BRENDA - Enzyme Database show
show all sequences of 2.1.1.22

The use of alternative substrates in the characterization of actin-methylating and carnosine-methylating enzymes

Raghavan, M.; Lindberg, U.; Schutt, C.; Eur. J. Biochem. 210, 311-318 (1992)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5
-
Actin peptide H
-
Oryctolagus cuniculus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
85000
-
gel filtration, sucrose density gradient centrifugation
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
actin peptide H + S-adenosyl-L-methionine
Oryctolagus cuniculus
synthetic peptide based on amino acid sequence of actin
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
-
Oryctolagus cuniculus
-
S-adenosyl-L-methionine + carnosine
Oryctolagus cuniculus
-
S-adenosyl-L-homocysteine + anserine
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oryctolagus cuniculus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
muscle
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
actin peptide H + S-adenosyl-L-methionine
synthetic peptide based on amino acid sequence of actin
485239
Oryctolagus cuniculus
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
-
485239
Oryctolagus cuniculus
-
S-adenosyl-L-methionine + carnosine
-
485239
Oryctolagus cuniculus
S-adenosyl-L-homocysteine + anserine
-
-
-
-
S-adenosyl-L-methionine + L-histidine
-
485239
Oryctolagus cuniculus
S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
-
485239
Oryctolagus cuniculus
?
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.5
-
Actin peptide H
-
Oryctolagus cuniculus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
85000
-
gel filtration, sucrose density gradient centrifugation
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
actin peptide H + S-adenosyl-L-methionine
Oryctolagus cuniculus
synthetic peptide based on amino acid sequence of actin
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
-
Oryctolagus cuniculus
-
S-adenosyl-L-methionine + carnosine
Oryctolagus cuniculus
-
S-adenosyl-L-homocysteine + anserine
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
muscle
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
actin peptide H + S-adenosyl-L-methionine
synthetic peptide based on amino acid sequence of actin
485239
Oryctolagus cuniculus
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
-
485239
Oryctolagus cuniculus
-
S-adenosyl-L-methionine + carnosine
-
485239
Oryctolagus cuniculus
S-adenosyl-L-homocysteine + anserine
-
-
-
-
S-adenosyl-L-methionine + L-histidine
-
485239
Oryctolagus cuniculus
S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
-
485239
Oryctolagus cuniculus
?
Other publictions for EC 2.1.1.22
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)
734309
Drozak
UPF0586 protein C9orf41 homolo ...
Gallus gallus, Homo sapiens, Rattus norvegicus
J. Biol. Chem.
290
17190-17205
2015
-
-
3
-
-
-
-
6
6
-
-
-
-
8
-
-
-
-
-
3
-
-
12
-
-
-
-
6
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
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6
6
-
-
-
-
-
-
-
-
3
-
-
12
-
-
-
-
6
-
-
-
-
-
3
3
-
-
-
735092
Drozak
Molecular identification of ca ...
Gallus gallus
PLoS ONE
8
e64805
2013
-
-
1
-
-
-
-
1
-
-
3
-
-
3
-
-
-
-
-
1
-
-
2
1
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
1
-
-
2
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
485239
Raghavan
The use of alternative substra ...
Oryctolagus cuniculus
Eur. J. Biochem.
210
311-318
1992
-
-
-
-
-
-
-
1
-
-
1
2
-
4
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
2
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
485238
McManus
-
Enzymatic synthesis of anserin ...
Cavia porcellus, Felis catus, Gallus gallus, Oryctolagus cuniculus, Rattus norvegicus
J. Biol. Chem.
237
1207-1211
1962
-
-
-
-
-
1
-
2
1
3
-
5
-
5
-
-
1
-
-
19
1
1
14
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
1
3
-
5
-
-
-
1
-
19
1
1
14
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-