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Literature summary for 4.1.1.18 extracted from

  • Kandiah, E.; Carriel, D.; Perard, J.; Malet, H.; Bacia, M.; Liu, K.; Chan, S.W.; Houry, W.A.; Ollagnier de Choudens, S.; Elsen, S.; Gutsche, I.
    Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA (2016), Sci. Rep., 6, 24601 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
gene ldcI, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3) Escherichia coli

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Escherichia coli
-
 cadaverine + CO2
-
 ?
additional information Escherichia coli 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9H3
-
-
Escherichia coli P52095
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography, dialysis, and tag cleavage through TEV protease, followed by another step of nickel affinity chromatography, and gel filtration Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
CadA
-
 Escherichia coli
constitutive lysine decarboxylase
-
 Escherichia coli
inducible lysine decarboxylase
-
 Escherichia coli
ldcC
-
 Escherichia coli
LdcI
-
 Escherichia coli

Cofactor

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

General Information

General Information Comment Organism
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 Escherichia coli
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 Escherichia coli
additional information Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC Escherichia coli
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 Escherichia coli