OCCURRENCE OF A NOVEL L-2,4-DIAMINOBUTYRATE DECARBOXYLASE ACTIVITY INSOME SPECIES OF ENTEROBACTERIACEAE, AND PURIFICATION AND CHARACTERIZATION OF THE ENZYMES OF ENTEROBACTER-AEROGENES AND SERRATIA-MARCESCENS
S. Yamamoto et al., OCCURRENCE OF A NOVEL L-2,4-DIAMINOBUTYRATE DECARBOXYLASE ACTIVITY INSOME SPECIES OF ENTEROBACTERIACEAE, AND PURIFICATION AND CHARACTERIZATION OF THE ENZYMES OF ENTEROBACTER-AEROGENES AND SERRATIA-MARCESCENS, Biological & pharmaceutical bulletin, 19(10), 1996, pp. 1298-1303
L-2,4-Diaminobutyrate decarboxylase (DABA DC) is a novel enzyme yieldi
ng 1,3-diaminopropane (DAP) from DABA, which has previously been purif
ied from strains of the genera Vibrio and Acinetobacter. In this study
, we also detected DABA DC activity in the species of Enterobacteriace
ae: E. aerogenes, E. cloacae, E. agglomerans, Serratia marcescens, S.
liquefaciens, Klebsiella pneumoniace, K. oxytoca and Citrobacter freun
dii, all of which produced DAP in sufficient amounts. Subsequently, th
e DABA DCs of E. aerogenes and S. marcescens were purified to homogene
ity and characterized. Two separate enzymes had similar properties wit
h respect to chromatographic behaviors, and were a dimer with subunits
of identical molecular mass of about 51 kDa. The maximal activity of
each enzyme was obtained at pH 8.0-8.25. Both enzymes required pyridox
al 5'-phosphate and Mg2+ for full activity, and were highly specific f
or L-DABA. There was immunological similarity, but not identity betwee
n these proteins, as determined by Ouchterlony double diffusion analys
is with antiserum against the E. aerogenes DABA DC. They showed the sa
me N-terminal amino acid sequence up to the 8th residue (S-K-L-N-P-I-L
-A-). These enzymes were different in molecular mass, N-terminal amino
acid sequence and antigenicity from DABA DCs of Acientobacter and Vib
rio species.