BRENDA - Enzyme Database
show all sequences of 2.1.1.59

Cytochrome c specific methylase from wheat germ

DiMaria, P.; Kim, S.; Paik, W.K.; Biochemistry 21, 1036-1044 (1982)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
S-Adenosyl-D-homocysteine
-
Triticum aestivum
S-adenosyl-L-homocysteine
-
Triticum aestivum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Triticum aestivum
0.000121
-
apocytochrome c
-
Triticum aestivum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + cytochrome c L-lysine
Triticum aestivum
-
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Triticum aestivum
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Triticum aestivum
-
-
-
Purification (Commentary)
Commentary
Organism
-
Triticum aestivum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
germ
-
Triticum aestivum
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Triticum aestivum
0.000508
-
purified enzyme
Triticum aestivum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + cytochrome c L-lysine
-
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
avian cytochromes c are much better substrates than those from mammalian sources
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
horse heart cytochrome c-72
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
does not randomly methylate cytochrome c, but shows absolute specificity for some amino acid sequences
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
also CNBr peptides of horse heart cytochrome c can serve as substrates, overview
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
overview: substrate activity of various cytochromes c
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
S-Adenosyl-D-homocysteine
-
Triticum aestivum
S-adenosyl-L-homocysteine
-
Triticum aestivum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Triticum aestivum
0.000121
-
apocytochrome c
-
Triticum aestivum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + cytochrome c L-lysine
Triticum aestivum
-
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Triticum aestivum
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Triticum aestivum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
germ
-
Triticum aestivum
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Triticum aestivum
0.000508
-
purified enzyme
Triticum aestivum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + cytochrome c L-lysine
-
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
avian cytochromes c are much better substrates than those from mammalian sources
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
horse heart cytochrome c-72
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
does not randomly methylate cytochrome c, but shows absolute specificity for some amino acid sequences
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
also CNBr peptides of horse heart cytochrome c can serve as substrates, overview
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
S-adenosyl-L-methionine + cytochrome c L-lysine
overview: substrate activity of various cytochromes c
485481
Triticum aestivum
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485481
Triticum aestivum
?
Other publictions for EC 2.1.1.59
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
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)
485478
Polevoda
Cytochrome c methyltransferase ...
Saccharomyces cerevisiae
J. Biol. Chem.
275
20508-20513
2000
-
-
1
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485477
Park
Enzymatic methylation of in vi ...
Saccharomyces cerevisiae
J. Biol. Chem.
262
14702-14708
1987
-
-
1
-
-
-
2
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
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-
-
-
-
-
-
-
-
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1
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2
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1
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-
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-
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-
2
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
485480
Paik
Enzymatic methylation and deme ...
Neurospora crassa
Methods Enzymol.
106
274-287
1984
-
-
-
-
-
-
2
7
2
-
1
1
-
1
-
-
1
-
-
1
1
1
5
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
1
7
2
-
1
1
-
-
-
1
-
1
1
1
5
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
485479
Durban
-
Cytochrome c-specific protein- ...
Neurospora crassa
Korean J. Biochem.
15
19-24
1983
-
-
-
-
-
-
2
2
-
-
-
1
-
1
-
-
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
1
2
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485474
Valentine
A cytochrome c methyltransfera ...
Strigomonas oncopelti
Biochem. J.
201
329-338
1982
-
-
-
-
-
-
-
-
-
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1
-
6
-
-
-
1
-
-
1
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
1
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
485481
DiMaria
Cytochrome c specific methylas ...
Triticum aestivum
Biochemistry
21
1036-1044
1982
-
-
-
-
-
-
2
2
-
-
-
1
-
1
-
-
1
-
-
1
2
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
1
-
-
-
1
-
1
2
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485482
DiMaria
Studies on cytochrome c methyl ...
Saccharomyces cerevisiae
J. Biol. Chem.
254
4645-4652
1979
-
-
-
-
-
-
1
2
-
-
1
2
-
1
-
-
1
-
-
-
1
2
11
-
-
-
-
-
1
-
-
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-
-
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-
-
-
-
-
-
-
1
-
2
-
-
1
2
-
-
-
1
-
-
1
2
11
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
485476
Durban
Cytochrome c-specific protein- ...
Neurospora crassa
J. Biol. Chem.
253
1427-1435
1978
-
-
-
-
-
-
2
7
1
-
1
1
-
2
-
-
1
1
-
-
1
-
11
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
1
7
1
-
1
1
-
-
-
1
-
-
1
-
11
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
485475
Nochumson
Cytochrome c-specific protein ...
Neurospora crassa
Biochem. J.
165
11-18
1977
-
-
-
-
-
-
-
2
3
-
-
1
-
3
-
-
1
1
-
1
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
3
-
-
1
-
-
-
1
-
1
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-