|PROSITE documentation PDOC00585|
Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [1,2]. The first family consists of:
One of the regions of sequence similarity contains a conserved lysine residue which is known, in Escherichia coli LDC  and in ADC , to be the site of attachment of the pyridoxal-phosphate group. We have used this region as a signature pattern.
These enzymes are collectively known as group III decarboxylases .Last update:
November 1997 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|Source||Unpublished observations (1993).|
|2||Authors||Sandmeier E., Hale T.I., Christen P.|
|Source||Eur. J. Biochem. 221:997-1002(1994).|
|3||Authors||Meng S.-Y., Bennett G.N.|
|Title||Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH.|
|Source||J. Bacteriol. 174:2659-2669(1992).|
|4||Authors||Stim K.P., Bennett G.N.|
|Title||Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli.|
|Source||J. Bacteriol. 175:1221-1234(1993).|