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Literature summary for 2.5.1.6 extracted from

  • Langkamp-Henken, B.; Geller, A.M.; LeGros, H.L., Jr.; Price, J.O.; De la Rosa, J.; Kotb, M.
    Characterization of distinct forms of methionine adenosyltransferase in nucleated, and mature human erythrocytes and erythroleukemic cells (1994), Biochim. Biophys. Acta, 1201, 397-404.
    View publication on PubMed
Search for more literature for 2.5.1.6

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0075
-
 L-methionine erythrocyte extract, alpha and beta subunit Homo sapiens
0.0125
-
 L-methionine erythrocyte extract, alpha subunit Homo sapiens
0.015
-
 L-methionine endogenous MAT II Homo sapiens
0.022
-
 L-methionine crude extract Homo sapiens
0.022 0.024 L-methionine ro subunit Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32500
-
 beta subunit, gel filtration Homo sapiens
53000
-
 alpha subunit, gel filtration Homo sapiens
60000
-
 isoenzyme ro, Peak I, gel filtration Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial on DEAE-cellulose, two peaks of activity: peak I contains ro isoform and peak II contains subunits alpha and beta Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Homo sapiens
-
erythroleukemia cell
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0002
-
 activity Peak II, adult erythrocytes Homo sapiens

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
? ro subunit may exist in a monomeric or polymeric form Homo sapiens