EC Number   |
General Information |
Reference  |
|---|
    4.1.1.18 | physiological function |
inducible lysine decarboxylase, LdcI/CadA, together with the inner-membrane lysine-cadaverine antiporter, CadB, provide cells with protection against mild acidic conditions (about pH 5.0) |
714832 |
| 4.1.1.18 | physiological function |
Lactobacillus saerimneri 30a contains a three-component decarboxylation system consisting of ornithine decarboxylase, lysine decarboxylase and a transporter catalyzing both lysine/cadaverine and ornithine/putrescine exchange |
-, 727766 |
| 4.1.1.18 | physiological function |
enzyme is involved in NRPS-independent siderophore biosynthesis |
-, 728330 |
| 4.1.1.18 | more |
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview |
-, 746801 |
| 4.1.1.18 | more |
the LDC monomer has a C-terminal domain (residues 564-715), that has a predominantly alpha-helical outer surface and an inner surface that consists of two sets of beta-sheets, and is very important. The C-terminal domain forms part of the entry channel into the active site of the enzyme. The amino acid change E583G changes a residue located in this channel with improving effects on enzyme activity |
-, 747358 |
| 4.1.1.18 | metabolism |
changes in the contents of plant biogenic amines (putrescine, cadaverine, spermidine, tryptamine, spermine and histamine) and key enzymes of their biosynthesis, i.e. lysine decarboxylase (LDC), tyrosine decarboxylase, and ornithine decarboxylase (ODC) in galls and other parts of Siberian elm (Ulmus pumila) leaves during the galling process caused by the aphid Tetraneura ulmi first instar larvae, overview |
747444 |
| 4.1.1.18 | more |
compared to the activity of lysine/ornithine decarboxylase from Selenomonas ruminantium and from Vibrio vulnificus, the cadaverine producing activity of enzyme gtLDC is severalfold reduced |
748513 |
| 4.1.1.18 | more |
structure of enzyme SrLDC in complex with pyridoxal 5'-phosphate and cadaverine and binding mode of cofactor and substrate, overview |
749097 |
| 4.1.1.18 | evolution |
Selenomonas ruminantium SrLDC shows much lower pyridoxal 5'-phosphate affinity than other pyridoxal 5'-phosphate-dependent enzymes. The highly flexible active site contributes to the low affinity for pyridoxal 5'-phosphate in SrLDC |
749101 |
| 4.1.1.18 | more |
due to the flexible pyridoxal 5'-phosphate binding site, the protein undergoes an open/closed conformational change at the PLP binding site depending on the pyridoxal 5'-phosphate binding. Especially, two loops located in the vicinity of the pyridoxal 5'-phosphate binding site, the pyridoxal 5'-phosphate stabilization loop (PS-loop) and the regulatory loop (R-loop), undergo a significant structural movement depending on the pyridoxal 5'-phosphate binding |
749101 |
