Information on EC 4.1.1.18 - Lysine decarboxylase:
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The expected taxonomic range for this enzyme is: Magnoliophyta

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EC NUMBERCOMMENTARY
4.1.1.18-

RECOMMENDED NAMEGeneOntology No.
Lysine decarboxylaseGO:0008923

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-lysine = cadaverine + CO2
show the reaction diagram		----
L-lysine = cadaverine + CO2
show the reaction diagram		reaction proceeds with retention of configuration at C-2, stereochemistryBacterium cadaveris, Bacterium cadaveris KY3402-37296

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
decarboxylation----

PATHWAYKEGG LinkMetaCyc Link
aminopropylcadaverine biosynthesis-PWY0-1303
Biosynthesis of secondary metabolites01110 -
bisucaberin biosynthesis-PWY-6381
desferrioxamine B biosynthesis-PWY-6376
desferrioxamine E biosynthesis-PWY-6375
lupanine biosynthesis-PWY-5468
Lysine degradation00310 -
lysine degradation I-PWY0-461
lysine degradation X-PWY-6328
Metabolic pathways01100 -
Tropane, piperidine and pyridine alkaloid biosynthesis00960 -

SYSTEMATIC NAMEIUBMB Comments
L-lysine carboxy-lyase (cadaverine-forming)A pyridoxal-phosphate protein. Also acts on 5-hydroxy-L-lysine.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
CadAVibrio vulnificus, Vibrio vulnificus CYK279H, Vibrio vulnificus MO6-24/O--680477
CadAEscherichia coli--680484, 690597
CadASalmonella enterica subsp. enterica serovar Typhimurium--704086
inducible lysine decarboxylaseEscherichia coli--690269, 714832, 716768
L-lysine decarboxylaseBacterium cadaveris, Bacterium cadaveris KY3402--715142
LDC----
LDCSelenomonas ruminantium--654982
LDCGlycine max--690395
LDCTriticum aestivum x Secale cereale--713611
LDCBacterium cadaveris, Bacterium cadaveris KY3402--715142
LdcIEscherichia coli--690269
LdcI/CadAEscherichia coli--714832, 716768
lysine decarboxylaseThalassobius aestuarii, Thalassobius aestuarii JC2049--698370

CAS REGISTRY NUMBERCOMMENTARY
9024-76-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Anchusa italica-37288--Manually annotated by BRENDA team
Arum maculatum-37288--Manually annotated by BRENDA team
Asarum maculatum-37288--Manually annotated by BRENDA team
Astragalus cicer-37288--Manually annotated by BRENDA team
Astragalus glycyphyllos-37288--Manually annotated by BRENDA team
Atropa belladonna-37288--Manually annotated by BRENDA team
Bacterium cadaveris-37294, 37295, 37296, 37298, 715142--Manually annotated by BRENDA team
Baptisia australiswild indigo37288--Manually annotated by BRENDA team
Calla palustris-37288--Manually annotated by BRENDA team
Chenopodium rubrum-37288--Manually annotated by BRENDA team
Conium maculatum-37288--Manually annotated by BRENDA team
Cytisus beanii-37288--Manually annotated by BRENDA team
Cytisus canariensis-37288--Manually annotated by BRENDA team
Cytisus scoparius-37288--Manually annotated by BRENDA team
Dictamnus albus-37288--Manually annotated by BRENDA team
Eikenella corrodens-656712--Manually annotated by BRENDA team
Escherichia coli-37286, 37292, 665713, 716768--Manually annotated by BRENDA team
Escherichia coli-690269, 714832P0A9H3UniProtManually annotated by BRENDA team
Escherichia coli2 enzyme form, one is encoded by the gen cadA and the other by the gene ldc37299--Manually annotated by BRENDA team
Escherichia colistrain B37289, 37293--Manually annotated by BRENDA team
Escherichia colistrain K-12690597--Manually annotated by BRENDA team
Escherichia coliwild-type strain MG1655, gene cadA680484--Manually annotated by BRENDA team
Galega officinalis-37288--Manually annotated by BRENDA team
Genista anglica-37288--Manually annotated by BRENDA team
Genista hispanica-37288--Manually annotated by BRENDA team
Genista lydia-37288--Manually annotated by BRENDA team
Genista pilosa-37288--Manually annotated by BRENDA team
Genista sagittalis-37288--Manually annotated by BRENDA team
Genista tinctoria-37288--Manually annotated by BRENDA team
Glycine max-37288, 37297--Manually annotated by BRENDA team
Glycine maxcultivar Sakai690395--Manually annotated by BRENDA team
Glycyrrhiza echinata-37288--Manually annotated by BRENDA team
Hafnia alvei-37283, 37285--Manually annotated by BRENDA team
Heimia salicifolia-37284--Manually annotated by BRENDA team
Laburnum alpinum-37288--Manually annotated by BRENDA team
Laburnum anagyroides-37288--Manually annotated by BRENDA team
Levisticum officinale-37288--Manually annotated by BRENDA team
Lupinus albus-37288--Manually annotated by BRENDA team
Lupinus luteus-37288--Manually annotated by BRENDA team
Lupinus polyphyllus-37288, 37291--Manually annotated by BRENDA team
Malva sylvestris-37288--Manually annotated by BRENDA team
Medicago sativa-37288--Manually annotated by BRENDA team
Melilotus albus-37288--Manually annotated by BRENDA team
Mentha suaveolens-37288--Manually annotated by BRENDA team
Menyanthes trifoliata-37288--Manually annotated by BRENDA team
Mus musculusall of the detectable lysine decarboxylase activity is due to the action of ornithine decarboxylase37301--Manually annotated by BRENDA team
Mycoplasma dispar-37287--Manually annotated by BRENDA team
Nicotiana tabacum-37288--Manually annotated by BRENDA team
no activity in Loktanella hongkongensis-698364--Manually annotated by BRENDA team
no activity in Marinovum algicola-698360--Manually annotated by BRENDA team
no activity in Marinovum algicola ATCC 51442-698360--Manually annotated by BRENDA team
no activity in Phaeobacter gallaeciensis BS107-698361--Manually annotated by BRENDA team
no activity in Rattus norvegicusall of the detectable lysine decarboxylase activity is due to the action of ornithine decarboxylase37301--Manually annotated by BRENDA team
no activity in Thalassobius mediterraneus-698370--Manually annotated by BRENDA team
no activity in Thalassobius mediterraneus XSM19-698370--Manually annotated by BRENDA team
no activity in Thalassococcus halodurans-698370--Manually annotated by BRENDA team
no activity in Thalassococcus halodurans UST050418-052-698370--Manually annotated by BRENDA team
Phaseolus vulgaris-37288--Manually annotated by BRENDA team
Pisum sativum-37288--Manually annotated by BRENDA team
Robinia pseudoacacia-37288--Manually annotated by BRENDA team
Ruta graveolens-37288--Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimuriumstrain CECT 443704086--Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium CECT 443strain CECT 443704086--Manually annotated by BRENDA team
Sanguisorba officinalis-37288--Manually annotated by BRENDA team
Saponaria officinalis-37288--Manually annotated by BRENDA team
Sedum acre-37288--Manually annotated by BRENDA team
Selenomonas ruminantium-37290, 654984--Manually annotated by BRENDA team
Selenomonas ruminantium-654982, 655829O50657SwissprotManually annotated by BRENDA team
Senecio fuchsii-37288--Manually annotated by BRENDA team
Sophora japonica-37288--Manually annotated by BRENDA team
Sophora tetraptera-37288--Manually annotated by BRENDA team
Spinacia oleracea-37288--Manually annotated by BRENDA team
Symphytum officinale-37288--Manually annotated by BRENDA team
Thalassobius aestuariiJC2049698370--Manually annotated by BRENDA team
Thalassobius aestuarii JC2049JC2049698370--Manually annotated by BRENDA team
Thermus thermophilusstrain HB8, isozymes TT1887, TT1465666850--Manually annotated by BRENDA team
Triticum aestivum x Secale cerealewinter triticale, cultivars Witon and Tornado713611--Manually annotated by BRENDA team
Trollius europaeus-37288--Manually annotated by BRENDA team
Valeriana sambucifolia-37288--Manually annotated by BRENDA team
Vibrio parahaemolyticusseveral acid adapted and nonadapted strains, gene cadA or VP2890680417Q87KT6UniProtManually annotated by BRENDA team
Vibrio parahaemolyticusstrain AQ 362737300--Manually annotated by BRENDA team
Vibrio parahaemolyticus AQ 3627strain AQ 362737300--Manually annotated by BRENDA team
Vibrio vulnificusgene cadA680477--Manually annotated by BRENDA team
Vicia faba-37288--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionEscherichia coli-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

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
delta-Hydroxylysine1,5-Diamino-2-hydroxypentane + CO2
show the reaction diagram		Bacterium cadaveris-at 35% of the activity with L-Lys37294, 37295---
delta-Hydroxylysine1,5-Diamino-2-hydroxypentane + CO2
show the reaction diagram		Vibrio parahaemolyticus-17% of the activity with L-Lys37300---
delta-Hydroxylysine1,5-Diamino-2-hydroxypentane + CO2
show the reaction diagram		Escherichia coli-25% of the activity with L-Lys37289, 37293---
L-LysCadaverine + CO2
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium--704086--?
L-LysCadaverine + CO2
show the reaction diagram		Phaseolus vulgaris, Vicia faba--37288-37288-
L-LysCadaverine + CO2
show the reaction diagram		Escherichia coli--37286-37286-
L-LysCadaverine + CO2
show the reaction diagram		Escherichia coli--37289-37289-
L-LysCadaverine + CO2
show the reaction diagram		Escherichia coli--37292-37292-
L-LysCadaverine + CO2
show the reaction diagram		Escherichia coli--37293-37293-
L-LysCadaverine + CO2
show the reaction diagram		Escherichia coli--37299-37299-
L-LysCadaverine + CO2
show the reaction diagram		Escherichia coli--690597--?
L-LysCadaverine + CO2
show the reaction diagram		Lupinus luteus, Spinacia oleracea, Pisum sativum, Nicotiana tabacum, Glycine max--37288-37288-
L-LysCadaverine + CO2
show the reaction diagram		Glycine max--37297-37297-
L-LysCadaverine + CO2
show the reaction diagram		Glycine max--690395--?
L-LysCadaverine + CO2
show the reaction diagram		Robinia pseudoacacia--37288-37288-
L-LysCadaverine + CO2
show the reaction diagram		Bacterium cadaveris--37294-37294-
L-LysCadaverine + CO2
show the reaction diagram		Bacterium cadaveris--37295-37295-
L-LysCadaverine + CO2
show the reaction diagram		Bacterium cadaveris--37296-37296-
L-LysCadaverine + CO2
show the reaction diagram		Bacterium cadaveris--37298-37298-
L-LysCadaverine + CO2
show the reaction diagram		Medicago sativa, Lupinus albus--37288-37288-
L-LysCadaverine + CO2
show the reaction diagram		Selenomonas ruminantium--37290-37290-
L-LysCadaverine + CO2
show the reaction diagram		Ruta graveolens, Glycyrrhiza echinata, Cytisus scoparius--37288-37288-
L-LysCadaverine + CO2
show the reaction diagram		Hafnia alvei--37283-37283-
L-LysCadaverine + CO2
show the reaction diagram		Hafnia alvei--37285-37285-
L-LysCadaverine + CO2
show the reaction diagram		Vibrio parahaemolyticus--37300-37300-
L-LysCadaverine + CO2
show the reaction diagram		Heimia salicifolia--37284-37284-
L-LysCadaverine + CO2
show the reaction diagram		Mycoplasma dispar--37287-37287-
L-LysCadaverine + CO2
show the reaction diagram		Lupinus polyphyllus--37288-37288-
L-LysCadaverine + CO2
show the reaction diagram		Lupinus polyphyllus--37291-37291-
L-LysCadaverine + CO2
show the reaction diagram		Baptisia australis, Cytisus beanii, Cytisus canariensis, Genista anglica, Genista hispanica, Genista lydia, Genista pilosa, Genista sagittalis, Genista tinctoria, Laburnum alpinum, Laburnum anagyroides, Sophora japonica, Sophora tetraptera, Astragalus cicer, Astragalus glycyphyllos, Galega officinalis, Melilotus albus, Levisticum officinale, Arum maculatum, Calla palustris, Asarum maculatum, Senecio fuchsii, Saponaria officinalis, Anchusa italica, Sedum acre, Menyanthes trifoliata, Mentha suaveolens, Malva sylvestris, Trollius europaeus, Sanguisorba officinalis, Dictamnus albus, Valeriana sambucifolia, Conium maculatum, Symphytum officinale, Chenopodium rubrum, Atropa belladonna--37288-37288-
L-LysCadaverine + CO2
show the reaction diagram		Selenomonas ruminantiumO50657-654982--?
L-LysCadaverine + CO2
show the reaction diagram		Escherichia coliP0A9H3-690269--?
L-LysCadaverine + CO2
show the reaction diagram		Selenomonas ruminantiumO50657constitutive enzyme is involved in synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth654982--?
L-LysCadaverine + CO2
show the reaction diagram		Selenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 0.69 in wild type enzyme, 1.0 in mutant enzyme A44V/G45T/V46P, 4.0 in mutant enzyme M50V/A52C/P54D/T55S, 0.64 in mutant enzyme M50V, 1.2 in mutant enzyme A52C, 1.8 in mutant enzyme P54D, 0.66 in mutant enzyme T55S, 1.9 in mutant enzyme M50V/A52C, 1.8 in mutant enzyme P54D/T55S, 2.6 in mutant enzyme A52C/P54D, 2.4 in mutant enzyme M50V/A52C/P54D and 2.7 in mutant enzyme A52C/P54D/T55S654984--?
L-LysCadaverine + CO2
show the reaction diagram		Selenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 0.83 for the wild-type enzyme655829--?
L-Lys?
show the reaction diagram		Escherichia coli-inducible enzyme37292, 37293---
L-Lys?
show the reaction diagram		Vibrio parahaemolyticus-inducible enzyme37300---
L-Lys?
show the reaction diagram		Lupinus polyphyllus-enzyme activity is positively correlated with the chlorophyll content during leaf regreening. The enzyme is an integrated part of the alkaloid specific biosynthetic sequence37288---
L-Lys?
show the reaction diagram		Selenomonas ruminantium-the enzyme is produced constitutively37290---
L-lysinecadaverine + CO2
show the reaction diagram		Escherichia coli--680484--?
L-lysinecadaverine + CO2
show the reaction diagram		Vibrio vulnificus--680477--?
L-lysinecadaverine + CO2
show the reaction diagram		Escherichia coli--714832--?
L-lysinecadaverine + CO2
show the reaction diagram		Bacterium cadaveris--715142cadaverine is 1,5-pentanediamine-?
L-lysinecadaverine + CO2
show the reaction diagram		Escherichia coli-CadA protects Escherichia coli starved of phosphate against fermentation acids in the host gut, the tolerance of the starved cells to fermentation acids is markedly increased as a result of the activity of the inducible CadBA lysine-dependent acid resistance system, independent of expression of the RpoS regulon, overview680484--?
L-lysinecadaverine + CO2
show the reaction diagram		Vibrio vulnificus MO6-24/O, Vibrio vulnificus CYK279H--680477--?
L-OrnPutrescine + CO2
show the reaction diagram		Selenomonas ruminantiumO50657-654982---
L-OrnPutrescine + CO2
show the reaction diagram		Selenomonas ruminantium--655829---
L-OrnPutrescine + CO2
show the reaction diagram		Selenomonas ruminantiumO50657-654982--?
L-OrnPutrescine + CO2
show the reaction diagram		Selenomonas ruminantium--655829--?
L-OrnPutrescine + CO2
show the reaction diagram		Selenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 0.69 in wild type enzyme, 1.0 in mutant enzyme A44V/G45T/V46P, 4.o in mutant enzyme M50V/A52C/P54D/T55S, 0.64 in mutant enzyme M50V, 1.2 in mutant enzyme A52C, 1.8 in mutant enzyme P54D, 0.66 in mutant enzyme T55S, 1.9 in mutant enzyme M50V/A52C, 1.8 in mutant enzyme P54D/T55S, 2.6 in mutant enzyme A52C/P54D, 2.4 in mutant enzyme M50V/A52C/P54D and 2.7 in mutant enzyme A52C/P54D/T55S654984--?
S-Aminoethyl-L-Cys1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
show the reaction diagram		Bacterium cadaveris-at 49% of the activity with L-Lys37294, 37295---
S-Aminoethyl-L-Cys1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
show the reaction diagram		Vibrio parahaemolyticus-23% of the activity with L-Lys37300---
S-Aminoethyl-L-Cys1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
show the reaction diagram		Escherichia coli-15% of the activity with L-Lys37289, 37293---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
L-LysCadaverine + CO2
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium--704086--
L-LysCadaverine + CO2
show the reaction diagram		Selenomonas ruminantiumO50657constitutive enzyme is involved in synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth654982--
L-Lys?
show the reaction diagram		Escherichia coli-inducible enzyme37292, 37293--
L-Lys?
show the reaction diagram		Vibrio parahaemolyticus-inducible enzyme37300--
L-Lys?
show the reaction diagram		Lupinus polyphyllus-enzyme activity is positively correlated with the chlorophyll content during leaf regreening. The enzyme is an integrated part of the alkaloid specific biosynthetic sequence37288--
L-Lys?
show the reaction diagram		Selenomonas ruminantium-the enzyme is produced constitutively37290--
L-lysinecadaverine + CO2
show the reaction diagram		Vibrio vulnificus--680477--
L-lysinecadaverine + CO2
show the reaction diagram		Escherichia coli-CadA protects Escherichia coli starved of phosphate against fermentation acids in the host gut, the tolerance of the starved cells to fermentation acids is markedly increased as a result of the activity of the inducible CadBA lysine-dependent acid resistance system, independent of expression of the RpoS regulon, overview680484--
L-lysinecadaverine + CO2
show the reaction diagram		Vibrio vulnificus MO6-24/O, Vibrio vulnificus CYK279H--680477--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
pyridoxal 5'-phosphateHafnia alvei, Hafnia alvei TPU 6440-contains 1 mol of pyridoxal 5'-phosphate per mol of subunit37283 2D-image
pyridoxal 5'-phosphateHeimia salicifolia--37284 2D-image
pyridoxal 5'-phosphateEscherichia coli-sequence of the pyridoxal 5'-phosphate binding site37292 2D-image
pyridoxal 5'-phosphateBacterium cadaveris, Bacterium cadaveris KY3402-contains 10 mol of pyridoxal 5'-phosphate per mol of enzyme37295 2D-image
pyridoxal 5'-phosphateVibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4-required as cofactor37300 2D-image
pyridoxal 5'-phosphateSelenomonas ruminantium--654982 2D-image
pyridoxal 5'-phosphateEscherichia coli-0.1 mM690269 2D-image
pyridoxal 5'-phosphateGlycine max, Glycine max L., Glycine max Williams 82--690395 2D-image
pyridoxal 5'-phosphateEscherichia coli--690597, 714832 2D-image
pyridoxal 5'-phosphateBacterium cadaveris, Bacterium cadaveris KY3402--715142 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,5-pentanediamineBacterium cadaveris, Bacterium cadaveris KY3402--715142 2D-image
6-AminohexanoateVibrio parahaemolyticus--37300 2D-image
alpha-difluoromethyl-lysineGlycine max-LCD suicide inhibitor, 74% inhibition at 1 mM690395 2D-image
alpha-DifluoromethylcadaverineVibrio parahaemolyticus--37300 2D-image
alpha-MonofluoromethylcadaverineVibrio parahaemolyticus--37300 2D-image
alpha-TrifluoromethylcadaverineVibrio parahaemolyticus--37300 2D-image
alpha-VinyllysineGlycine max--37297 2D-image
Br-Glycine max--37297 2D-image
Ca2+Heimia salicifolia--37284 2D-image
CaCl2Glycine max--37297 2D-image
cadaverineGlycine max--37297 2D-image
Cl-Glycine max--37297 2D-image
diethyldithiocarbamic acidHeimia salicifolia--37284 2D-image
DL-alpha-DifluoromethyllysineMycoplasma dispar--37287 2D-image
DL-alpha-DifluoromethyllysineSelenomonas ruminantium-competitive654982 2D-image
DL-alpha-difluoromethylornithineSelenomonas ruminantium-competitive and irreversible654982 2D-image
F-Glycine max--37297 2D-image
Fe2+Heimia salicifolia--37284 2D-image
Fe3+Heimia salicifolia--37284 2D-image
FeCl2Glycine max--37297 2D-image
GDPEscherichia coli--714832 2D-image
GTPEscherichia coli--714832 2D-image
H2PO4-Glycine max--37297 2D-image
HgCl2Bacterium cadaveris, Bacterium cadaveris KY3402--37294 2D-image
HPO42-Glycine max--37297 2D-image
hydroxylamineBacterium cadaveris, Bacterium cadaveris KY3402--37294 2D-image
I-Glycine max--37297 2D-image
iodoacetamideBacterium cadaveris, Bacterium cadaveris KY3402--37294 2D-image
KClGlycine max--37297 2D-image
L-ArgBacterium cadaveris, Bacterium cadaveris KY3402--715142 2D-image
LiClGlycine max--37297 2D-image
NaBH4Escherichia coli--37289 2D-image
NaClEscherichia coli-1 M, 45% inhibition37293 2D-image
NaClGlycine max--37297 2D-image
NaClBacterium cadaveris-about 65% residual activity at 1 M715142 2D-image
PCMBBacterium cadaveris-inhibition is eliminated by addition of 2-mercaptoethanol or glutathione, and pyridoxal 5'-phosphate37294 2D-image
ppGppEscherichia coli-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 5.0714832 2D-image
ppGppEscherichia coli-LdcI activity is strongly inhibited by the binding of ppGpp. The RavA-LdcI interaction reduces the inhibition of LdcI activity by ppGpp in vitro as well as in vivo716768 2D-image
pppGppEscherichia coli-inhibits LdcI only at pH values higher than 6.5714832 2D-image
SemicarbazideBacterium cadaveris--37294 2D-image
SO42-Glycine max--37297 2D-image
UreaSelenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35--37290 2D-image
MnCl2Glycine max--37297 2D-image
additional informationEscherichia coli-at pH values lower than 5.0, there is no effect of ppGpp, pppGpp, GDP and GTP on LdcI activity714832-
additional informationBacterium cadaveris-at 30°C the presence of L-Arg has little effect on the activity of the enzyme715142-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Sulfhydryl groupsEscherichia coli-the enzyme contains six sulfhydryl groups37292 2D-image
additional informationVibrio parahaemolyticusQ87KT6the enzyme is encoded in an acid-induced operon680417-
additional informationVibrio vulnificus, Vibrio vulnificus CYK279H, Vibrio vulnificus MO6-24/O-the enzyme is upregulated by CadC in response to acid stress, and is also induced by SoxR in response to superoxide stress, SoxR binds directly to the promoter region of the cadBA operon, coding for a lysine-cadaverine antiporter, CadB, and the lysine decarboxylase CadA680477-
additional informationEscherichia coli-RpoS is not required either for induction of the cadBA operon or for activity of the Cad system in Escherichia coli starved of phosphate680484-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
7-delta-hydroxylysineEscherichia coli--37289 2D-image
0.37-L-LysBacterium cadaveris, Bacterium cadaveris KY3402--37294 2D-image
0.37-L-LysBacterium cadaveris, Bacterium cadaveris KY3402--37295 2D-image
0.63-L-LysSelenomonas ruminantium-pH 6.0, 40°C654982 2D-image
0.76-L-LysLupinus polyphyllus--37291 2D-image
1.17-L-LysGlycine max--37297 2D-image
1.25-L-LysHeimia salicifolia--37284 2D-image
1.5-L-LysEscherichia coli--37289 2D-image
1.5-L-LysSelenomonas ruminantium--37290 2D-image
1.5-L-LysSelenomonas ruminantium-pH 6.0, 30°C, wild-type enzyme655829 2D-image
1.7-L-LysHafnia alvei--37283 2D-image
1.71-L-LysGlycine max--37297 2D-image
1.9-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C655829 2D-image
2-L-LysEscherichia coli--37286 2D-image
2.4-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C/P54D655829 2D-image
3-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P655829 2D-image
3.2-L-LysVibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4--37300 2D-image
3.6-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S655829 2D-image
4-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme G319W655829 2D-image
5.7-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme P54D655829 2D-image
6.7-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322A655829 2D-image
8-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D655829 2D-image
17-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322T/I326L655829 2D-image
22-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L655829 2D-image
270-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A655829 2D-image
0.42-L-lysineEscherichia coli-at pH 6.5, between 4°C and 10°C714832 2D-image
0.96-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, wild type enzyme655829 2D-image
0.98-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P655829 2D-image
1.2-L-OrnSelenomonas ruminantium-pH 6.0, 40°C654982 2D-image
1.2-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322A655829 2D-image
1.3-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C; pH 6.0, 30°C, mutant enzyme G319W655829 2D-image
1.3-L-OrnSelenomonas ruminantium HD4, Selenomonas ruminantium JY35-pH 6.0, 30°C, mutant enzyme A52C655829 2D-image
1.5-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322T/I326L655829 2D-image
1.6-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C/P54D655829 2D-image
2.1-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme P54D655829 2D-image
3.1-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D655829 2D-image
3.3-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L655829 2D-image
4-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A655829 2D-image
4.5-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S655829 2D-image
3.4-S-aminoethyl-L-CysEscherichia coli--37289 2D-image
4.5-S-aminoethyl-L-CysBacterium cadaveris--37294, 37295 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.6-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S655829 2D-image
4.8-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322A655829 2D-image
5.5-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A655829 2D-image
5.6-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme G319W655829 2D-image
6.8-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C/P54D655829 2D-image
9.8-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D655829 2D-image
10-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C655829 2D-image
13-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P655829 2D-image
16-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme P54D; pH 6.0, 30°C, wild-type enzyme655829 2D-image
19-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L655829 2D-image
21-L-LysSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322T/I326L655829 2D-image
175-L-LysHafnia alvei, Hafnia alvei TPU 6440--37283 2D-image
636-L-LysSelenomonas ruminantium-pH 6.0, 40°C654982 2D-image
30-L-lysineEscherichia coli-at pH 6.5, between 4°C and 10°C714832 2D-image
36L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L655829 2D-image
4.7-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S655829 2D-image
4.8-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A655829 2D-image
7-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C655829 2D-image
7.2-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A52C/P54D; pH 6.0, 30°C, mutant enzyme G319W655829 2D-image
8.4-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P655829 2D-image
8.6-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, wild type enzyme655829 2D-image
13-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme P54D655829 2D-image
14-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D655829 2D-image
20-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322A655829 2D-image
24-L-OrnSelenomonas ruminantium-pH 6.0, 30°C, mutant enzyme S322T/I326L655829 2D-image
289.8-L-OrnSelenomonas ruminantium-pH 6.0, 40°C654982 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
71-L-lysineEscherichia coli-at pH 6.5, between 4°C and 10°C71483212307

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0175-DL-alpha-DifluoromethyllysineSelenomonas ruminantium-pH 6.0, 40°C, reaction with L-Lys654982 2D-image
0.028-DL-alpha-DifluoromethyllysineSelenomonas ruminantium-pH 6.0, 40°C, reaction with L-Orn654982 2D-image
0.00525-DL-alpha-difluoromethylornithineSelenomonas ruminantium-pH 6.0, 40°C, reaction with L-Lys654982 2D-image
0.0082-DL-alpha-difluoromethylornithineSelenomonas ruminantium-pH 6.0, 40°C, reaction with L-Orn654982 2D-image
0.0002377-ppGppEscherichia coli-uncompetitive inhibition, at pH 6.5, between 4°C and 10°C714832 2D-image
0.000374-ppGppEscherichia coli-noncompetitive inhibition, at pH 6.5, between 4°C and 10°C714832 2D-image
0.002791-ppGppEscherichia coli-mixed type inhibition, at pH 6.5, between 4°C and 10°C714832 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
600-L-ArgBacterium cadaveris, Bacterium cadaveris KY3402-at 37°C, pH not specified in the publication715142 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
5.95-Selenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35--37290
11.88-Selenomonas ruminantium--654982
17.8-Glycine max--37297
85.7-Bacterium cadaveris, Bacterium cadaveris KY3402--37295
1000-Escherichia coli--37289
1018-Escherichia coli--37293
additional information-Escherichia coli-assay by the pH-stat method37286
additional information-Escherichia coli--37299
additional information-Vibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4--37300
additional information-Vibrio parahaemolyticusQ87KT6lysine decarboxylase-dependent acid-tolerance assays, overview680417
additional information-Vibrio vulnificus CYK279H, Vibrio vulnificus MO6-24/O, Vibrio vulnificus-pH-dependent enzyme activities, overview680477

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
57.5Vibrio vulnificus-assay at, transcription of cadBA in a pH-dependent manner, overview680477
5.5-Vibrio parahaemolyticus--37300
5.7-Escherichia coli--37286, 37289, 37293
5.8-Bacterium cadaveris--37295
6-Selenomonas ruminantium--37290, 654982
6.28Escherichia coli--37299
7.5-Glycine max--37297
8-Lupinus polyphyllus--37291
8.3-Heimia salicifolia--37284
additional information-Vibrio parahaemolyticusQ87KT6survival of acid adapted and nonadpted strains at pH 5.5 and pH 7.5, 30°C, overview680417

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
4.57Vibrio parahaemolyticus-pH 4.5: about 35% of maximal activity, pH 7.0: about 60% of maximal activity37300
4.58Escherichia coli-pH 4.5: about 30% of maximal activity, pH 8: about 35% of maximal activity37286
4.76.6Escherichia coli-50% of maximal activity at pH 4.7 and 6.637293
5.28.8Escherichia coli-pH 5.2: 40% of maximal activity, pH 8.8: 30% of maximal activity37299
78Selenomonas ruminantium-pH 7.0: about 70% of maximal activity, pH 9.0: about 25% of maximal activity37290

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
30-Vibrio vulnificus, Vibrio vulnificus CYK279H, Vibrio vulnificus MO6-24/O-assay at680477
37-Glycine max--37297
41-Selenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35--37290
4550Vibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4--37300
45-Selenomonas ruminantium--654982
60-Escherichia coli--37286

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2080Vibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4-20°C: about 25% of maximal activity, 80°C: about 95% of maximal activity37300
3041Selenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35-30°C: 38% of maximal activity, 37°C: 71% of maximal activity, 41°C: optimum37290
4070Escherichia coli-40°C: about 40% of maximal activity, 70°C: about 90% of maximal activity37286

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
4.9-Selenomonas ruminantium--654982

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
axisGlycine max--37297Manually annotated by BRENDA team
callusHeimia salicifolia--37284Manually annotated by BRENDA team
cell cultureHeimia salicifolia--37284Manually annotated by BRENDA team
cell cultureSelenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35-grown in chemically defined medium without Lys37290Manually annotated by BRENDA team
cell cultureSelenomonas ruminantium-drastic descent of enzyme activity owing to degradation of LDC at entry into the stationary phase of cell growth654982Manually annotated by BRENDA team
flowerLupinus luteus, Phaseolus vulgaris--37288Manually annotated by BRENDA team
hypocotylGlycine max--690395Manually annotated by BRENDA team
leafBaptisia australis, Lupinus luteus, Phaseolus vulgaris--37288Manually annotated by BRENDA team
leafLupinus polyphyllus--37288, 37291Manually annotated by BRENDA team
podBaptisia australis, Lupinus luteus--37288Manually annotated by BRENDA team
rootBaptisia australis, Lupinus luteus, Phaseolus vulgaris--37288Manually annotated by BRENDA team
rootGlycine max-lysine decarboxylase activity is mainly localized in the roots690395Manually annotated by BRENDA team
rootTriticum aestivum x Secale cereale--713611Manually annotated by BRENDA team
seedlingGlycine max--690395Manually annotated by BRENDA team
shootHeimia salicifolia--37284Manually annotated by BRENDA team
stemBaptisia australis, Lupinus luteus, Phaseolus vulgaris--37288Manually annotated by BRENDA team
leafTriticum aestivum x Secale cereale--713611Manually annotated by BRENDA team
additional informationGlycine max-no appreciable activity is detected in cotyledons and shoots690395Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastLupinus polyphyllus--950737291Manually annotated by BRENDA team
cytoplasmEscherichia coli--5737714832Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3n75, downloadSCOP (3n75)CATH (3n75)Escherichia coli (strain K12)
3q16, downloadSCOP (3q16)CATH (3q16)Escherichia coli (strain K12)
2plj, downloadSCOP (2plj)CATH (2plj)Vibrio vulnificus (strain CMCP6)
2plk, downloadSCOP (2plk)CATH (2plk)Vibrio vulnificus (strain CMCP6)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
82000-Escherichia coli-SDS-PAGE690597
88000-Selenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35-gel filtration37290
88000-Selenomonas ruminantium-gel filtration654982
95000-Glycine max-gel filtration37297
154000-Escherichia coli-dimeric enzyme form, sedimentation data37289
422000-Hafnia alvei-pentameric enzyme form, native PAGE37283
531000-Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4-gel filtration37300
545000-Hafnia alvei-heptameric enzyme form, gel filtration37283
730000-Escherichia coli-decameric enzyme form, sedimentation data37289
761000-Hafnia alvei-decameric enzyme form, analytical ultracentrifugation at 6800 rpm37283
795700-Hafnia alvei-decameric enzyme form, analytical ultracentrifugation at 3600 rpm37283
800000-Escherichia coli-gel filtration37299
1000000-Bacterium cadaveris, Bacterium cadaveris KY3402-equilibrium sedimentation37294
1000000-Bacterium cadaveris, Bacterium cadaveris KY3402-equilibrium sedimentation37295
1174000-Hafnia alvei-pentadecameric enzyme form, analytical ultracentrifugation at 2600 rpm37283

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Hafnia alvei, Hafnia alvei TPU 6440-? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits37283
?Escherichia coli-x * 80000, equilibrium ultracentrifugation in 6 M guanidine-HCl, SDS-PAGE. Association of the dimeric form to the decamer is concomitant with the increase in ionic strength37289
?Escherichia coli-x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length37293
decamerEscherichia coli-10 * 80000, SDS-PAGE37299
decamerEscherichia coli-x-ray crystallography690269
decamerEscherichia coli-the protein is an oligomer of five dimers that associate to form a decamer, X-ray crystallography714832
dimerSelenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35-2 * 44000, SDS-PAGE37290
dimerSelenomonas ruminantium-2 * 42000, SDS-PAGE654982
heptamerVibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4-7 * 79000, SDS-PAGE37300
hexamerThermus thermophilus-isozyme TT1465, crystallization data666850
homodecamerEscherichia coli-10 * 81000, X-ray crystallography716768
tetramerThermus thermophilus-isozyme TT1887, crystallization data666850
monomerGlycine max-1 * 95000, SDS-PAGE37297
additional informationEscherichia coli-enzyme interacts strongly with regulatory ATPase variant A, RavA, forming a cage-like structure consisting of two enzyme decamers linked by up to five RavA oligomers. Enzyme activity is not affected by binding to RavA, but complex formation results in stimulation of RavA ATPase activity665713

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacterium cadaveris, Bacterium cadaveris KY3402-37294, 37295
-Escherichia coli-37293, 714832
cage-like complex of about 3.3 MDa consisting of two LdcI (81 kDa) decamers and up to five RavA (56 kDa) hexamers, hanging drop vapor diffusion method, usingEscherichia coli-716768
hanging drop vapour diffusion method, with 18-28% (w/v) PEG 1000, 100 mM NaCl, 100 mM Tris-HCl pH 8.5, 15% (v/v) glycerol, 5 mM tris(2-carboxyethyl)phospine hydrochlorideEscherichia coli-690269
both isozymes TT1465 and TT1887Thermus thermophilus-666850

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
5.3-Bacterium cadaveris-crystalline enzyme is stable37294
5.58Selenomonas ruminantium-stable654982

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
35-Selenomonas ruminantium-30 min, 50% loss of activity without pyridoxal-5'-phosphate654982
50-Bacterium cadaveris, Bacterium cadaveris KY3402-alkaline pH, 5 min, labile37294
50-Selenomonas ruminantium-30 min, 50% loss of activity in presence of pyridoxal 5'-phosphate654982
60-Selenomonas ruminantium HD4, Selenomonas ruminantium JY35, Selenomonas ruminantium-pH 6.5, 0.1 mM pyridoxal 5'-phosphate, 30% loss of activity after 5 min. 90% loss of activity within 5 min, at pH 6.5 in absence of pyridoxal 5'-phosphate37290
60-Escherichia coli-5 min, 45% loss of activity, enzyme form encoded by the gene ldc. Enzyme form encoded by cadA is very stable after 15 min37299
65-Glycine max-no activity detected after 10 min37297
80-Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4-pH 5.5, 10 min, 35% loss of activity37300

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
calcium alginate can completely entrap the enzyme while retaining activity and improving stability during operation and storageBacterium cadaveris, Bacterium cadaveris KY3402-715142
dithiothreitol is required for stabilization during purification and storageVibrio parahaemolyticus-37300
pyridoxal 5'-phosphate is indispensable for stabilityVibrio parahaemolyticus-37300
dithiothreitol is required for stabilization during purification and storageVibrio parahaemolyticus AQ 3627-37300
pyridoxal 5'-phosphate is indispensable for stabilityVibrio parahaemolyticus AQ 3627-37300
dithiothreitol is required for stabilization during purification and storageVibrio parahaemolyticus EB101-37300
pyridoxal 5'-phosphate is indispensable for stabilityVibrio parahaemolyticus EB101-37300
dithiothreitol is required for stabilization during purification and storageVibrio parahaemolyticus KN1699-37300
pyridoxal 5'-phosphate is indispensable for stabilityVibrio parahaemolyticus KN1699-37300
dithiothreitol is required for stabilization during purification and storageVibrio parahaemolyticus RIMD2210633-37300
pyridoxal 5'-phosphate is indispensable for stabilityVibrio parahaemolyticus RIMD2210633-37300
dithiothreitol is required for stabilization during purification and storageVibrio parahaemolyticus Y-4-37300
pyridoxal 5'-phosphate is indispensable for stabilityVibrio parahaemolyticus Y-4-37300

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, 0.01 M potassium phosphate buffer, pH 6.2, 0.01 mM pyridoxal 5'-phosphate, stable for several weeksBacterium cadaveris, Bacterium cadaveris KY3402-37294
0-4°C,50% loss of activity within 24 hGlycine max-37297
-20°C, crude extract, stable for monthsHafnia alvei, Hafnia alvei TPU 6440-37283
-80°C, stable for one month in presence of 20% glycerol, loss of activity within 2 weeks without glycerolSelenomonas ruminantium-654982

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacterium cadaveris, Bacterium cadaveris KY3402-37294, 37295
-Escherichia coli-37289, 37293, 714832
enzyme form ldcEscherichia coli-37299
Mono Q column chromatography and Superdex 200 gel filtrationEscherichia coli-690269
-Glycine max-37297
-Hafnia alvei, Hafnia alvei TPU 6440-37283
-Selenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35-37290, 654982, 655829
-Vibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627, Vibrio parahaemolyticus EB101, Vibrio parahaemolyticus KN1699, Vibrio parahaemolyticus RIMD2210633, Vibrio parahaemolyticus Y-4-37300

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coli-37299
expressed in Corynebacterium glutamicum ATCC 13032Escherichia coli-690597
expressed in Escherichia coli BL21 (DE3) pLysS cellsEscherichia coli-690269
expression in Escherichia coliHafnia alvei, Hafnia alvei TPU 6440-37285
-Selenomonas ruminantium, Selenomonas ruminantium HD4, Selenomonas ruminantium JY35-655829
gene cadA from strain V02-64, DNA and amino acid sequence, and gene cluster and intergenic region determination and analysis, subcloning in Escherichia coli, quantitative analysis of lysine decarboxylase expression levels dependent on acid conditions at pH 4.0-7.5, primer extension analysis, the gene encoding the enzyme is located in an acid-induced operon, overview, cadA mRNA exhibited about 40fold greater expression at pH 5.0 than at pH 5.5, in cells exposed to pH 7.5, the cadA transcript shows the largest quantity under all conditions, the amount of cadA single transcript is nearly 100fold higher than the polycistronic cadBA transcript for each pH conditionVibrio parahaemolyticusQ87KT6680417
gene cadA, encoded in the cadBA operon, also coding for a lysine-cadaverine antiporter, CadB, expression of cadA in Escherichia coli strain S17-1 and S17-1lambdapir, transcription of cadBA in a pH-dependent manner, overviewVibrio vulnificus, Vibrio vulnificus CYK279H, Vibrio vulnificus MO6-24/O-680477

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
cadA (encoding the lysine decarboxylase) shows higher relative expression level in acid adapted cells than non-acid adapted cellsSalmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium 14028, Salmonella enterica subsp. enterica serovar Typhimurium 14028s, Salmonella enterica subsp. enterica serovar Typhimurium CECT 44, Salmonella enterica subsp. enterica serovar Typhimurium CECT 443, Salmonella enterica subsp. enterica serovar Typhimurium CV-19, Salmonella enterica subsp. enterica serovar Typhimurium Cys- DW 18.1, Salmonella enterica subsp. enterica serovar Typhimurium DsbA homologous, Salmonella enterica subsp. enterica serovar Typhimurium DW378, Salmonella enterica subsp. enterica serovar Typhimurium G-30A, Salmonella enterica subsp. enterica serovar Typhimurium G30, Salmonella enterica subsp. enterica serovar Typhimurium G30A, Salmonella enterica subsp. enterica serovar Typhimurium HD11-AE2, Salmonella enterica subsp. enterica serovar Typhimurium LT-12, Salmonella enterica subsp. enterica serovar Typhimurium LT-2, Salmonella enterica subsp. enterica serovar Typhimurium LT12, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium me-A15, Salmonella enterica subsp. enterica serovar Typhimurium overproducing, Salmonella enterica subsp. enterica serovar Typhimurium PR122, Salmonella enterica subsp. enterica serovar Typhimurium PU011, Salmonella enterica subsp. enterica serovar Typhimurium SG12, Salmonella enterica subsp. enterica serovar Typhimurium SJW1103, Salmonella enterica subsp. enterica serovar Typhimurium SJW2941, Salmonella enterica subsp. enterica serovar Typhimurium SL 1102, Salmonella enterica subsp. enterica serovar Typhimurium SL797, Salmonella enterica subsp. enterica serovar Typhimurium ST89pGK2, Salmonella enterica subsp. enterica serovar Typhimurium Su 422, Salmonella enterica subsp. enterica serovar Typhimurium TA 1538, Salmonella enterica subsp. enterica serovar Typhimurium TA100, Salmonella enterica subsp. enterica serovar Typhimurium TA387, Salmonella enterica subsp. enterica serovar Typhimurium TA98, Salmonella enterica subsp. enterica serovar Typhimurium TA997, Salmonella enterica subsp. enterica serovar Typhimurium TN2529-704086
the Sitobion avenae feeding on triticale cultivar Tornado causes a decrease in the LCD activity with exception of root tissue after two weeks of feeding. In case of cultivar Witon reduction of LCD activity is observed only durig initial period of Sitobion avenae feedingTriticum aestivum x Secale cereale-713611

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
L89REscherichia coli-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 ppGpp714832
R206SEscherichia coli-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 ppGpp714832
R97AEscherichia coli-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 ppGpp714832
A44V/G45T/V46PSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 1.0, compared to 0.69 for the wild-type enzyme654984
A44V/G45T/V46PSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 2.0, compared to 0.83 for the wild-type enzyme655829
A44V/G45T/V46P/P54DSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 3.8, compared to 0.83 for the wild-type enzyme655829
A44V/G45T/V46P/P54D/S322ASelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 58, compared to 0.83 for the wild-type enzyme655829
A44V/G45T/V46P/P54D/S322T/I326LSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 13, compared to 0.83 for the wild-type enzyme655829
A52CSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 1.2, compared to 0.69 for the wild-type enzyme654984
A52CSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.0, compared to 0.83 for the wild-type enzyme655829
A52C/P54DSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 2.6, compared to 0.69 for the wild-type enzyme654984
A52C/P54DSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.6, compared to 0.83 for the wild-type enzyme655829
A52C/P54D/T55SSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 2.7, compared to 0.69 for the wild-type enzyme654984
G319WSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 3.9, compared to 0.83 for the wild-type enzyme655829
M50VSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 0.64, compared to 0.69 for the wild-type enzyme654984
M50V/A52CSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 1.9, compared to 0.69 for the wild-type enzyme654984
M50V/A52C/P54DSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 2.4, compared to 0.69 for the wild-type enzyme654984
M50V/A52C/P54D/T55SSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 4.0, compared to 0.69 for the wild-type enzyme654984
M50V/A52C/P54D/T55SSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.5, compared to 0.83 for the wild-type enzyme655829
P54DSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme654984
P54DSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 2.2, compared to 0.83 for the wild-type enzyme655829
P54D/T55SSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme654984
S322ASelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 24, compared to 0.83 for the wild-type enzyme655829
S322T/I326LSelenomonas ruminantium-the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 13, compared to 0.83 for the wild-type enzyme655829
T55SSelenomonas ruminantium-the ratio of activity with L-Orn to activity with L-Lys is 0.66, compared to 0.69 for the wild-type enzyme654984
A44V/G45T/V46PSelenomonas ruminantium HD4-the ratio of activity with L-Orn to activity with L-Lys is 1.0, compared to 0.69 for the wild-type enzyme654984
A52CSelenomonas ruminantium HD4-the ratio of activity with L-Orn to activity with L-Lys is 1.2, compared to 0.69 for the wild-type enzyme654984
M50VSelenomonas ruminantium HD4-the ratio of activity with L-Orn to activity with L-Lys is 0.64, compared to 0.69 for the wild-type enzyme654984
M50V/A52C/P54D/T55SSelenomonas ruminantium HD4-the ratio of activity with L-Orn to activity with L-Lys is 4.0, compared to 0.69 for the wild-type enzyme654984
P54DSelenomonas ruminantium HD4-the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme654984
A44V/G45T/V46PSelenomonas ruminantium JY35-the ratio of activity with L-Orn to activity with L-Lys is 1.0, compared to 0.69 for the wild-type enzyme654984
A52CSelenomonas ruminantium JY35-the ratio of activity with L-Orn to activity with L-Lys is 1.2, compared to 0.69 for the wild-type enzyme654984
M50VSelenomonas ruminantium JY35-the ratio of activity with L-Orn to activity with L-Lys is 0.64, compared to 0.69 for the wild-type enzyme654984
M50V/A52C/P54D/T55SSelenomonas ruminantium JY35-the ratio of activity with L-Orn to activity with L-Lys is 4.0, compared to 0.69 for the wild-type enzyme654984
P54DSelenomonas ruminantium JY35-the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme654984
additional informationVibrio parahaemolyticusQ87KT6construction of a cadA gene-inactivated strain from wild-type strain V02-64, serotype O3:K, by a plasmid integrated in its chromosome, single crossing over, acid resistance of the mutant strain at pH 4.0 in phosphate buffer is weaker than in the parental strain680417
additional informationVibrio vulnificus, Vibrio vulnificus CYK279H, Vibrio vulnificus MO6-24/O-a lack of cadaverine caused by mutation in cadA results in low tolerance to oxidative stress compared to the wild type, cadaverine, which neutralizes the external medium, also appears to scavenge superoxide radicals, since increasing cellular cadaverine by elevating the gene dosage of cadBA significantly diminished the induction of Mn-containing superoxide dismutase under methyl viologen-induced oxidative stress, overview680477

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
37283Beier, H.; Fecker, L.F.; Berlin, J.Lysine decarboxylase from Hafnia alvei: purification, molecular data and preparation of polyclonal antibodiesZ. Naturforsch. C421307-13121987Hafnia alvei-
37284Pelosi, L.A.; Rother, A.; Edwards, J.M.Lysine decarboxylase activity and alkaloid production in Heimia salicifolia culturesPhytochemistry252315-23191986Heimia salicifolia-
37285Fecker, L.F.; Beier, H.; Berlin, J.Cloning and characterization of a lysine decarboxylase gene from Hafnia alveiMol. Gen. Genet.203177-1841986Hafnia alvei-
37286Vienozinskiene, J.; Januseviciute, R.; Pauliukonis, A.; Kazlauskas, D.Lysine decarboxylase assay by the pH-stat methodAnal. Biochem.146180-1831985Escherichia coli PubMed
37287Poesoe, H.; McCann, P.P.; Tanskanen, R.; Bey, P.; Sjoerdsma, A.Inhibition of growth of Mycoplasma dispar by DL-alpha-difluoromethyllsine, a selective irreversible inhibitor of lysine decarboxylase, and reversal by cadaverine (1,5-diaminopentane)Biochem. Biophys. Res. Commun.125205-2101984Mycoplasma dispar PubMed
37288Schoofs, G.; Teichmann, S.; Hartmann, T.; Wink, M.Lysine decarboxylase in plants and its integration in quinolizidine alkaloid biosynthesisPhytochemistry2265-691983Anchusa italica, Arum maculatum, Asarum maculatum, Astragalus cicer, Astragalus glycyphyllos, Atropa belladonna, Baptisia australis, Calla palustris, Chenopodium rubrum, Conium maculatum, Cytisus beanii, Cytisus canariensis, Cytisus scoparius, Dictamnus albus, Galega officinalis, Genista anglica, Genista hispanica, Genista lydia, Genista pilosa, Genista sagittalis, Genista tinctoria, Glycine max, Glycyrrhiza echinata, Laburnum alpinum, Laburnum anagyroides, Levisticum officinale, Lupinus albus, Lupinus luteus, Lupinus polyphyllus, Malva sylvestris, Medicago sativa, Melilotus albus, Mentha suaveolens, Menyanthes trifoliata, Nicotiana tabacum, Phaseolus vulgaris, Pisum sativum, Robinia pseudoacacia, Ruta graveolens, Sanguisorba officinalis, Saponaria officinalis, Sedum acre, Senecio fuchsii, Sophora japonica, Sophora tetraptera, Spinacia oleracea, Symphytum officinale, Trollius europaeus, Valeriana sambucifolia, Vicia faba-
37289Boeker, E.A.; Fischer, E.H.Lysine decarboxylase (Escherichia coli B)Methods Enzymol.94180-1841983Escherichia coli PubMed
37290Kamio, Y.; Terawaki, Y.Purification and properties of Selenomonas ruminantium lysine decarboxylaseJ. Bacteriol.153658-6641983Selenomonas ruminantium PubMed
37291Hartmann, T.; Schoofs, G.; Wink, M.A chloroplast-localized lysine decarboxylase of Lupinus polyphyllus: the first enzyme in the biosynthetic pathway of quinolizidine alkaloidsFEBS Lett.11535-381980Lupinus polyphyllus PubMed
37292Sabo, D.L.; Fischer, E.H.Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5 -phosphate binding siteBiochemistry13670-6761974Escherichia coli PubMed
37293Sabo, D.L.; Boeker, E.A.; Byers, B.; Waron, H.; Fischer, E.H.Purification and physical properties of inducible Escherichia coli lysine decarboxylaseBiochemistry13662-6701974Escherichia coli PubMed
37294Soda, K.; Moriguchi, M.L-Lysine decarboxylase (Bacterium cadaveris)Methods Enzymol.17B677-6811971Bacterium cadaveris-
37295Soda, K.; Moriguchi, M.Crystalline lysine decarboxylaseBiochem. Biophys. Res. Commun.3434-391969Bacterium cadaveris PubMed
37296Battersby, A.R.; Murphy, R.; Staunton, J.Studies of enzyme-mediated reactions. Part 14. Stereochemical course of the formation of cadaverine by decarboxylation of (2S)-lysine with lysine decarboxylase (E.C. 4.1.1.18) from Bacillus cadaverisJ. Chem. Soc. Perkin Trans. I1982449-4531982Bacterium cadaveris-
37297Kim, H.S.; Kim, B.H.; Cho, Y.D.Purification and characterization of monomeric lysine decarboxylase from soybean (Glycine max) axesArch. Biochem. Biophys.35440-461998Glycine max PubMed
37298Berkowitz, D.B.; Jahng, W.J.; Pedersen, M.L.alpha-Vinyllysine and alpha-vinylarginine are time-dependent inhibitors of their cognate decarboxylasesBioorg. Med. Chem. Lett.62151-21561996Bacterium cadaveris-
37299Kikuchi, Y.; Kojima, H.; Tanaka, T.; Takasuka, Y.; Kamio, Y.Characterization of a second lysine decarboxylase isolated from Escherichia coliJ. Bacteriol.1794486-44921997Escherichia coli PubMed
37300Yamamoto, S.; Imamura, T.; Kusaba, K.; Shinoda, S.Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticusChem. Pharm. Bull.393067-30701991Vibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627 PubMed
37301Pegg, A.E.; McGill, S.Decarboxylation of ornithine and lysine in rat tissuesBiochim. Biophys. Acta568416-4271979Mus musculus, no activity in Rattus norvegicus PubMed
654982Takatsuka, Y.; Onoda, M.; Sugiyama, T.; Muramoto, K.; Tomita, T.; Kamio, Y.Novel characteristics of Selenomonas ruminantium lysine decarboxylase capable of decarboxylating both L-lysine and L-ornithineBiosci. Biotechnol. Biochem.631063-10691999Selenomonas ruminantium, Selenomonas ruminantium (O50657) PubMed
654984Takatsuka, Y.; Tomita, T.; Kamio, Y.Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylaseBiosci. Biotechnol. Biochem.631843-18461999Selenomonas ruminantium PubMed
655829Takatsuka, Y.; Yamaguchi, Y.; Ono, M.; Kamio, Y.Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotesJ. Bacteriol.1826732-67412000Selenomonas ruminantium, Selenomonas ruminantium (O50657) PubMed
656712Levine, M.; Progulske-Fox, A.; Denslow, N.D.; Farmerie, W.G.; Smith, D.M.; Swearingen, W.T.; Miller, F.C.; Liang, Z.; Roe, B.A.; Pan, H.Q.Identification of lysine decarboxylase as a mammalian cell growth inhibitor in Eikenella corrodens: possible role in periodontal diseaseMicrob. Pathog.30179-1922001Eikenella corrodens PubMed
665713Snider, J.; Gutsche, I.; Lin, M.; Baby, S.; Cox, B.; Butland, G.; Greenblatt, J.; Emili, A.; Houry, W.A.Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPaseJ. Biol. Chem.2811532-15462006Escherichia coli PubMed
666850Kukimoto-Niino, M.; Murayama, K.; Kato-Murayama, M.; Idaka, M.; Bessho, Y.; Tatsuguchi, A.; Ushikoshi-Nakayama, R.; Terada, T.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8Protein Sci.133038-30422004Thermus thermophilus PubMed
680417Tanaka, Y.; Kimura, B.; Takahashi, H.; Watanabe, T.; Obata, H.; Kai, A.; Morozumi, S.; Fujii, T.Lysine decarboxylase of Vibrio parahaemolyticus: kinetics of transcription and role in acid resistanceJ. Appl. Microbiol.1041283-12932007Vibrio parahaemolyticus (Q87KT6), Vibrio parahaemolyticus PubMed
680477Kim, J.S.; Choi, S.H.; Lee, J.K.Lysine decarboxylase expression by Vibrio vulnificus is induced by SoxR in response to superoxide stressJ. Bacteriol.1888586-85922006Vibrio vulnificus PubMed
680484Moreau, P.L.The lysine decarboxylase CadA protects Escherichia coli starved of phosphate against fermentation acidsJ. Bacteriol.1892249-22612007Escherichia coli PubMed
690269Alexopoulos, E.; Kanjee, U.; Snider, J.; Houry, W.A.; Pai, E.F.Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coliActa Crystallogr. Sect. F64700-7062008Escherichia coli, Escherichia coli (P0A9H3) PubMed
690395Ohe, M.; Scoccianti, V.; Bagni, N.; Tassoni, A.; Matsuzaki, S.Putative occurrence of lysine decarboxylase isoforms in soybean (Glycine max) seedlingsAmino Acids3665-702009Glycine max PubMed
690597Tateno, T.; Okada, Y.; Tsuchidate, T.; Tanaka, T.; Fukuda, H.; Kondo, A.Direct production of cadaverine from soluble starch using Corynebacterium glutamicum coexpressing alpha-amylase and lysine decarboxylaseAppl. Microbiol. Biotechnol.82115-1212009Escherichia coli PubMed
698360Lafay, B.; Ruimy, R.; de Traubenberg, C.R.; Breittmayer, V.; Gauthier, M.J.; Christen, R.Roseobacter algicola sp. nov., a new marine bacterium isolated from the phycosphere of the toxin-producing dinoflagellate Prorocentrum limaInt. J. Syst. Bacteriol.45290-2961995no activity in Marinovum algicola, no activity in Marinovum algicola ATCC 51442 PubMed
698361Ruiz-Ponte, C.; Cilia, V.; Lambert, C.; Nicolas, J.L.Roseobacter gallaeciensis sp. nov., a new marine bacterium isolated from rearings and collectors of the scallop Pecten maximusInt. J. Syst. Bacteriol.48 Pt 2537-5421998no activity in Phaeobacter gallaeciensis BS107 PubMed
698364Lau, S.C.; Tsoi, M.M.; Li, X.; Plakhotnikova, I.; Wu, M.; Wong, P.K.; Qian, P.Y.Loktanella hongkongensis sp. nov., a novel member of the alpha-Proteobacteria originating from marine biofilms in Hong Kong watersInt. J. Syst. Evol. Microbiol.542281-22842004no activity in Loktanella hongkongensis PubMed
698370Lee, O.O.; Tsoi, M.M.; Li, X.; Wong, P.K.; Qian, P.Y.Thalassococcus halodurans gen. nov., sp. nov., a novel halotolerant member of the Roseobacter clade isolated from the marine sponge Halichondria panicea at Friday Harbor, USAInt. J. Syst. Evol. Microbiol.571919-19242007no activity in Thalassobius mediterraneus, no activity in Thalassobius mediterraneus XSM19, no activity in Thalassococcus halodurans, no activity in Thalassococcus halodurans UST050418-052, Thalassobius aestuarii, Thalassobius aestuarii JC2049 PubMed
704086Alvarez-Ordonez, A.; Fernandez, A.; Bernardo, A.; Lopez, M.Arginine and lysine decarboxylases and the acid tolerance response of Salmonella typhimuriumInt. J. Food Microbiol.136278-2822010Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium CECT 443 PubMed
713611Sempruch, C.; Leszczynski, B.; Wojcicka, A.; Makosz, M.; Matok, H.; Chrzanowski, G.Changes in activity of lysine decarboxylase in winter triticale in response to grain aphid feedingActa Biol. Hung.61512-5152010Triticum aestivum x Secale cereale PubMed
714832Kanjee, 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 decarboxylaseEMBO J.30931-9442011Escherichia coli, Escherichia coli (P0A9H3) PubMed
715142Teng, Y.; Scott, E.; Van Zeeland, A.; Sanders, J.The use of L-lysine decarboxylase as a means to separate amino acids by electrodialysisGreen Chem.13624-6302011Bacterium cadaveris-
716768El Bakkouri, M.; Gutsche, I.; Kanjee, U.; Zhao, B.; Yu, M.; Goret, G.; Schoehn, G.; Burmeister, W.P.; Houry, W.A.Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activityProc. Natl. Acad. Sci. USA10722499-225042010Escherichia coli PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.18)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)