BRENDA - Enzyme Database
show all sequences of 2.1.1.59

A cytochrome c methyltransferase from Crithidia oncopelti

Valentine, J.; Pettigrew, G.W.; Biochem. J. 201, 329-338 (1982)

Data extracted from this reference:

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
Strigomonas oncopelti
-
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Strigomonas oncopelti
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Strigomonas oncopelti
-
-
-
Reaction
Reaction
Commentary
Organism
S-adenosyl-L-methionine + [cytochrome c]-L-lysine = S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
specific methylation site, 1 lysine in cytochrome c, comparison
Strigomonas oncopelti
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
development of a radioactive assay method
Strigomonas oncopelti
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
-
485474
Strigomonas oncopelti
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485474
Strigomonas oncopelti
?
S-adenosyl-L-methionine + cytochrome c L-lysine
lysine-72 of horse cytochrome c is a poor acceptor
485474
Strigomonas oncopelti
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
485474
Strigomonas oncopelti
?
S-adenosyl-L-methionine + cytochrome c L-lysine
Crithidia cytochrome c-557 is far the best substrate
485474
Strigomonas oncopelti
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
485474
Strigomonas oncopelti
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Strigomonas oncopelti
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
Strigomonas oncopelti
-
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Strigomonas oncopelti
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
development of a radioactive assay method
Strigomonas oncopelti
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
-
485474
Strigomonas oncopelti
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
485474
Strigomonas oncopelti
?
S-adenosyl-L-methionine + cytochrome c L-lysine
lysine-72 of horse cytochrome c is a poor acceptor
485474
Strigomonas oncopelti
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
485474
Strigomonas oncopelti
?
S-adenosyl-L-methionine + cytochrome c L-lysine
Crithidia cytochrome c-557 is far the best substrate
485474
Strigomonas oncopelti
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
485474
Strigomonas oncopelti
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Strigomonas oncopelti
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
-
-
-
-
-
-
-
-
-
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6
-
-
-
-
-
-
1
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3
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-
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-
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1
-
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-
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-
1
-
3
-
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-
-
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-
-
-
-
-
-
-
-
-
485477
Park
Enzymatic methylation of in vi ...
Saccharomyces cerevisiae
J. Biol. Chem.
262
14702-14708
1987
-
-
1
-
-
-
2
-
-
-
-
1
-
1
-
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-
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2
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1
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2
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1
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-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
1
-
6
-
-
-
1
-
-
1
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3
-
1
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1
-
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-
-
-
1
-
3
-
1
-
-
-
-
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-
-
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-
-
-
485481
DiMaria
Cytochrome c specific methylas ...
Triticum aestivum
Biochemistry
21
1036-1044
1982
-
-
-
-
-
-
2
2
-
-
-
1
-
1
-
-
1
-
-
1
2
-
6
-
-
-
-
-
-
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-
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-
-
2
-
2
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-
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1
-
-
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1
-
1
2
-
6
-
-
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-
-
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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-
-
-
-
-
-
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
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3
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1
1
-
1
1
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4
-
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1
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2
3
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1
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1
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1
1
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4
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1
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