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Literature summary extracted from

  • Kotowska, M.; Pawlik, K.; Smulczyk-Krawczyszyn, A.; Bartosz-Bechowski, H.; Kuczek, K.
    Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate (2009), Appl. Environ. Microbiol., 75, 887-896.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.2.20 isopropyl-thio-beta-D-galactoside inducer Streptomyces coelicolor

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.2.20 wild-type ScoT and the H224Y mutant expressed in Escherichia coli BL21(DE3)/pLysS cells. Mutants S90A and S90C expressed in Escherichia coli strain BL21Star(DE3). Mutant H210Y expressed in Escherichia coli BL21Star(DE3) cells additionally transformed with plasmid pGroESL encoding chaperones Streptomyces coelicolor

Protein Variants

EC Number Protein Variants Comment Organism
3.1.2.20 H210Y activity is close to that of the wild-type Streptomyces coelicolor
3.1.2.20 H224Y activity is much lower than that of the wild-type Streptomyces coelicolor
3.1.2.20 S90A completely abolishes the hydrolytic activity of ScoT Streptomyces coelicolor
3.1.2.20 S90C exhibits some residual activity Streptomyces coelicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.2.20 34
-
 N-acetylcysteamine acetate at pH 7.5, 30°C Streptomyces coelicolor
3.1.2.20 52
-
 N-acetylcysteamine propionate at pH 7.5, 30°C Streptomyces coelicolor
3.1.2.20 56
-
 N-acetylcysteamine butyrate at pH 7.5, 30°C Streptomyces coelicolor

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.20 Streptomyces coelicolor
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.20 by nickel affinity chromatography followed by anion-exchange chromatography Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.20 additional information ScoT associated with polyketide synthase Cpk from Streptomyces coelicolor A3 is able to hydrolyze acetyl, propionyl, and butyryl residues. ScoT is an alpha/beta hydrolase with Ser90 and His224 in its active site and it clearly prefers propionate Streptomyces coelicolor ?
-
 ?
3.1.2.20 N-acetylcysteamine acetate
-
 Streptomyces coelicolor N-acetylcysteamine + acetate
-
 ?
3.1.2.20 N-acetylcysteamine butyrate
-
 Streptomyces coelicolor N-acetylcysteamine + butyrate
-
 ?
3.1.2.20 N-acetylcysteamine propionate
-
 Streptomyces coelicolor N-acetylcysteamine + propionate
-
 ?
3.1.2.20 p-nitrophenyl acetate + H2O
-
 Streptomyces coelicolor p-nitrophenol + acetate
-
 ?
3.1.2.20 p-nitrophenyl butyrate
-
 Streptomyces coelicolor p-nitrophenol + butyrate
-
 ?
3.1.2.20 p-nitrophenyl propionate
-
 Streptomyces coelicolor p-nitrophenol + propionate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.2.20 SCOT
-
 Streptomyces coelicolor
3.1.2.20 TE II
-
 Streptomyces coelicolor
3.1.2.20 type II thioesterase
-
 Streptomyces coelicolor

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.2.20 0.9
-
 N-acetylcysteamine propionate at pH 7.5, 30°C Streptomyces coelicolor
3.1.2.20 1.817
-
 N-acetylcysteamine butyrate at pH 7.5, 30°C Streptomyces coelicolor
3.1.2.20 7.5
-
 N-acetylcysteamine acetate at pH 7.5, 30°C Streptomyces coelicolor