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Literature summary for 4.1.1.18 extracted from

  • Kanjee, U.; Gutsche, I.; Alexopoulos, E.; Zhao, B.; El Bakkouri, M.; Thibault, G.; Liu, K.; Ramachandran, S.; Snider, J.; Pai, E.F.; Houry, W.A.
    Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase (2011), EMBO J., 30, 931-944.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.18

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
L89R the mutant elutes at the expected position for an LdcI dimer (about 150000 Da), the mutant shows about 5fold lower level of activity than wild type and this activity is not inhibited by ppGpp Escherichia coli
R206S the ppGpp-binding site mutant shows wild type oligomerisation profile, the mutant is insensitive to the addition of ppGpp and has activity comparable to wild type LdcI in the absence of ppGpp Escherichia coli
R97A the ppGpp-binding site mutant shows wild type oligomerisation profile, the mutant is insensitive to the addition of ppGpp and has activity comparable to wild type LdcI in the absence of ppGpp Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
GDP
-
 Escherichia coli
GTP
-
 Escherichia coli
additional information at pH values lower than 5.0, there is no effect of ppGpp, pppGpp, GDP and GTP on LdcI activity Escherichia coli
ppGpp addition of ppGpp at low salt concentrations (25-135 mM NaCl depending on the buffer) results in a dramatic inhibition of LdcI activity of about 10fold at pH values higher than 5.0 Escherichia coli
pppGpp inhibits LdcI only at pH values higher than 6.5 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.42
-
 L-lysine at pH 6.5, between 4°C and 10°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Escherichia coli 5737
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9H3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
 Escherichia coli cadaverine + CO2
-
 ?

Subunits

Subunits Comment Organism
decamer the protein is an oligomer of five dimers that associate to form a decamer, X-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
inducible lysine decarboxylase
-
 Escherichia coli
LdcI/CadA
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
30
-
 L-lysine at pH 6.5, between 4°C and 10°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0002377
-
 ppGpp uncompetitive inhibition, at pH 6.5, between 4°C and 10°C Escherichia coli
0.000374
-
 ppGpp noncompetitive inhibition, at pH 6.5, between 4°C and 10°C Escherichia coli
0.002791
-
 ppGpp mixed type inhibition, at pH 6.5, between 4°C and 10°C Escherichia coli

General Information

General Information Comment Organism
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) Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
71
-
 L-lysine at pH 6.5, between 4°C and 10°C Escherichia coli