Cloning and characterization of the ddc homolog encoding L-2,4- diaminobutyrate decarboxylase in Enterobacter aerogenes

Shigeo Yamamoto; Nobuo Mutoh; Daisuke Tsuzuki; Hisato Ikai; Hiroshi Nakao; Sumio Shinoda; Shizuo Narimatsu; Shin Ichi Miyoshi

doi:10.1248/bpb.23.649

Cloning and characterization of the ddc homolog encoding L-2,4- diaminobutyrate decarboxylase in Enterobacter aerogenes

Shigeo Yamamoto, Nobuo Mutoh, Daisuke Tsuzuki, Hisato Ikai, Hiroshi Nakao, Sumio Shinoda, Shizuo Narimatsu, Shin Ichi Miyoshi

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

L-2,4-Diaminobutyrate decarboxylase (DABA DC) catalyzes the formation of 1,3-diaminopropane (DAP) from DABA. In the present study, the ddc gene encoding DABA DC from Enterobacter aerogenes ATCC 13048 was cloned and characterized. Determination of the nucleotide sequence revealed an open reading frame of 1470 hp encoding a 53659-Da protein of 490 amino acids, whose deduced NH₂-terminal sequence was identical to that of purified DABA DC from E. aerogenes. The deduced amino acid sequence was highly similar to those of Acinetobacter baumannii and Haemophilus influenzae DABA DCs encoded by the ddc genes. The lysine-307 of the E. aerogenes DABA DC was identified as the pyridoxal 5'-phosphate binding residue by site-directed mutagenesis. Furthermore, PCR analysis revealed the distribution of E. aerogenes ddc homologs in some other species of Enterobacteriaceae. Such a relatively wide occurrence of the ddc homologs implies biological significance of DABA DC and its product DAP.

Original language	English
Pages (from-to)	649-653
Number of pages	5
Journal	Biological and Pharmaceutical Bulletin
Volume	23
Issue number	5
DOIs	https://doi.org/10.1248/bpb.23.649
Publication status	Published - May 2000

Keywords

Diaminobutyrate decarboxylase
E. aerogenes
Enterobacteriaceae
Gene cloning

ASJC Scopus subject areas

Pharmacology
Pharmaceutical Science

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Cloning and characterization of the ddc homolog encoding L-2,4- diaminobutyrate decarboxylase in Enterobacter aerogenes. / Yamamoto, Shigeo; Mutoh, Nobuo; Tsuzuki, Daisuke; Ikai, Hisato; Nakao, Hiroshi; Shinoda, Sumio; Narimatsu, Shizuo; Miyoshi, Shin Ichi.

In: Biological and Pharmaceutical Bulletin, Vol. 23, No. 5, 05.2000, p. 649-653.

Research output: Contribution to journal › Article › peer-review

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abstract = "L-2,4-Diaminobutyrate decarboxylase (DABA DC) catalyzes the formation of 1,3-diaminopropane (DAP) from DABA. In the present study, the ddc gene encoding DABA DC from Enterobacter aerogenes ATCC 13048 was cloned and characterized. Determination of the nucleotide sequence revealed an open reading frame of 1470 hp encoding a 53659-Da protein of 490 amino acids, whose deduced NH2-terminal sequence was identical to that of purified DABA DC from E. aerogenes. The deduced amino acid sequence was highly similar to those of Acinetobacter baumannii and Haemophilus influenzae DABA DCs encoded by the ddc genes. The lysine-307 of the E. aerogenes DABA DC was identified as the pyridoxal 5'-phosphate binding residue by site-directed mutagenesis. Furthermore, PCR analysis revealed the distribution of E. aerogenes ddc homologs in some other species of Enterobacteriaceae. Such a relatively wide occurrence of the ddc homologs implies biological significance of DABA DC and its product DAP.",

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