Open AccessMultiple evolutionary origin of pyridoxal‐5′‐phosphate‐dependent amino acid decarboxylases
Author(s) -
SANDMEIER Erika,
HALE Terence I.,
CHRISTEN Philipp
Publication year - 1994
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1994.tb18816.x
Subject(s) - histidine decarboxylase , biochemistry , arginine decarboxylase , pyridoxal phosphate , arginine , amino acid , pyridoxal , lysine , enzyme , lysine decarboxylase , glutamate decarboxylase , carboxy lyases , aromatic l amino acid decarboxylase , biology , ornithine decarboxylase , decarboxylation , ornithine , histidine , cofactor , putrescine , cadaverine , catalysis
Comparison of the amino acid sequences of nine different pyridoxal‐5′‐phosphate‐dependent amino acid decarboxylases indicated that they can be subdivided into four different groups that seem to be evolutionarily unrelated to each other. Group I is represented by glycine decarboxylase, a component of a multienzyme system; group II comprises glutamate, histidine, tyrosine, and aromatic‐ l ‐amino‐acid decarboxylases; group III, procaryotic ornithine and lysine decarboxylase as well as the procaryotic biodegradative type of arginine decarboxylase; group IV, eucaryotic ornithine and arginine decarboxylase as well as the procaryotic biosynthetic type of arginine decarboxylase and diaminopimelate decarboxylase. ( N –1) profile analysis, a more stringent application of profile analysis, established the homology among the enzymes of each group. A search with the profile of group II indicated a distant relationship with aminotransferases and thus with the α family of pyridoxal‐5′‐phosphate‐dependent enzymes. No evidence was obtained that groups I, III and IV were related with other pyridoxal‐5′‐phosphate‐dependent enzymes or any other protein in the databse. Unlike the aminotransferases, which, with few possible exceptions, costitute a single group of homologous proteins, the amino acid decarboxylases, by the criterion of profile analysis, have evolved along multiple lineages, in some cases even if they have the same substrate specificity.