4.1.1.18	L-Lys	-	
4.1.1.18	L-Lys	constitutive enzyme is involved in synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth	
4.1.1.18	L-Lys	inducible enzyme	
4.1.1.18	L-Lys	enzyme activity is positively correlated with the chlorophyll content during leaf regreening. The enzyme is an integrated part of the alkaloid specific biosynthetic sequence	
4.1.1.18	L-Lys	the enzyme is produced constitutively	
4.1.1.18	L-lysine	-	
4.1.1.18	L-lysine	CadA protects Escherichia coli starved of phosphate against fermentation acids in the host gut, the tolerance of the starved cells to fermentation acids is markedly increased as a result of the activity of the inducible CadBA lysine-dependent acid resistance system, independent of expression of the RpoS regulon, overview	
4.1.1.18	additional information	optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0	
4.1.1.18	additional information	the cofactor pyridoxal 5'-phosphate-dependent decarboxylation of the amino acid into a polyamine is catalysed in a multistep reaction that consumes a cytoplasmic proton and produces a CO2 molecule passively diffusing out of the cell, while the polyamine is excreted by the antiporter in exchange for a new amino acid substrate	
4.1.1.18	additional information	when used for whole-cell biotransformation of L-lysine to cadaverine at pH 7.5, 37°C, recombinant AsLdc in Escherichia coli cells completes the transformation within 7 h	
4.1.1.18	additional information	whole-cell bioconversion by Klebsiella pneumoniae lysine decaarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells