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Literature summary extracted from

  • Vaaler, G.L.; Snell, E.E.
    Pyridoxal 5'-phosphate dependent histidine decarboxylase: overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues (1989), Biochemistry, 28, 7306-7313.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.22 expression in Escherichia coli Morganella morganii

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.22 H231F mutant enzymes His231Phe and His231Arg are inactive Morganella morganii
4.1.1.22 H231N mutant enzyme His231Asn is 0.2% as active as the wild-type enzyme Morganella morganii
4.1.1.22 H231Q mutant His231Gln is 12% as active as the wild-type enzyme Morganella morganii
4.1.1.22 H231R mutant enzymes His231Phe and His231Arg are inactive Morganella morganii
4.1.1.22 K232A mutant enzyme Lys232Ala is inactive but retains ability to bind both pyridoxal 5'-phosphate and His efficiently Morganella morganii
4.1.1.22 additional information none of the four residues Met233, Cys230, Cys239 and Ser322 are essential for activity, altough all replacements reduce the activity of the enzyme significantly Morganella morganii
4.1.1.22 S229A mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme Morganella morganii
4.1.1.22 S229C mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme Morganella morganii

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.22 Morganella morganii
-
-
-
4.1.1.22 Morganella morganii AM-15
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.22
-
 Morganella morganii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.22 L-His
-
 Morganella morganii Histamine + CO2
-
 ?
4.1.1.22 L-His
-
 Morganella morganii AM-15 Histamine + CO2
-
 ?