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Literature summary for 3.5.1.4 extracted from

  • Sharma, M.; Sharma, N.N.; Bhalla, T.C.
    Purification studies on a thermo-active amidase of Geobacillus pallidus BTP-5x MTCC 9225 isolated from thermal springs of Tatapani (Himachal Pradesh) (2013), Appl. Biochem. Biotechnol., 169, 1-14.
    View publication on PubMed
Search for more literature for 3.5.1.4

Activating Compound

Activating Compound Comment Organism Structure
8-hydroxyquinoline 18% activation aat 1 mM Aeribacillus pallidus
hydroxylamine 11% activation aat 1 mM Aeribacillus pallidus

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, sequence comparison Aeribacillus pallidus

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol 9% inhibition at 1 mM Aeribacillus pallidus
Ag+ complete inhibition at 1 mM Aeribacillus pallidus
Cd2+ 98% inhibition at 1 mM Aeribacillus pallidus
Co2+ 52% inhibition at 1 mM Aeribacillus pallidus
Cu2+ complete inhibition at 1 mM Aeribacillus pallidus
Hg2+ complete inhibition at 1 mM Aeribacillus pallidus
L-ascorbic acid 19% inhibition at 1 mM Aeribacillus pallidus
additional information the enzyme shows resistance to metal chelating agents EDTA, 8-hydroxyquinoline, and sodium azide and is not inhibited by DTT and PMSF or by ammonium persulfate Aeribacillus pallidus
phenyl hydrazine complete inhibition at 1 mM Aeribacillus pallidus
Urea 47% inhibition at 1 mM Aeribacillus pallidus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
10.54
-
 Acrylamide pH 8.0, 50°C Aeribacillus pallidus

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metalloenzyme, no effect on enzyme activity by Fe2+, Mn2+, Mg2+, and Ca2+ Aeribacillus pallidus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38400
-
 4 * 38500, SDS-PAGE, 4 * 38400, about, sequence calculation Aeribacillus pallidus
38500
-
 4 * 38500, SDS-PAGE, 4 * 38400, about, sequence calculation Aeribacillus pallidus
158000
-
 native PAGE Aeribacillus pallidus

Organism

Organism UniProt Comment Textmining
Aeribacillus pallidus
-
 isolated from thermal springs of Tatapani (Himachal Pradesh)
-
Aeribacillus pallidus BTP-5x MTCC 9225
-
 isolated from thermal springs of Tatapani (Himachal Pradesh)
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 6.2fold to apparent homogeneity by anion exchange chromatography and gel filtration Aeribacillus pallidus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
30.49
-
 purified native enzyme, pH 8.0, 50°C Aeribacillus pallidus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetamide + H2O high activity Aeribacillus pallidus acetate + NH3
-
 ?
acetamide + H2O high activity Aeribacillus pallidus BTP-5x MTCC 9225 acetate + NH3
-
 ?
acrylamide + H2O
-
 Aeribacillus pallidus acrylate + NH3
-
 ?
acrylamide + H2O
-
 Aeribacillus pallidus BTP-5x MTCC 9225 acrylate + NH3
-
 ?
formamide + H2O
-
 Aeribacillus pallidus formate + NH3
-
 ?
formamide + H2O
-
 Aeribacillus pallidus BTP-5x MTCC 9225 formate + NH3
-
 ?
lactamide + H2O
-
 Aeribacillus pallidus lactate + NH3
-
 ?
additional information the enzyme preferentially hydrolyzes small aliphatic amides and has a narrow substrate spectrum, overview. Poor activity with methacrylamide, N-methyl acetamide, cyanoacetamide, and butyramide. No activity with thioacetamide, trimethylacetamide, N-ethylacetamide, dimethylformamide, nicotinamide, and benzamide Aeribacillus pallidus ?
-
 ?
additional information the enzyme preferentially hydrolyzes small aliphatic amides and has a narrow substrate spectrum, overview. Poor activity with methacrylamide, N-methyl acetamide, cyanoacetamide, and butyramide. No activity with thioacetamide, trimethylacetamide, N-ethylacetamide, dimethylformamide, nicotinamide, and benzamide Aeribacillus pallidus BTP-5x MTCC 9225 ?
-
 ?
propionamide + H2O best substrate Aeribacillus pallidus propionate + NH3
-
 ?
propionamide + H2O best substrate Aeribacillus pallidus BTP-5x MTCC 9225 propionate + NH3
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 38500, SDS-PAGE, 4 * 38400, about, sequence calculation Aeribacillus pallidus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 broad optimum of 45-70°C Aeribacillus pallidus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 70 activity range Aeribacillus pallidus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the multimeric nature of the holozyme as a tetramer contributes to protection of the enzyme against thermal denaturation Aeribacillus pallidus
50 55 purified enzyme, stable up to 6 h at 50°C, with a t1/2 of 7 h at 55°C Aeribacillus pallidus
60
-
 purified enzyme, pH 8.0, the activity decreases rapidly after 4 h Aeribacillus pallidus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0715
-
 Acrylamide pH 8.0, 50°C Aeribacillus pallidus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2 8.3 broad optimum of pH 6.0-9.0 Aeribacillus pallidus

pH Range

pH Minimum pH Maximum Comment Organism
4 10.5 activity range Aeribacillus pallidus

pI Value

Organism Comment pI Value Maximum pI Value
Aeribacillus pallidus sequence calculation
-
 5.38

General Information

General Information Comment Organism
additional information acysteine residue is involved in catalysis Aeribacillus pallidus