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Literature summary for 3.13.2.3 extracted from

  • Kornfuehrer, T.; Romanowski, S.; de Crecy-Lagard, V.; Hanson, A.D.; Eustaquio, A.S.
    An enzyme containing the conserved domain of unknown function DUF62 acts as a stereoselective (Rs,Sc)-S-adenosylmethionine hydrolase (2020), ChemBioChem, 21, 3495-3499 .
    View publication on PubMed
Search for more literature for 3.13.2.3

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00063
-
 (R)-S-adenosyl-L-methionine pH 7.5, 37°C Salinispora tropica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-S-adenosyl-L-methionine + H2O Salinispora tropica
-
 adenosine + L-methionine
-
 ?

Organism

Organism UniProt Comment Textmining
Salinispora tropica A4X4S2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-S-adenosyl-L-methionine + H2O
-
 Salinispora tropica adenosine + L-methionine
-
 ?

Synonyms

Synonyms Comment Organism
(Rs,Sc)-S-adenosylmethionine hydrolase
-
 Salinispora tropica
StDUF62
-
 Salinispora tropica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0045
-
 (R)-S-adenosyl-L-methionine pH 7.5, 37°C Salinispora tropica

General Information

General Information Comment Organism
physiological function the enzyme likely plays a role in preventing accumulation of (R)-S-adenosyl-L-methionine in cells. Maintenance of (S)-S-denosyl-L-methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases Salinispora tropica