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Literature summary for 2.5.1.6 extracted from

  • Chamberlin, M.E.; Ubagai, T.; Pao, V.Y.; Pearlstein, R.A.; Yang Chou, J.
    Structural requirements for catalysis and dimerization of human methionine adenosyltransferase I/III (2000), Arch. Biochem. Biophys., 373, 56-62.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in M15 bacteria Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
L-methionine wild-type Homo sapiens
0.08
-
L-methionine S283T mutant Homo sapiens
0.088
-
L-methionine Q113A mutant, S-adenosylmethionine synthesis Homo sapiens
0.22
-
L-methionine wild-type Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + H2O
-
Homo sapiens S-adenosyl-L-methionine + phosphate + diphosphate
-
?

Subunits

Subunits Comment Organism
dimer substrate and/or reaction products promotes dimer formation Homo sapiens