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Literature summary extracted from

  • Hanphakphoom, S.; Maneewong, N.; Sukkhum, S.; Tokuyama, S.; Kitpreechavanich, V.
    Characterization of poly(L-lactide)-degrading enzyme produced by thermophilic filamentous bacteria Laceyella sacchari LP175 (2014), J. Gen. Appl. Microbiol., 60, 13-22.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.66 DNA and amino acid sequence determination and analysis, phylogenetic tree Laceyella sacchari

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.66 1,10-phenanthroline at 5 mM Laceyella sacchari
3.4.21.66 2-mercaptoethanol slight inhibition Laceyella sacchari
3.4.21.66 Ca2+ 18% inhibition at 1 mM, 85% inhibition at 4 mM Laceyella sacchari
3.4.21.66 CTAB
-
 Laceyella sacchari
3.4.21.66 Cu2+ 8% inhibition at 1 mM, 99% inhibition at 4 mM Laceyella sacchari
3.4.21.66 DTT slight inhibition at 1-10 mM Laceyella sacchari
3.4.21.66 EDTA strong inhibition at 1 mM Laceyella sacchari
3.4.21.66 EGTA strong inhibition at 1 mM Laceyella sacchari
3.4.21.66 Fe2+ 54% inhibition at 1 mM, 80% inhibition at 4 mM Laceyella sacchari
3.4.21.66 K+ 36% inhibition at 1 mM, 53% inhibition at 4 mM Laceyella sacchari
3.4.21.66 Mg2+ 54% inhibition at 1 mM, 89% inhibition at 4 mM Laceyella sacchari
3.4.21.66 additional information inhibition by metal ions is blocked by EDTA Laceyella sacchari
3.4.21.66 Na+ 35% inhibition at 1 mM, 54% inhibition at 4 mM Laceyella sacchari
3.4.21.66 Plysurf A210G strong inhibition Laceyella sacchari
3.4.21.66 PMSF strong inhibition at 1 mM Laceyella sacchari
3.4.21.66 SDS strong inhibition Laceyella sacchari
3.4.21.66 Triton X-100
-
 Laceyella sacchari
3.4.21.66 Tween 20 strong inhibition Laceyella sacchari
3.4.21.66 Tween 80 strong inhibition Laceyella sacchari
3.4.21.66 Urea slight inhibition Laceyella sacchari
3.4.21.66 Zn2+ 65% inhibition at 1 mM, 81% inhibition at 4 mM Laceyella sacchari

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.66 extracellular
-
 Laceyella sacchari
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.66 Co2+ activates to 119% at 1 mM Laceyella sacchari

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.66 28000
-
 gel filtration Laceyella sacchari

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.66 additional information Laceyella sacchari the enzyme degrades poly(L-lactide) and is a serine protease ?
-
 ?
3.4.21.66 additional information Laceyella sacchari LP175 the enzyme degrades poly(L-lactide) and is a serine protease ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.66 Laceyella sacchari
-
 isolated from forest soil in Thailand
-
3.4.21.66 Laceyella sacchari LP175
-
 isolated from forest soil in Thailand
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.66 native enzyme 15.3fold to homogeneity from culture supernatant by dialysis, cation exchange chromatography, and again dialysis Laceyella sacchari

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.21.66 262
-
 purified native enzyme, substrate gelatin, pH 9.0, 60°C Laceyella sacchari
3.4.21.66 328
-
 purified native enzyme, substrate N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide, pH 9.0, 60°C Laceyella sacchari
3.4.21.66 340
-
 purified native enzyme, substrate casein, pH 9.0, 60°C Laceyella sacchari

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.66 casein + H2O strong activity Laceyella sacchari ?
-
 ?
3.4.21.66 casein + H2O strong activity Laceyella sacchari LP175 ?
-
 ?
3.4.21.66 Gelatin + H2O strong activity Laceyella sacchari ?
-
 ?
3.4.21.66 Gelatin + H2O strong activity Laceyella sacchari LP175 ?
-
 ?
3.4.21.66 additional information substrate specificity, overview Laceyella sacchari ?
-
 ?
3.4.21.66 additional information the enzyme degrades poly(L-lactide) and is a serine protease Laceyella sacchari ?
-
 ?
3.4.21.66 additional information substrate specificity, overview Laceyella sacchari LP175 ?
-
 ?
3.4.21.66 additional information the enzyme degrades poly(L-lactide) and is a serine protease Laceyella sacchari LP175 ?
-
 ?
3.4.21.66 N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O weak activity Laceyella sacchari ?
-
 ?
3.4.21.66 N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O weak activity Laceyella sacchari LP175 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.66 monomer 1 * 28000, SDS-PAGE Laceyella sacchari

Synonyms

EC Number Synonyms Comment Organism
3.4.21.66 PLLA-degrading enzyme
-
 Laceyella sacchari
3.4.21.66 thermostable serine protease
-
 Laceyella sacchari

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.66 60
-
-
 Laceyella sacchari

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.66 50
-
 purified native enzyme, stable up to Laceyella sacchari

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.66 9
-
-
 Laceyella sacchari

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.21.66 8.5 10.5 purified native enzyme, stable at Laceyella sacchari