan D
Title Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62).
Journal Sequence Reference Authors Kornfuehrer T, Romanowski S, de Crecy-Lagard V, Hanson AD, Eustaquio AS.
Title An Enzyme Containing the Conserved Domain of Unknown Function DUF62 Acts as a Stereoselective (Rs ,Sc )-S-Adenosylmethionine Hydrolase.
Journal Sequence Other DBs ExplorEnz - The Enzyme Database: 3.13.2.3
ExPASy - ENZYME nomenclature database: 3.13.2.3
