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Literature summary for 2.1.1.22 extracted from

  • Raghavan, M.; Lindberg, U.; Schutt, C.
    The use of alternative substrates in the characterization of actin-methylating and carnosine-methylating enzymes (1992), Eur. J. Biochem., 210, 311-318.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5
-
Actin peptide H
-
Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
85000
-
gel filtration, sucrose density gradient centrifugation Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
S-adenosyl-L-methionine + carnosine Oryctolagus cuniculus
-
S-adenosyl-L-homocysteine + anserine
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
actin peptide H + S-adenosyl-L-methionine synthetic peptide based on amino acid sequence of actin Oryctolagus cuniculus actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
-
?
S-adenosyl-L-methionine + carnosine
-
Oryctolagus cuniculus S-adenosyl-L-homocysteine + anserine
-
?
S-adenosyl-L-methionine + L-histidine
-
Oryctolagus cuniculus S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
-
?