A pyridoxal 5'-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae . The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro .
A pyridoxal 5'-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae [1]. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro [3].
the Campylobacter jejuni enzyme is a carboxyspermidine decarboxylase and not a carboxynorspermidine decarboxylase in vivo and is essential for spermidine biosynthesis
the Campylobacter jejuni enzyme is a carboxyspermidine decarboxylase and not a carboxynorspermidine decarboxylase in vivo and is essential for spermidine biosynthesis
75% and 51% of the maximum activity remains at 30°C and 45°C, respectively, but the activity decreases rapidly at temperatures above 55°C or below 20°C
carboxynorspermidine decarboxylase (NspC) levels inversely regulate biofilm and motility and implicate the presence of an effective feedback mechanism maintaining norspermidine homeostasis in Vibrio cholerae. High levels of NspC enhances growth, biofilm formation with 5fold increase in biofilm cell density, and vps gene transcription and decreases motility. Increased NspC levels do not lead to increases in intracellular norspermidine production
a deletion mutant shows severe growth defects in minimal medium and a severe biofilm deficiency. Exogenous spermidine and norspermidine restore prototrophic growth for CASDC mutants, but only spermidine inhibits biofilm formation. The CASDC mutants accumulate homospermidine via a homospermidine synthase homologue
Deletion of the gene encoding carboxyspermidine decarboxylase results in the depletion of spermidine and loss of decarboxylase activity. The deletion strain also shows growth defects in polyamine-free growth medium
identification of a spermidine retroconversion activity in bacteria, producing diamine putrescine from triamine spermidine. When spermidine levels are pharmacologically decreased, synthesis of spermine from spermidine is induced via carboxyspermidine dehydrogenase and carboxyspermidine decarboxylase which produce spermidine from putrescine. A strain lacking carboxyspermidine decarboxylase activity accumulates carboxyspermidine, some putrescine and a small amount of homospermidine
carboxynorspermidine decarboxylase (NspC) levels inversely regulate biofilm and motility and implicate the presence of an effective feedback mechanism maintaining norspermidine homeostasis in Vibrio cholerae. High levels of NspC enhances growth, biofilm formation with 5fold increase in biofilm cell density, and vps gene transcription and decreases motility. Increased NspC levels do not lead to increases in intracellular norspermidine production
Deletion of the gene encoding carboxyspermidine decarboxylase results in the depletion of spermidine and loss of decarboxylase activity. The deletion strain also shows growth defects in polyamine-free growth medium
identification of a spermidine retroconversion activity in bacteria, producing diamine putrescine from triamine spermidine. When spermidine levels are pharmacologically decreased, synthesis of spermine from spermidine is induced via carboxyspermidine dehydrogenase and carboxyspermidine decarboxylase which produce spermidine from putrescine. A strain lacking carboxyspermidine decarboxylase activity accumulates carboxyspermidine, some putrescine and a small amount of homospermidine
a deletion mutant shows severe growth defects in minimal medium and a severe biofilm deficiency. Exogenous spermidine and norspermidine restore prototrophic growth for CASDC mutants, but only spermidine inhibits biofilm formation. The CASDC mutants accumulate homospermidine via a homospermidine synthase homologue
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing the purified preparation results in almost complete loss of activity. A substantial loss of activity (about 20%) is observed when the enzyme is dialysed for 12 h or stored at 4°C for 2 days without addition of EDTA
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Sephacryl S-200 gel filtration, and hydroxyapatite column chromatography. The enzyme is greatly stabilized by the addition of both dithiothreitol and EDTA, but not pyridoxal 5'-phosphate, during purification
Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine
Sakanaka, M.; Sugiyama, Y.; Kitakata, A.; Katayama, T.; Kurihara, S.
Carboxyspermidine decarboxylase of the prominent intestinal microbiota species Bacteroides thetaiotaomicron is required for spermidine biosynthesis and contributes to normal growth