SEQUENCE-ANALYSIS OF THE GENE ENCODING A NOVEL L-2,4-DIAMINOBUTYRATE DECARBOXYLASE OF ACINETOBACTER-BAUMANNII - SIMILARITY TO THE GROUP-II AMINO-ACID DECARBOXYLASES
H. Ikai et S. Yamamoto, SEQUENCE-ANALYSIS OF THE GENE ENCODING A NOVEL L-2,4-DIAMINOBUTYRATE DECARBOXYLASE OF ACINETOBACTER-BAUMANNII - SIMILARITY TO THE GROUP-II AMINO-ACID DECARBOXYLASES, Archives of microbiology, 166(2), 1996, pp. 128-131
The gene (ddc) encoding a novel enzyme, L-2,4-diaminobutyrate decarbox
ylase (DABA-DC; EC 4.1.1-) in Acinetobacter baumannii was sequenced, a
nd an open reading frame of 1,530 nucleotides was detected. The sequen
ce of 20 N-terminal amino acids of purified DABA-DC and of its proteol
ytic peptide fragments coincided with those deduced from the nucleotid
e sequence determined. Comparison of the predicted amino acid sequence
of the A. baumannii enzyme with those of other pyridoxal 5'-phosphate
-dependent decarboxylases revealed significant similarity to the group
II amino acid decarboxylases and conservation of the group II amino a
cid decarboxylases and conservation of the putative pyridoxal 5'-phosp
hate-binding domain.