BRENDA - Enzyme Database
show all sequences of 3.6.1.25

Biochemical basis for the dominant inheritance of hypermethioninemia associated with the R264H mutation of the MAT1A gene. A monomeric methionine adenosyltransferase with tripolyphosphatase activity

Perez Mato, I.; Sanchez del Pino, M.M.; Chamberlin, M.E.; Mudd, S.H.; Mato, J.M.; Corrales, F.J.; J. Biol. Chem. 276, 13803-13809 (2001)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
His-tagged R265H mutant, expressed in E. coli BL21
Rattus norvegicus
Engineering
Protein Variants
Commentary
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
Commentary
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]
Commentary
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
Commentary
Textmining
Rattus norvegicus
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
His-tagged R265H mutant purified with Ni2+ Sepharose column chromatography and wildtype enzyme purified from liver
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
triphosphate + H2O
-
669193
Rattus norvegicus
diphosphate + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterodimer
containing one R265H mutant subunit and one wildtype subunit, impaired AdoMet synthetase activity
Rattus norvegicus
monomer
R265H mutant
Rattus norvegicus
Cloned(Commentary) (protein specific)
Commentary
Organism
His-tagged R265H mutant, expressed in E. coli BL21
Rattus norvegicus
Engineering (protein specific)
Protein Variants
Commentary
Organism
R265H
no AdoMet synthetase activity, normal tripolyphosphatase activity
Rattus norvegicus
R265S
no AdoMet synthetase activity, reduced tripolyphosphatase activity
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Purification (Commentary) (protein specific)
Commentary
Organism
His-tagged R265H mutant purified with Ni2+ Sepharose column chromatography and wildtype enzyme purified from liver
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
triphosphate + H2O
-
669193
Rattus norvegicus
diphosphate + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
containing one R265H mutant subunit and one wildtype subunit, impaired AdoMet synthetase activity
Rattus norvegicus
monomer
R265H mutant
Rattus norvegicus
Other publictions for EC 3.6.1.25
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
719965
Delvaux
A specific inorganic triphosph ...
Nitrosomonas europaea
J. Biol. Chem.
286
34023-34035
2011
-
-
1
1
3
-
3
11
-
3
1
-
-
7
-
-
1
-
-
-
-
-
3
1
3
1
-
-
11
1
-
-
-
-
-
3
-
-
1
-
1
3
-
3
3
-
11
-
3
1
-
-
-
-
1
-
-
-
-
3
1
1
-
-
11
1
-
-
-
-
-
-
-
11
11
669193
Perez Mato
Biochemical basis for the domi ...
Rattus norvegicus
J. Biol. Chem.
276
13803-13809
2001
-
-
1
-
2
-
-
6
-
-
2
-
-
3
-
-
1
-
-
1
12
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
6
-
-
2
-
-
-
-
1
-
1
12
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
210003
Yu
Structure-function analysis of ...
Vaccinia virus
J. Virol.
71
9837-9843
1997
-
-
-
-
-
-
-
-
-
-
1
1
-
8
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
210002
Trilisenko
Subcellular localization of en ...
Kitasatospora aureofaciens
Folia Microbiol. (Praha)
32
402-410
1987
-
-
-
-
-
-
1
-
1
-
-
1
-
4
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
210001
Kulalev
-
A comparative characterization ...
Neurospora crassa
Biochemistry (Moscow)
39
309-312
1974
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
210000
Kulaev
-
Localization of polyphosphatas ...
Neurospora crassa
Biochemistry (Moscow)
37
190-194
1972
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-