A new enzyme activity, which catalyzes decarboxylation of l-2,4-diaminobutyric acid (DABA) to yield 1,3-diaminopropane (DAP), has been found in dialyzed crude extracts prepared from Vibrio alginolyticus. The pH optimum for the activity was 8.0-8.5, and the enzyme showed a pyridoxal 5′-phosphate (PLP) requirement. Mg2+ caused about 30% stimulation in activity. The enzyme was active to only l-DABA among the diamino acids examined, and the Km value for l-DABA was 0.13 mM. Ammonium sulfate fractionation of a dialyzed crude extract followed by HPLC separation allowed us to conclude that this enzyme differed from the decarboxylase which occurs in Vibrio spp. to produce norspermidine (Nspd) for carboxynorspermidine (C-Nspd) having a moiety similar in structure to DABA. The same enzyme activity was detected in several other Vibrio species.
|Number of pages||5|
|Journal||FEMS Microbiology Letters|
|Publication status||Published - Jul 1986|
- Pyridoxal 5′-phosphate-dependent enzyme
- precursor of norspermidine
ASJC Scopus subject areas
- Molecular Biology