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Literature summary for 3.6.1.25 extracted from

  • Perez Mato, I.; Sanchez del Pino, M.M.; Chamberlin, M.E.; Mudd, S.H.; Mato, J.M.; Corrales, F.J.
    Biochemical basis for the dominant inheritance of hypermethioninemia associated with the R264H mutation of the MAT1A gene. A monomeric methionine adenosyltransferase with tripolyphosphatase activity (2001), J. Biol. Chem., 276, 13803-13809.
    View publication on PubMed
Search for more literature for 3.6.1.25

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged R265H mutant, expressed in E. coli BL21 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
R265H no AdoMet synthetase activity, normal tripolyphosphatase activity Rattus norvegicus
R265S no AdoMet synthetase activity, reduced tripolyphosphatase activity Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information no change in activity after nitrosylation of the enzyme with 250 microM nitrosylated glutathione Rattus norvegicus
0.02
-
 tripolyphosphate wildtype, 2 mM substrate Rattus norvegicus
0.078
-
 tripolyphosphate R265H mutant, 2 mM substrate in the presence of 5 mM ATP Rattus norvegicus
0.083
-
 tripolyphosphate R265H mutant, 2 mM substrate Rattus norvegicus
0.122
-
 tripolyphosphate R265S mutant, 2 mM substrate Rattus norvegicus
0.143
-
 tripolyphosphate R265H mutant, 2 mM substrate in the presence of 5 mM diphosphate Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41600
-
 R265H mutant, gel filtration, column equilibrated with 2 mM tripolyphosphate Rattus norvegicus
90000
-
 heterodimer of R265H mutant and wildtype enzyme, size exclusion chromatography Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
His-tagged R265H mutant purified with Ni2+ Sepharose column chromatography and wildtype enzyme purified from liver Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 tripolyphosphate activity of R265H mutant is specific for tripolyphosphate and depends on magnesium ions, potassium is not required Rattus norvegicus
0.001
-
 R265S mutant, 2 mM methionine and 2 mM ATP as substrate Rattus norvegicus
0.0012
-
 tripolyphosphatase activity of R265H mutant, 2 mM ATP as substrate Rattus norvegicus
0.0019
-
 tripolyphosphatase activity of R265H mutant, 2 mM pyrophosphate as substrate Rattus norvegicus
0.002
-
 R265H mutant, 2 mM methionine and 2 mM ATP as substrate Rattus norvegicus
0.004
-
 tripolyphosphatase activity of R265H mutant, 2 mM metatripolyphosphate as substrate Rattus norvegicus
0.029
-
 tripolyphosphatase activity of R265S mutant, 2 mM tripolyphosphate as substrate Rattus norvegicus
0.067
-
 tripolyphosphatase activity of R265H mutant, 2 mM tripolyphosphate as substrate in the presence of 5 mM pyrophosphate Rattus norvegicus
0.128
-
 tripolyphosphatase activity of R265H mutant, 2 mM tripolyphosphate as substrate Rattus norvegicus
0.129
-
 tripolyphosphatase activity of R265H mutant, 2 mM tripolyphosphate as substrate in the presence of 5 mM ATP Rattus norvegicus
0.156
-
 tripolyphosphatase activity of wildtype, 2 mM tripolyphosphate as substrate Rattus norvegicus
0.588
-
 wildtype, 2 mM methionine and 2 mM ATP as substrate Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
triphosphate + H2O
-
 Rattus norvegicus diphosphate + phosphate
-
 ?

Subunits

Subunits Comment Organism
heterodimer containing one R265H mutant subunit and one wildtype subunit, impaired AdoMet synthetase activity Rattus norvegicus
monomer R265H mutant Rattus norvegicus