4.1.1.19: arginine decarboxylase
This is an abbreviated version!
For detailed information about arginine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.19
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4.1.1.19
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polyamine
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putrescine
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ornithine
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spermidine
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s-adenosylmethionine
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arginase
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diamine
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samdc
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decarboxylases
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agmatinase
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deiminase
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alpha-difluoromethylornithine
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cadaverine
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imidazoline
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d-arginine
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pao
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3.5.3.1
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iminohydrolase
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arginine-dependent
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scots
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ureohydrolase
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difluoromethylornithine
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pyrogenic
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drug development
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agriculture
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hyoscyamine
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trifoliata
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poncirus
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speb
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tropane
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dl-alpha-difluoromethylornithine
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antizyme
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datura
- 4.1.1.19
- polyamine
- putrescine
- ornithine
- spermidine
- s-adenosylmethionine
- arginase
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diamine
- samdc
- decarboxylases
- agmatinase
- deiminase
- alpha-difluoromethylornithine
- cadaverine
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imidazoline
- d-arginine
- pao
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3.5.3.1
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iminohydrolase
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arginine-dependent
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scots
-
ureohydrolase
- difluoromethylornithine
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pyrogenic
- drug development
- agriculture
- hyoscyamine
- trifoliata
- poncirus
- speb
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tropane
- dl-alpha-difluoromethylornithine
- antizyme
- datura
Reaction
Synonyms
AaxB, AaxB protein, acid-induced biodegradative arginine decarboxylase, ADC, ADC 1, ADC 2, ADC1, ADC2, AdiA, ARGDC, arginine decarboxlase 2, arginine decarboxylase, arginine decarboxylase2, arginine:agmatine exchange system, ATADC1, AtADC2, AtDC2, bADC, Biosynthetic arginine decarboxylase, biosynthetic arginine decarboxylase 1, biosynthetic arginine decarboxylase 2, ClADC, CPn1032 homolog, dADC, Decarboxylase, arginine, HP0422, HVO_1958, L-Arginine decarboxylase, More, NtADC1, NtADC2, PaADC1, PaADC2, PBCV-1 DC, PdaD, PpADC, protein SSO0536, PtADC, PvlArgDC, pyruvoyl-dependent arginine decarboxylase, pyruvoyl-dependent arginine decraboxylase, slr0662, slr1312, SPE1, SPE2, SpeA, speA1, speA2, StADC, Synthetic arginine decarboxylase, Tk-PdaD, TK0149
ECTree
4.1.1.19 arginine decarboxylaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.1.1.19 - arginine decarboxylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C524A
91.8% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity
K136A
97.7% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity
T52S
X128W
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the purified X128W variant protein catalyzes the decarboxylation of L-arginine with a pH optimum near 3.4 with increased Km and decreased kcat values compared to the wild type enzyme
C487A
E109Q
E109Q mutation reduces the activity by 7.7fold compared to the wild type enzyme, reduced decarboxylation activity results in part from incomplete pyruvoyl-group formation
N47A
The activity of N47A is reduced by 500fold compared with the wild type protein
T142A
Paramecium bursaria chlorella virus
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site-directed mutagenesis, structural comparison to the wild-type enzyme, overview
D296E
Paramecium bursaria Chlorella virus-1
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responsible for changes in substrate specificity
E296D
Paramecium bursaria Chlorella virus-1
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increased Km and decreased turnover with L-Arg, minor effect on Km with L-ornithine, decreased turnover with L-ornithine
additional information
T52S
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site-directed mutagenesis, the mutant enzyme is significantly impaired in proteolytic self-cleavage
T52S
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site-directed mutagenesis, the mutant enzyme is significantly impaired in proteolytic self-cleavage
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C487A
site-directed mutagenesis, the mutant shows less than 10% of wild-type activity, but only slightly reduced temperature stability compared to wild-type
C487A
Helicobacter pylori ATCC 700392 / 26695
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site-directed mutagenesis, the mutant shows less than 10% of wild-type activity, but only slightly reduced temperature stability compared to wild-type
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additional information
construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
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construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
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construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
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construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
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additional information
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construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
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additional information
construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae
additional information
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construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae
additional information
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agmatine-producing mouse cortical astrocytes were developed through transduction of the transformed heterologous human ADC gene
additional information
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downregulation of nicotine biosynthesis via antisense approach, diminishing of ADC activity in transformed roots, alkaloid profile of cultured hairy roots and regenerated transgenic plants, growth of transformed roots is unaltered, overview
additional information
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in vivo knockdown of translation of ODC1 (EC 4.1.1.17) and ADC mRNAs individually and in combination. Double knockdown of ODC1 and ADC (MAO-ODC1:ADC) results in two phenotypes (a or b) of conceptuses: 33% of conceptuses appear to be morphologically and functionally normal (phenotype a) and 67% of the conceptuses present an abnormal morphology and functionality (phenotype b). Furthermore, MAO-ODC1:ADC (a) conceptuses have greater tissue concentrations of agmatine, putrescine, and spermidine than MAO control conceptuses, while AO-ODC1:ADC (b) conceptuses only have greater tissue concentrations of agmatine. Uterine flushes from ewes with MAO-ODC1:ADC (a) have greater amounts of arginine, aspartate, tyrosine, citrulline, lysine, phenylalanine, isoleucine, leucine, and glutamine, while uterine flushes of ewes with MAO-ODC1:ADC (b) conceptuses have lower amount of putrescine, spermidine, spermine, alanine, aspartate, glutamine, tyrosine, phenylalanine, isoleucine, leucine, and lysine. Phenotypes, overview
additional information
marker-less gene speA deletion by by double-crossover recombination, construction of a double knockout DELTAtdk/DELTAspeA mutant strain MS531 by knockout of gene speA in DELTAtdk strain MS416. DELTAtdk strains show 5-fluoro-2'-deoxyuridine resistance. Mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium
additional information
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marker-less gene speA deletion by by double-crossover recombination, construction of a double knockout DELTAtdk/DELTAspeA mutant strain MS531 by knockout of gene speA in DELTAtdk strain MS416. DELTAtdk strains show 5-fluoro-2'-deoxyuridine resistance. Mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium
additional information
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marker-less gene speA deletion by by double-crossover recombination, construction of a double knockout DELTAtdk/DELTAspeA mutant strain MS531 by knockout of gene speA in DELTAtdk strain MS416. DELTAtdk strains show 5-fluoro-2'-deoxyuridine resistance. Mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium
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additional information
the PA14 aguA-Gm, DELTAagu2ABCA' mutant cannot break down agmatine. Some clinical isolates of Pseudomonas aeruginosa also lack a functional agmatine deiminase
additional information
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the PA14 aguA-Gm, DELTAagu2ABCA' mutant cannot break down agmatine. Some clinical isolates of Pseudomonas aeruginosa also lack a functional agmatine deiminase
additional information
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the PA14 aguA-Gm, DELTAagu2ABCA' mutant cannot break down agmatine. Some clinical isolates of Pseudomonas aeruginosa also lack a functional agmatine deiminase
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additional information
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
additional information
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modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
additional information
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modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
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