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Literature summary for 3.5.1.137 extracted from

  • Hashimoto, M.; Fukui, M.; Hayano, K.; Hayatsu, M.
    Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100 (2002), Appl. Environ. Microbiol., 68, 1220-1227 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.137

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Rhizobium sp. AC100

Inhibitors

Inhibitors Comment Organism Structure
Hg2+ the enzyme is completely inhibited by 1 mM Hg2+ Rhizobium sp. AC100
additional information EDTA, iodoacetamide, diisopropyl fluorophosphate, and paraoxon have no effect on the enzyme activity Rhizobium sp. AC100

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.062
-
 Carbaryl at pH 7.0 and 30°C Rhizobium sp. AC100

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
160000
-
 gel filtration Rhizobium sp. AC100

Organism

Organism UniProt Comment Textmining
Rhizobium sp. AC100 Q8RR61
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Q Sepharose column chromatography, SP Sepharose column chromatography, and Sephacryl S-200 gel filtration Rhizobium sp. AC100

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.05
-
 crude extract, at pH 7.0 and 30°C Rhizobium sp. AC100
30.7
-
 after 614fold purification, at pH 7.0 and 30°C Rhizobium sp. AC100

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-naphthyl acetate + H2O
-
 Rhizobium sp. AC100 1-naphthol + acetate
-
 ?
3,5-dimethylphenyl N-methylcarbamate + H2O XMC, 115% activity compared to carbaryl Rhizobium sp. AC100 ?
-
 ?
4-nitrophenyl acetate + H2O
-
 Rhizobium sp. AC100 4-nitrophenol + acetate
-
 ?
carbaryl + H2O i.e. 1-naphthyl N-methylcarbamate, 100% activity Rhizobium sp. AC100 1-naphthol + methylamine + CO2
-
 ?
fenobucarb + H2O i.e 2-s-butylphenyl N-methylcarbamate, 11% activity compared to carbaryl Rhizobium sp. AC100 ?
-
 ?
isoprocarb + H2O i.e. 2-isopropylphenyl N-methylcarbamate, 21% activity compared to carbaryl Rhizobium sp. AC100 ?
-
 ?
methylparathion + H2O i.e. O,O-dimethyl-O-4-nitrophenylthiophosphate Rhizobium sp. AC100 ?
-
 ?
metolcarb + H2O i.e. 3-methylphenyl N-methylcarbamate, 54% activity compared to carbaryl Rhizobium sp. AC100 ?
-
 ?
additional information hydrolase activity is undetectable with the substrates of carbofuran and chloropropham Rhizobium sp. AC100 ?
-
-
propoxur + H2O i.e. 2-isopropoxyphenyl N-methylcarbamate, 9% activity compared to carbaryl Rhizobium sp. AC100 ?
-
 ?
xylylcarb + H2O i.e. 3,4-dimethylphenyl N-methylcarbamate, 61% activity compared to carbaryl Rhizobium sp. AC100 ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 82000, SDS-PAGE Rhizobium sp. AC100

Synonyms

Synonyms Comment Organism
carbaryl hydrolase
-
 Rhizobium sp. AC100
cehA
-
 Rhizobium sp. AC100

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Rhizobium sp. AC100

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 50 the enzyme is stable for 10 min at temperatures up to 30°C, and 50% of the initial activity is retained at 50°C Rhizobium sp. AC100

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 at 30°C Rhizobium sp. AC100

pH Range

pH Minimum pH Maximum Comment Organism
6 11 the enzyme retains over 80% of its maximal activity between pH values of 6.0 to 11.0 Rhizobium sp. AC100

pH Stability

pH Stability pH Stability Maximum Comment Organism
10 11 the hydrolase is stable within a pH range of 10.0 to 11.0 Rhizobium sp. AC100