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Literature summary extracted from

  • McGinnis, K.; Ku, G.M.; Fu, J.; Stern, A.M.; Friedman, P.A.
    The five cysteine residues located in the active site region of bovine aspartyl (asparaginyl) beta-hydroxylase are not essential for catalysis (1998), Biochim. Biophys. Acta, 1387, 454-456.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.16 wild-type and mutant enzymes expressed in Escherichia coli Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.16 C637A 38% activity of wild-type Bos taurus
1.14.11.16 C644A 62% activity of wild-type Bos taurus
1.14.11.16 C656A 100% activity of wild-type Bos taurus
1.14.11.16 C681A 60% activity of wild-type Bos taurus
1.14.11.16 C696A 29% activity of wild-type Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.16 Bos taurus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.16 peptide L-asparagine + 2-oxoglutarate + O2
-
 Bos taurus peptide 3-hydroxy-L-asparagine + succinate + CO2
-
 ?
1.14.11.16 peptide L-aspartate + 2-oxoglutarate + O2
-
 Bos taurus peptide 3-hydroxy-L-aspartate + succinate + CO2
-
 ?