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
-
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
-
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
-
simmons
-
alvei
-
macconkey
-
quinolizidine
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hafnia
-
eikenella
-
huperzia
-
d-arabitol
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4.1.1.17
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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
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pH Range
pH Range on EC 4.1.1.18 - lysine decarboxylase
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4.5 - 7
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pH 4.5: about 35% of maximal activity, pH 7.0: about 60% of maximal activity
4.5 - 8
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pH 4.5: about 30% of maximal activity, pH 8: about 35% of maximal activity
5.5 - 8
maximal activity at pH 5.5, 30% of maximal activity at pH 8.0
6.2 - 8.8
soluble wild-type enzyme, maximal activity at pH 6.2-8.0, 30% of maximal activity at pH 8.8
7 - 8
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pH 7.0: about 70% of maximal activity, pH 9.0: about 25% of maximal activity
7.5 - 9
recombinant enzyme inclusion bodies, EcLDCc-CatIBs, range of higher activity
8 - 9
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enzyme gtLDC does not exhibit effective activity in alkaline pH conditions, the conversion rate of about 8% is similar at pH 8.0 and pH 9.0, no activity at pH 10.0
additional information
CadA is rapidly inactivated as the pH increases during the decarboxylation of lysine because it has an acidic optimum pH 5.0-6.0
additional information
CadA is rapidly inactivated as the pH increases during the decarboxylation of lysine because it has an acidic optimum pH 5.0-6.0
additional information
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CadA is rapidly inactivated as the pH increases during the decarboxylation of lysine because it has an acidic optimum pH 5.0-6.0
additional information
the cadaverine conversion rate is negatively affected at above pH 9
additional information
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the cadaverine conversion rate is negatively affected at above pH 9