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
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4.1.1.18
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ornithine
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urease
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aeromonas
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dihydrolase
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decarboxylases
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voges-proskauer
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dna-dna
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esculin
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non-motile
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cadba
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salicin
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1,5-diaminopentane
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d-mannitol
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melibiose
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dulcitol
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ruminantium
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adonitol
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selenomonas
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sobria
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enteroinvasive
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d-sorbitol
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carbenicillin
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cephalothin
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corrodens
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simmons
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alvei
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macconkey
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quinolizidine
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hafnia
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eikenella
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huperzia
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d-arabitol
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4.1.1.17
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synthesis
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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
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Inhibitors
Inhibitors on EC 4.1.1.18 - lysine decarboxylase
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PCMB
Bacterium cadaveris
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inhibition is eliminated by addition of 2-mercaptoethanol or glutathione, and pyridoxal 5'-phosphate
competitive inhibition mechanism, 90% inhibition at 10 mM
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
ppGpp
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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 vivo
Bacterium cadaveris
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at 30°C the presence of L-Arg has little effect on the activity of the enzyme
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additional information
Bacterium cadaveris
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inhibitory effect of organophosphate esters (OPEs) with aromatic, alkyl or chlorinated alkyl substituents on the activity of lysine decarboxylase (LDC) is assessed quantitatively with an economic and label-free fluorescence sensor and cell assay. Molecular docking analysis of the LDC/OPE complexes reveals that different binding modes contribute to the difference in their inhibitory effect. No inhibition by tris(2-ethylhexyl) phosphate, tributoxyethyl phosphate, tri-n-butyl phosphate, tri-n-propyl phosphate, triethyl phosphate, and trimethyl phosphate. In vivo cytotoxic effect of the compounds in Rattus norvegicus PC-12 cells, overview
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additional information
at pH values lower than 5.0, there is no effect of ppGpp, pppGpp, GDP and GTP on LdcI activity
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additional information
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at pH values lower than 5.0, there is no effect of ppGpp, pppGpp, GDP and GTP on LdcI activity
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additional information
enzyme LdcC shows no or poor substrate inhibition by L-lysine
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additional information
enzyme LdcC shows no or poor substrate inhibition by L-lysine
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additional information
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enzyme LdcC shows no or poor substrate inhibition by L-lysine
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