ISSN:
1432-072X
Keywords:
Key wordsl-2
;
4-Diaminobutyrate decarboxylase
;
Acinetobacter baumannii
;
Nucleotide sequence
;
1
;
3-Diaminopropane
;
Pyridoxal 5′-phosphate enzyme
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The gene (ddc) encoding a novel enzyme, l-2,4-diaminobutyrate decarboxylase (DABA-DC; EC 4.1.1.-) in Acinetobacter baumannii was sequenced, and an open reading frame of 1,530 nucleotides was detected. The sequence of 20 N-terminal amino acids of purified DABA-DC and of its proteolytic peptide fragments coincided with those deduced from the nucleotide 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 putative pyridoxal 5′-phosphate-binding domain.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002030050366
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