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Literature summary for 4.4.1.16 extracted from

  • Mihara, H.; Fujii, T.; Kato, S.; Kurihara, T.; Hata, Y.; Esaki, N.
    Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine (2002), J. Biochem., 131, 679-685.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
H123A only 1% of activity remaining compared to wild type, contributes to stabilization of pyridoxal 5'-phospahte Escherichia coli
H55A no effect on activity Escherichia coli
R379A less than 1% of activity remaining compared to wild type Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-selenocysteine + reduced acceptor Escherichia coli
-
selenide + L-alanine + acceptor
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-selenocysteine + reduced acceptor
-
Escherichia coli selenide + L-alanine + acceptor
-
?
L-selenocysteine + reduced acceptor enzyme bound pyridoxal 5'-phosphate serves as acceptor Escherichia coli selenide + L-alanine + acceptor
-
?
additional information traces of activity with L-cysteine Escherichia coli ?
-
?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate required Escherichia coli