4.1.1.18: lysine decarboxylase
This is an abbreviated version!
For detailed information about lysine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.18
-
4.1.1.18
-
ornithine
-
urease
-
aeromonas
-
dihydrolase
-
decarboxylases
-
voges-proskauer
-
dna-dna
-
esculin
-
non-motile
-
cadba
-
salicin
-
1,5-diaminopentane
-
d-mannitol
-
melibiose
-
dulcitol
-
ruminantium
-
adonitol
-
selenomonas
-
sobria
-
enteroinvasive
-
d-sorbitol
-
carbenicillin
-
cephalothin
-
corrodens
-
simmons
-
alvei
-
macconkey
-
quinolizidine
-
hafnia
-
eikenella
-
huperzia
-
d-arabitol
-
4.1.1.17
-
synthesis
-
medicine
- 4.1.1.18
- ornithine
- urease
- aeromonas
-
dihydrolase
- decarboxylases
-
voges-proskauer
-
dna-dna
- esculin
-
non-motile
-
cadba
- salicin
- 1,5-diaminopentane
- d-mannitol
- melibiose
- dulcitol
- ruminantium
- adonitol
-
selenomonas
- sobria
-
enteroinvasive
- d-sorbitol
- carbenicillin
- cephalothin
- corrodens
-
simmons
- alvei
-
macconkey
-
quinolizidine
-
hafnia
- eikenella
- huperzia
- d-arabitol
-
4.1.1.17
- synthesis
- medicine
Reaction
Synonyms
AsLdc, CadA, constitutive LDCc, constitutive lysine decarboxylase, DesA, EcLDCc, ECORLD, gtLDC, inducible lysine decarboxylase, L-Lys-OD, L-lysine decarboxylase, LDC, ldcC, LdcI, LdcI/CadA, LysA, lysine decarboxylase, MaLDC, multimeric lysine decarboxylase, SrLDC, VSAL_I2491
ECTree
4.1.1.18 lysine decarboxylaseAdvanced search results
results (
results (General Information
General Information on EC 4.1.1.18 - lysine decarboxylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
physiological function
additional information
evolution
certain enterobacteria exert evolutionary pressure on the lysine decarboxylase towards the macromolecular cage-like assembly with AAA+ ATPase RavA, implying that this complex may have an important function under particular stress conditions. The C-terminal beta-sheet of a lysine decarboxylase is a highly conserved signature allowing to distinguish between LdcI and LdcC. RavA is binding to LdcI, but is not capable of binding to LdcC, LDC sequence comparisons and phylogenetic analysis
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
evolution
the L-lysine decarboxylase (LDC) genes from Escherichia coli include genes cadA and ldcC encoding the acid-inducible enzyme CadA and the constitutive LDCc, respectively
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)
physiological function
enzyme is involved in NRPS-independent siderophore biosynthesis
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
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
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
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
physiological function
-
enzyme is involved in NRPS-independent siderophore biosynthesis
-
physiological function
Ligilactobacillus saerimneri 30a ATCC 33222
-
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
-
additional information
-
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
additional information
construction of a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and yo-electron microscopy 3D reconstructions of the Escherichia coli LdcI and LdcC at optimal pH, overview. RavA is not capable of binding to LdcC. Conformational rearrangements in the enzyme LdcI active site, overview
additional information
construction of a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and yo-electron microscopy 3D reconstructions of the Escherichia coli LdcI and LdcC at optimal pH, overview. RavA is not capable of binding to LdcC. Conformational rearrangements in the enzyme LdcI active site, overview
additional information
-
construction of a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and yo-electron microscopy 3D reconstructions of the Escherichia coli LdcI and LdcC at optimal pH, overview. RavA is not capable of binding to LdcC. Conformational rearrangements in the enzyme LdcI active site, overview
additional information
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
additional information
-
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
additional information
Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC
additional information
Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC
additional information
-
Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC
additional information
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
-
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
structure of enzyme SrLDC in complex with pyridoxal 5'-phosphate and cadaverine and binding mode of cofactor and substrate, overview
additional information
-
structure of enzyme SrLDC in complex with pyridoxal 5'-phosphate and cadaverine and binding mode of cofactor and substrate, overview
additional information
-
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
additional information
Escherichia coli K-12 / MG1655
-
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
-
additional information
Hafnia alvei AS1.1009
-
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
-
