EC Number   |
General Information |
Reference |
|---|
    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 | physiological function |
enzyme is involved in NRPS-independent siderophore biosynthesis |
-, 728330 |
| 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 |
lysine decarboxylase (LDC) is an important enzyme for maintenance of pH homeostasis and the biosynthesis of cadaverine. Most of bacteria utilize acid stress-induced lysine decarboxylase in the response to the environmental acid stress |
749101 |
| 4.1.1.18 | physiological function |
lysine decarboxylase MaLDC is involved in the biosynthesis of DNJ alkaloids. 1-Deoxynojirimycin (DNJ) is the main bioactive compound of Morus alba and has pharmacological effects in humans, including blood sugar level regulation and antiviral activity. The enzyme expression is correlated with DNJ content in leaves |
749226 |
| 4.1.1.18 | physiological function |
the inducible lysine decarboxylase LdcI (or CadA) is an important enterobacterial acid stress response enzyme whereas constitutive lysine decarboxylase LdcC is its close paralogue, thought to play mainly a metabolic role. Escherichia coli AAA+ ATPase RavA, involved in multiple stress response pathways, tightly interacts with enzyme LdcI. A unique macromolecular cage is formed by two decamers (two double pentameric rings) of the Escherichia coli LdcI and five hexamers of the AAA+ ATPase RavA (UniProt ID P31473) counteracting acid stress under starvation. LdcI is bound to the LARA domain of RavA |
749315 |
